DRAVP_ID Sequence Sequence_Length Name Source Uniprot_ID Validation Taxon_ID Gene_Name_ID GenBank Amino acid position Domain_Accession_ID Nucleotide_sequence_ID Molecular_Type Chromosomal position PDB_ID Target_Organism Family Assay Activity Hemolytic_Activity Cytotoxicity_Activity Predicted_structure_ID Structure Linear_Cyclic N-terminal_Modification C-terminal_Modification Other_Modification Stereochemistry Binding_Target Mechanism Mass Formula Absent_amino_acids Common_amino_acids pI Basic_residues Acidic_residues Net_charge Polar_residues Hydrophobic_residues Hydrophobicity Boman_Index Half_Life_Mammalian_ Half_Life__Yeast_ Half_Life__E_coli_ Aliphatic_Index Extinction_Coefficient_cystines Absorbance_280nm Pubmed_ID Reference Author Title Doi Other_link Connectives DRAVPe01811 IFKAIWSGIKSLF 13 Hp1090 Heterometrus petersii "P0DJ02,T1DEJ9" Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae In vitro HCV RNA inhibitory assay [Ref.20950663]Hepatitis C virus (HCV): inhibition of viral infection in Huh7.5.1 cells(IC50 = 7.62 μg/ml (5.0 μM)). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.20950663]the peptide concentration was less than 20 μg/ml, the viability of the peptide-treated cells was greater than 90%." No predicted structure available DRAVPe01811.cif Linear Free Amidation None L membrane Has the ability to prevent the initiation step of HCV infection by direct interaction with HCV virus and readily disrupting their phospholipid membrane. 1509.85 C76H116N16O16 CDEHMNPQRTVY I 10 2 0 2 3 8 107.69 1282 20 hour 30 min >10 hour 127.69 5500 458.33 20950663 Peptides. 2011 Jan;32(1):11-9. "Yan R, Zhao Z, He Y, Wu L, Cai D, Hong W, Wu Y, Cao Z, Zheng C, Li W. " A new natural α-helical peptide from the venom of the scorpion Heterometrus petersii kills HCV. 10.1016/j.peptides.2010.10.008 Anti-HCV DRAVPe01809 FIKRIARLLRKIF 13 Kn2-7 Synthetic construct(derived from BmKn2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase Assay [Ref.22536342]human Immunodeficiency viruses-1(HIV-1): inhibition of viral particle(EC50= 2.76 μg/ml (1.65 μM)). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22536342]TZM-bl cells: CC50 = 38.46 µg/ml. No predicted structure available DRAVPe01809.cif Linear Free Free None L Not found "Kn2-7 aggregates and inserts into viral envelope so that the hydrophobic peptide region aligns with the lipid core region and the hydrophilic peptide regions form the interior region of the pore, with the help of positive charge of peptide somehow" 1674.15 C81H140N24O14 CDEGHMNPQSTVWY IR 12.31 5 0 5 0 8 55.38 -2349 1.1 hour 3 min 2 min 157.69 0 0 22536342 PLoS One. 2012;7(4):e34947. "Chen Y, Cao L, Zhong M, Zhang Y, Han C, Li Q, Yang J, Zhou D, Shi W, He B, Liu F, Yu J, Sun Y, Cao Y, Li Y, Li W, Guo D, Cao Z, Yan H." Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7. 10.1371/journal.pone.0034947 Anti-HIV DRAVPe01808 MITHGCYTRTRHKHKLKKTL 20 SA-35 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Antiviral assay [Ref.32124885]Respiratory syncytial virus (RSV):SA-35 caused a significant decrease of the RSV infectivity by 33 times at concentrations 1 mg/ml. No hemolysis information or data found in the reference(s) presented in this entry [Ref.32124885]MA-104 cells:CC50= 2.1 ± 0.1 mg/ml. No predicted structure available DRAVPe01808.cif Linear Free Free None L Not found It is likely that these peptides exert anti-RSV activity through a combination of two mechanisms: destabilization of the viral envelope and competitive inhibition of attachment/fusion of the virus with the target cell. 2452.97 C107H182N36O26S2 ADEFNPQSVW KT 10.58 9 0 9 7 3 -111 -5711 30 hour >20 hour >10 hour 58.5 1490 78.42 32124885 J Mater Chem B. 2020 Apr 1;8(13):2607-2617 "Kozhikhova KV, Shilovskiy IP, Shatilov AA, Timofeeva AV, Turetskiy EA, Vishniakova LI, Nikolskii AA, Barvinskaya ED, Karthikeyan S, Smirnov VV, Kudlay DA, Andreev SM, Khaitov MR" "Linear and dendrimeric antiviral peptides: design, chemical synthesis and activity against human respiratory syncytial virus." 10.1039/c9tb02485a Anti-RSV DRAVPe01807 KRRGGGKLLKLLLKLLLKLLKC 22 NC-783 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Antiviral assay [Ref.32124885]Respiratory syncytial virus (RSV):inhibition of viral infection in the MA-104 cell(IC50=0.04mg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.32124885]MA-104 cells:CC50= 0.04 ± 0.01 mg/ml. No predicted structure available DRAVPe01807.cif Linear Free Free None L Not found It is likely that these peptides exert anti-RSV activity through a combination of two mechanisms: destabilization of the viral envelope and competitive inhibition of attachment/fusion of the virus with the target cell. 2505.32 C117H222N34O23S ADEFHIMNPQSTVWY L 11.27 8 0 8 4 10 31.36 -984 1.3 hour 3 min 2 min 177.27 0 0 32124885 J Mater Chem B. 2020 Apr 1;8(13):2607-2617 "Kozhikhova KV, Shilovskiy IP, Shatilov AA, Timofeeva AV, Turetskiy EA, Vishniakova LI, Nikolskii AA, Barvinskaya ED, Karthikeyan S, Smirnov VV, Kudlay DA, Andreev SM, Khaitov MR" "Linear and dendrimeric antiviral peptides: design, chemical synthesis and activity against human respiratory syncytial virus." 10.1039/c9tb02485a Anti-RSV DRAVPe01806 gikefkrivqrikdflrnlv 20 GI-20D Synthetic construct(derived from LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Plaque assay [Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=0.99 µM);inhibition of viral infection in primary macrophages(IC50=2.2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01806.cif Linear Free Amidation None D Not found "Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry." 2473.01 H-38O-19 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 11 0 0 0 0 0 0 0 0 0 0 32252021 iScience. 2020 Apr 24;23(4):100999. "Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K." Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. 10.1016/j.isci.2020.100999 Anti-EBOV DRAVPe01805 GXKRlVQRlKDXlRNLV 17 17BIPHE2 Synthetic construct(derived from LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Plaque assay [Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=0.71 µM);inhibition of viral infection in primary macrophages(IC50=5.6 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01805.cif Linear Free Amidation The 'X' at position 2 and 12 indicates biphenylalanine. "Mixed(D-Leu5, 9, 13)" Not found "Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry." 2030.86 C61H103N25O12 ACEFHIMPSTWY R 11.72 5 1 4 2 3 -117.65 -6282 30 hour >20 hour >10 hour 57.06 0 0 32252021 iScience. 2020 Apr 24;23(4):100999. "Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K." Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. 10.1016/j.isci.2020.100999 Anti-EBOV DRAVPe01803 RGAHINGRWDSRCHRF 16 FBP1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Plaque reduction assay [Ref.35259078]influenza A virus(H1N1): inhibition of viral multicycle growth in MDCK cells(>50% inhibition at 100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01803.cif Linear Free Free None L HA FBP could have dual functions: blocked HA-mediated fusion by binding and inhibited endosomal acidification from interfering viral entry by the endocytic pathway. 1968.19 C83H126N34O21S EKLMPQTVY R 11.52 6 1 5 5 4 -139.38 -7256 1 hour 2 min 2 min 30.63 5500 366.67 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. " 10.1080/22221751.2022.2051753 Anti-Anti-Influenza A virus DRAVPe01804 RGAHIKGRWDSRCHRF 16 FBP2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Plaque reduction assay [Ref.35259078]influenza A virus(H1N1): inhibition of viral multicycle growth in MDCK cells(>50% inhibition at 50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01804.cif Linear Free Free None L HA FBP could have dual functions: blocked HA-mediated fusion by binding and inhibited endosomal acidification from interfering viral entry by the endocytic pathway. 1982.26 C85H132N34O20S ELMNPQTVY R 11.54 7 1 6 4 4 -141.88 -7147 1 hour 2 min 2 min 30.63 5500 366.67 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. " 10.1080/22221751.2022.2051753 Anti-Anti-Influenza A virus DRAVPe01802 RGAHIKGRWKSRCHRF 16 FBP Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "Influenza A virus, Influenza B virus, SARS-CoV-2" "Orthomyxoviridae, Coronaviridae" Plaque reduction assay [Ref.35259078]influenza A virus(H1N1): inhibition of viral multicycle growth in MDCK cells(IC50=3.9 μg/ml);##influenza A virus(H3N2): inhibition of viral replication in MDCK cells(IC50=1.6 μg/ml);##influenza B virus: inhibition of viral replication in MDCK cells(IC50=7.1 μg/ml);##SARS-CoV-2 HKU001a: inhibition of viral replication in Vero E6 cells(IC50=2.9 μg/ml);##SARS-CoV-2 B.1.1.63: inhibition of viral replication in Vero E6 cells(IC50=3.0 μg/ml);##SARS-CoV-2 Delta: inhibition of viral replication in Vero E6 cells(IC50=3.9 μg/ml). [Ref.35259078]No significant haemolysis was observed when Turkey red blood cells (RBC) were treated with FBP. [Ref.35259078]no significant cytotoxicity was detected in MDCK cells treated with 1 mg/ml of FBP. No predicted structure available DRAVPe01802.cif Linear Free Free None L HA FBP could have dual functions: blocked HA-mediated fusion by binding and inhibited endosomal acidification from interfering viral entry by the endocytic pathway.the notable antiviral activity and fusion inhibition activity of FBP on SARS-CoV-2 could be attributed to the inhibition of FBP on endosomal acidification 1995.34 C87H139N35O18S DELMNPQTVY R 12.01 8 0 8 4 4 -144.38 -6830 1 hour 2 min 2 min 30.63 5500 366.67 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. " 10.1080/22221751.2022.2051753 "Anti-Anti-Influenza A virus, Anti-Influenza B virus, Anti-SARS-CoV-2" DRAVPe01801 IPLRGAFINGRWDSQCHRFS 20 U5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Plaque reduction assay [Ref.35259078]influenza A virus(H1N1): inhibition of viral replication in MDCK cells(IC50=12.9 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01801.cif Linear Free Free None L HA Bind to the HA stem of group 1 influenza A virus. 2360.68 C105H158N34O27S EKMTVY R 10.26 4 1 3 6 7 -47 -4910 20 hour 30 min >10 hour 63.5 5500 289.47 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. " 10.1080/22221751.2022.2051753 Anti-Anti-Influenza A virus DRAVPe01800 FINGRWDSQCHRFSNGAIACA 21 U4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Plaque reduction assay [Ref.35259078]influenza A virus(H1N1): inhibition of viral replication in MDCK cells(IC50=6.6 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01800.cif Linear Free Free None L HA Bind to the HA stem of group 1 influenza A virus. 2353.62 C101H149N33O29S2 EKLMPTVY A 8.08 3 1 2 8 8 -21.43 -4084 1.1 hour 3 min 2 min 51.43 5625 281.25 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. " 10.1080/22221751.2022.2051753 Anti-Anti-Influenza A virus DRAVPe01799 WEDWVR 6 C6b Synthetic construct(derived from gp36 membrane proximal external region of FIV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01799.cif Linear Free Free None L membrane Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. 889.97 C42H55N11O11 ACFGHIKLMNPQSTY W 4.37 1 2 -1 0 3 -151.67 -2175 2.8 hour 3 min 2 min 48.33 11000 2200 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 "Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM." Structural basis of antiviral activity of peptides from MPER of FIV gp36 10.1371/journal.pone.0204042 Anti-FIV DRAVPe01798 DWVRWI 6 C6a Synthetic construct(derived from gp36 membrane proximal external region of FIV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50=0.06-0.15 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01798.cif Linear Free Free None L membrane Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. 874.01 C43H59N11O9 ACEFGHKLMNPQSTY W 5.84 1 1 0 0 4 -18.33 -1002 1.1 hour 3 min >10 hour 113.33 11000 2200 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 "Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM." Structural basis of antiviral activity of peptides from MPER of FIV gp36 10.1371/journal.pone.0204042 Anti-FIV DRAVPe01797 WEDWVRWI 8 C8 Synthetic construct(derived from gp36 membrane proximal external region of FIV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50=0.05-0.06 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01797.cif Linear Free Free None L membrane Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. 1189.34 C59H76N14O13 ACFGHKLMNPQSTY W 4.37 1 2 -1 0 5 -68.75 -1450 2.8 hour 3 min 2 min 85 16500 2357.14 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 "Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM." Structural basis of antiviral activity of peptides from MPER of FIV gp36 10.1371/journal.pone.0204042 Anti-FIV DRAVPe01796 XGSGSGVALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSI 42 Chol-PEG4-VG Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.1 ± 0.0001 nM,IC50<0.0007 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50>10000 nM. No predicted structure available DRAVPe01796.cif Linear Acetylation Amidation The 'X' at position 1 indicates cholesterol-PEG4 conjugated cysteine. L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4510.27 C190H316N54O64 CFHMQTY S 5.05 6 7 -1 13 14 -38.33 -8236 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01795 XGSGSGVALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSI 42 Chol-VG Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=1.7 ± 0.42 nM,IC50=0.06 ± 0.035 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50=9000 nM. No predicted structure available DRAVPe01795.cif Linear Acetylation Amidation The 'X' at position 1 indicates cholesterol-conjugated cysteine. L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4510.27 C190H316N54O64 CFHMQTY S 5.05 6 7 -1 13 14 -38.33 -8236 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01794 VALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-PEG24-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.1 ± 0.0003 nM,IC50=0.007 ± 0.007 nM);##Nipah virus(NiV):inhibition of virus infection in Vero cells(IC90~2 nM." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50=1300 nM. No predicted structure available DRAVPe01794.cif Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-PEG24 conjugated cysteine. L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4510.27 C190H316N54O64 CFHMQTY S 5.05 6 7 -1 13 14 -38.33 -8236 100 hour >20 hour >10 hour 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01792 VALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.7 ± 0.26 nM,IC50=0.015 ± 0.07 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50+10000 nM. No predicted structure available DRAVPe01792.cif Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-conjugated cysteine. L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4510.27 C190H316N54O64 CFHMQTY S 5.05 6 7 -1 13 14 -38.33 -8236 100 hour >20 hour >10 hour 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01793 VALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-PEG4-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.7 ± 0.007 nM,IC50=0.03 ± 0.04 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50=4500 nM. No predicted structure available DRAVPe01793.cif Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-PEG4 conjugated cysteine. L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4510.27 C190H316N54O64 CFHMQTY S 5.05 6 7 -1 13 14 -38.33 -8236 100 hour >20 hour >10 hour 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01791 VALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGC 42 VG Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV 3 Paramyxoviridae Plaque reduction assay "[Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=280 ± 247 nM,IC50=1 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.28344321]Vero cells: CC50>10000 nM. No predicted structure available DRAVPe01791.cif Linear Acetylation Amidation None L membrane "Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion." 4502.08 C193H323N55O66S FHMQTY S 5.05 6 7 -1 14 14 -32.38 -8108 100 hour >20 hour >10 hour 102.14 5500 134.15 28344321 Sci Rep. 2017 Mar 8;7:43610. "Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A" Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides 10.1038/srep43610 Anti-HPIV 3 DRAVPe01790 SKVNGQSGRMEFFWTIAK 18 m15 /Leu17 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01790.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2086.4 C94H144N26O26S CDHLPY FGKS 9.99 3 1 2 6 6 -48.89 -3109 1.9 hour >20 hour >10 hour 43.33 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01789 SKVNGQSGRMEFFWTALK 18 m14 /lle16 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>10% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01789.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2086.4 C94H144N26O26S CDHIPY FGKS 9.99 3 1 2 6 6 -52.78 -3109 1.9 hour >20 hour >10 hour 43.33 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01787 SKVNGQSGRMAFFWTILK 18 m9 /Glu11 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>50% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01787.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2070.44 C95H148N26O24S CDEHPY FGKS 11.17 3 0 3 6 7 -8.33 -1936 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01788 SKVNGQSGRMEFAWTILK 18 m11 /Phe13 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>80% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01788.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2052.38 C91H146N26O26S CDHPY GKS 9.99 3 1 2 6 6 -43.33 -2915 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01786 SKVNGQSGRAEFFWTILK 18 m8 /Met10 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>80% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01786.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2068.36 C95H146N26O26 CDHMPY FGKS 9.99 3 1 2 6 7 -38.33 -2852 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01785 SKVNGQAGRMEFFWTILK 18 m6 /Ser7 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(~60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01785.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2112.48 C97H150N26O25S CDHPY FGK 9.99 3 1 2 5 7 -23.33 -2277 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01784 SKVNGASGRMEFFWTILK 18 m5 /GIn6 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01784.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2071.42 C95H147N25O25S CDHPQY FGKS 9.99 3 1 2 6 7 -8.33 -2063 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01783 SKVAGQSGRMEFFWTILK 18 m4 /Asn4 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>70% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01783.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2085.45 C96H149N25O25S CDHNPY FGKS 9.99 3 1 2 5 7 -8.33 -1953 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01782 SKANGQSGRMEFFWTILK 18 m3 /Val3 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>50% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01782.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2100.42 C95H146N26O26S CDHPVY FGKS 9.99 3 1 2 6 6 -51.11 -3021 1.9 hour >20 hour >10 hour 48.89 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01781 SAVNGQSGRMEFFWTILK 18 m2 /Arg2 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(~20% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01781.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2071.38 C94H143N25O26S CDHPY FGS 8.46 2 1 1 6 7 -6.11 -2062 1.9 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01780 AKVNGQSGRMEFFWTILK 18 m1 /Ser1 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>20% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01780.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2112.48 C97H150N26O25S CDHPY FGK 9.99 3 1 2 5 7 -23.33 -2277 4.4 hour >20 hour >10 hour 65 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Anti-Influenza A virus DRAVPe01779 PxTXXLPX 8 "Plitidepsin, Aplidine" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae antiviral assay "[Ref.33495306]SARS-CoV-2:inhibition of replication In Vero E6 cells(IC50=0.70 nM,IC90=1.76 nM);inhibition of replication In hACE2-HEK293T cells(IC50=0.73 nM,IC90=0.88 nM);inhibition of replication In pneumocyte-like cells(IC50=1.62 nM,IC90=3.14 nM).##[Ref.35231500]SARS-CoV-2 D614G:inhibition of replication in Vero E6 cells(IC50=5.2 nM);##SARS-CoV-2 Delta:inhibition of replication in Vero E6 cells(IC50=3.9 nM);##SARS-CoV-2 Omicron:inhibition of replication in Vero E6 cells(IC50=4.3 nM)." No hemolysis information or data found in the reference(s) presented in this entry "[Ref.33495306]Vero E6 cells:CC10=0.36 nM,CC50=1.99 nM;hACE2-293T cells:CC10=2.00 nM,CC50>200 nM;pneumocyte-like cells:CC10=20.88 nM,CC50=65.43 nM." No predicted structure available DRAVPe01779.cif Linear Pyruvoyl Free "The 'X' at position 2 is N-methylleucine,position 4 is 4-amino-3-hydroxy-5-methyl-Heptanoic acid, position 5 is Hydroxyisovalerylpropionyl, and position 8 is N-methyl-4-methyl-tyrosine.There is a Sidechain-Mainchain Bond between position 3 and 8." Mixed(D-meth-Leu2) Not found The antiviral activity of plitidepsin against SARS-CoV-2 is mediated through inhibition of the known target eEF1A (eukaryotic translation elongation factor 1A). 871.84 C20H26N4O2 ACDEFGHIKMNQRSVWY X 5.96 0 0 0 1 1 -1.25 235 >20 hour >20 hour ? 48.75 0 0 35231500##33495306 Antiviral Res. 2022 Apr;200:105270.##Science. 2021 Feb 26;371(6532):926-931. "Sachse M, Tenorio R, Fernández de Castro I, Muñoz-Basagoiti J, Perez-Zsolt D, Raïch-Regué D, Rodon J, Losada A, Avilés P, Cuevas C, Paredes R, Segalés J, Clotet B, Vergara-Alert J, Izquierdo-Useros N, Risco C.##White KM, Rosales R, Yildiz S, Kehrer T, Miorin L, Moreno E, Jangra S, Uccellini MB, Rathnasinghe R, Coughlan L, Martinez-Romero C, Batra J, Rojc A, Bouhaddou M, Fabius JM, Obernier K, Dejosez M, Guillén MJ, Losada A, Avilés P, Schotsaert M, Zwaka T, Vignuzzi M, Shokat KM, Krogan NJ, Garc" Unraveling the antiviral activity of plitidepsin against SARS-CoV-2 by subcellular and morphological analysis.##Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by targeting the host protein eEF1A. 10.1016/j.antiviral.2022.105270##10.1126/science.abf4058 Anti-SARS-CoV-2 DRAVPe01778 XxXVXAaXXXX 11 "Alisporivir, Debio-025" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae plaque assay "[Ref.32376613]SARS-CoV-2:Inhibition of infection in Vero E6 cells(EC50=0.46±0.04 µM,E90=3.10±1.40 μM).##[Ref.32568027]SARS-CoV-2:Inhibition of infection in Vero E6 cells(EC50=4.9±1.3 µM);##SARS-CoV:Inhibition of infection in Vero E6 cells(EC50=4.3±1.0 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.32376613]Vero E6 cells:CC50>20µM. No predicted structure available DRAVPe01778.cif Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 1 is alpha-aminobutyric acid,position 2 is N-methylalanine,the 'V' at position 3 is N-methylalanine,the 'X' at position 5,8,9 are N-methylleucine,the 'X' at position 10 is N-methylvaline and position 11 is N-methyl-(4R)-4-[(E)-but-2-enyl]-4-methyl-L-threonyl" "Mixed(D-Ala7,D-meth-Ala2)" Not found Comment: No comments found on DRAMP database 0 C8H-2N2O-6 CDEFGHIKLMNPQRSTWY X 0 0 0 0 0 2 54.55 585 35.45 0 0 32376613##32568027 Antimicrob Agents Chemother. 2020 Jun 23;64(7):e00876-20. ##J Gen Virol. 2020 Sep;101(9):925-940. "Softic L, Brillet R, Berry F, Ahnou N, Nevers Q, Morin-Dewaele M, Hamadat S, Bruscella P, Fourati S, Pawlotsky JM, Ahmed-Belkacem A.##Ogando NS, Dalebout TJ, Zevenhoven-Dobbe JC, Limpens RWAL, van der Meer Y, Caly L, Druce J, de Vries JJC, Kikkert M, Bárcena M, Sidorov I, Snijder EJ." "Inhibition of SARS-CoV-2 Infection by the Cyclophilin Inhibitor Alisporivir (Debio 025).##SARS-coronavirus-2 replication in Vero E6 cells: replication kinetics, rapid adaptation and cytopathology." 10.1128/AAC.00876-20##10.1099/jgv.0.001453 Anti-SARS-CoV-2 DRAVPe01777 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 P3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Neutralizing assay [Ref.32482145]HCoV-19:inhibition of HCoV-19 S mediated cell–cell fusion(EC50=0.72 μM);neutralizing activities against pseudotype HCoV-19 virus(EC50=0.32 μM);inhibition of authentic HCoV-19 virus infection in Vero E6 cells(EC50=0.58 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01777.cif Linear Free Free None L Not found Comment: No comments found on DRAMP database 3893.41 C168H287N47O58 CFHMPTWY ILN 4.36 3 6 -3 9 15 -8.29 -5930 20 hour 30 min >10 hour 142 0 0 32482145 Emerg Microbes Infect. 2020 Dec;9(1):1238-1241. "Sun H, Li Y, Liu P, Qiao C, Wang X, Wu L, Liu K, Hu Y, Su C, Tan S, Zou S, Wu G, Yan J, Gao GF, Qi J, Wang Q. " Structural basis of HCoV-19 fusion core and an effective inhibition peptide against virus entry. 10.1080/22221751.2020.1770631 Anti-SARS-CoV-2 DRAVPe01776 RGAHIKGRWKSRCHRF 16 FBP Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Plaque reduction assay "[Ref.35259078]A(H1N1)(IC50 = 3.9 μg/ml);A(H3N2)(IC50 = 1.6 μg/ml);FluB (IC50 = 7.1 μg/ml);##SARS-CoV-2 (HKU001a):inhibition of infection in Vero-E6 cells(IC50=2.9 μg/ml);##SARS-CoV-2 (B.1.1.63, D614G):inhibition of infection in Vero-E6 cells(IC50=3.0 μg/ml);##SARS-CoV-2(Delta):inhibition of infection in Vera-E6 cells(IC50=3.9 μg/ml)." [Ref.35259078]No significant hemolysis against Turkey red blood cells (RBC). [Ref.35259078]No significant cytotoxicity was detected in MDCK(Madin Darby canine kidney) cells at 1 mg/ml(TC50 > 1 mg/ml). No predicted structure available DRAVPe01776.cif Linear Free Free None L membrane The fusion-inhibition peptide FBP could broadly inhibit influenza virus and SARS-CoV-2 by interfering the viral fusion by the endocytic pathway and showed potently antiviral activity against the influenza virus in mice and SARS-CoV-2 variants in hamsters. 1995.34 C87H139N35O18S DELMNPQTVY R 12.01 8 0 8 4 4 -144.38 -6830 1 hour 2 min 2 min 30.63 5500 366.67 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. "Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY." "Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants." 10.1080/22221751.2022.2051753 Anti-SARS-CoV-2 DRAVPe01775 SALEEQYKTFLDKFMHELEDLLYQLAL 27 P10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae plaque assay [Ref.33580154]SARS-CoV-2:95% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=42 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. No predicted structure available DRAVPe01775.cif Linear Free Amidation None L Not found "The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein." 3288.76 C152H231N33O46S CGINPRVW L 4.35 3 6 -3 4 11 -20 -3140 1.9 hour >20 hour >10 hour 108.52 2980 114.62 33580154 Commun Biol. 2021 Feb 12;4(1):197. "Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O." Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. 10.1038/s42003-021-01736-8 Anti-SARS-CoV-2 DRAVPe01774 SALEEQYKTFLDKFMHELEDLLYQLSL 27 P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae plaque assay [Ref.33580154]SARS-CoV-2:93% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=53 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. No predicted structure available DRAVPe01774.cif Linear Free Amidation None L Not found "The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein." 3304.76 C152H231N33O47S CGINPRVW L 4.35 3 6 -3 5 10 -29.63 -3661 1.9 hour >20 hour >10 hour 104.81 2980 114.62 33580154 Commun Biol. 2021 Feb 12;4(1):197. "Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O." Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. 10.1038/s42003-021-01736-8 Anti-SARS-CoV-2 DRAVPe01773 SALEEQLKTFLDKFMHELEDLLYQLAL 27 P8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae plaque assay [Ref.33580154]SARS-CoV-2:91% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=46 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. No predicted structure available DRAVPe01773.cif Linear Free Amidation None L Not found "The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein." 3238.74 C149H233N33O45S CGINPRVW L 4.35 3 6 -3 3 12 -1.11 -2634 1.9 hour >20 hour >10 hour 122.96 1490 57.31 33580154 Commun Biol. 2021 Feb 12;4(1):197. "Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O." Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. 10.1038/s42003-021-01736-8 Anti-SARS-CoV-2 DRAVPe01772 SALEEQYKTFLDKFLHELEDLLYQLALAL 29 P7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae plaque assay [Ref.33580154]SARS-CoV-2:54% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50>1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01772.cif Linear Free Amidation None L Not found "The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein." 3454.96 C162H249N35O48 CGIMNPRVW L 4.35 3 6 -3 4 14 7.24 -2210 1.9 hour >20 hour >10 hour 131.38 2980 106.43 33580154 Commun Biol. 2021 Feb 12;4(1):197. "Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O." Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. 10.1038/s42003-021-01736-8 Anti-SARS-CoV-2 DRAVPe01771 RFDGKGLGIYQYMEEIEHAASRFAYFFYQHLA 32 Covid_extented_1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae virus neutralization assay [Ref.34624194]SARS-CoV-2:inhibition of infection in Vero cells(IC50=5.76 ± 1.65 μM);##SARS-CoV-2 variants B.1.1.7:inhibition of infection in Vero cells(IC50=5.57 ± 4.04 μM);##SARS-CoV-2 variants B.1.351:inhibition of infection in Vero cells(IC50=7.37 ± 1.80 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01771.cif Linear Acylation Amidation None D Not found The peptide acts as an inhibitor of the RBD–ACE2 interaction 3859.33 C181H253N45O48S CNPTVW AFY 6.03 5 4 1 8 12 -33.13 -4489 1 hour 2 min 2 min 61.25 5960 192.26 34624194 J Med Chem. 2021 Oct 28;64(20):14955-14967. "Valiente PA, Wen H, Nim S, Lee J, Kim HJ, Kim J, Perez-Riba A, Paudel YP, Hwang I, Kim KD, Kim S, Kim PM. " Computational Design of Potent D-Peptide Inhibitors of SARS-CoV-2. 10.1021/acs.jmedchem.1c00655 Anti-SARS-CoV-2 DRAVPe01770 LQTALYALMEEIHIAALEKTWTALRHQYT 29 Covid3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae virus neutralization assay [Ref.34624194]SARS-CoV-2:inhibition of infection in Vero cells(IC50=6.56 ± 2.14 μM);##SARS-CoV-2 variants B.1.1.7:inhibition of infection in Vero cells(IC50=33.40 ± 10.75 μM);##SARS-CoV-2 variants B.1.351:inhibition of infection in Vero cells(IC50=11.13 ± 3.82 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01770.cif Linear Acylation Amidation None D Not found The peptide acts as an inhibitor of the RBD–ACE2 interaction 3415.95 C156H244N40O44S CDFGNPSV AL 6.02 4 3 1 6 13 1.03 -2369 5.5 hour 3 min 2 min 111.38 8480 302.86 34624194 J Med Chem. 2021 Oct 28;64(20):14955-14967. "Valiente PA, Wen H, Nim S, Lee J, Kim HJ, Kim J, Perez-Riba A, Paudel YP, Hwang I, Kim KD, Kim S, Kim PM. " Computational Design of Potent D-Peptide Inhibitors of SARS-CoV-2. 10.1021/acs.jmedchem.1c00655 Anti-SARS-CoV-2 DRAVPe01769 RVKR 4 CMK Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Plaque assay "[Ref.33007239]SARS-CoV-2:inhibition of virus production in Vero E6 cells(IC50=0.057 µM).##[Ref.31683742]Virus:Zika virus (ZIKV):inhibition of virus release in Vero cells(IC50=18.59 µM);Japanese encephalitis virus (JEV):inhibition of virus release in BHK-21 cells(IC50=19.91 µM).##[Ref.23617302]Hepatitis B virus (HBV):Inhibition of HBeAg secretion in HepG2.2.15 cells(26±11% inhibition at 20 µM,21±13% Inhibition at 100 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.31683742]Vero cells:CC50=712.9 µM.##[Ref.33007239]Vero E6 cells:IC50=318.2 µM. No predicted structure available DRAVPe01769.cif Linear Decanoyl(C10) chloromethylketone(CMK) None L Not found "CMK blocks virus entry, but it further suppresses cleavage of spikes and the syncytium." 557.7 C23H47N11O5 ACDEFGHILMNPQSTWY R 12.01 3 0 3 0 1 -217.5 -3135 1 hour 2 min 2 min 72.5 0 0 23617302##31683742##33007239 Liver Int. 2013 Sep;33(8):1230-8. ##Viruses. 2019 Oct 31;11(11):1011.##Cell Rep. 2020 Oct 13;33(2):108254. "Pang YJ, Tan XJ, Li DM, Zheng ZH, Lei RX, Peng XM.##Imran M, Saleemi MK, Chen Z, Wang X, Zhou D, Li Y, Zhao Z, Zheng B, Li Q, Cao S, Ye J.##Cheng YW, Chao TL, Li CL, Chiu MF, Kao HC, Wang SH, Pang YH, Lin CH, Tsai YM, Lee WH, Tao MH, Ho TC, Wu PY, Jang LT, Chen PJ, Chang SY, Yeh SH." Therapeutic potential of furin inhibitors for the chronic infection of hepatitis B virus.##Decanoyl-Arg-Val-Lys-Arg-Chloromethylketone: An Antiviral Compound That Acts against Flaviviruses through the Inhibition of Furin-Mediated prM Cleavage.##Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects. 10.1111/liv.12185##10.3390/v11111011##10.1016/j.celrep.2020.108254 Anti-SARS-CoV-2 DRAVPe01768 PHSCN 5 ATN-161 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae ELISA [Ref.33102950]SARS-CoV-2:inhibition of virus replication In VeroE6 cells(IC50=3.16 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01768.cif Linear Acylation Amidation None L Not found The peptide inhibits the spike protein interaction with α5β1 integrin and the interaction between α5β1 integrin and ACE2. 556.59 C21H32N8O8S ADEFGIKLMQRTVWY CHNPS 7.12 1 0 1 3 0 -132 -1342 >20 hour >20 hour ? 0 0 0 33102950 JACC Basic Transl Sci. 2021 Jan;6(1):1-8. "Beddingfield BJ, Iwanaga N, Chapagain PP, Zheng W, Roy CJ, Hu TY, Kolls JK, Bix GJ." "The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2 Infection." 10.1016/j.jacbts.2020.10.003 Anti-SARS-CoV-2 DRAVPe01767 ANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQ 42 SARS-CoV-2 HR1P Synthetic construct P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae Cell-cell fusion assay "[Ref.32047258]SARS-CoV-2(No inhibition of cell-cell fusion up to 40 µM in Huh-7 cells,No inhibition of infection up to 40 µM in 293T/ACE2 cells)" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01767.cif Linear Free Free None L Not found The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. 4386.89 C187H314N56O65 CEHMPRWY AQ 8.54 3 2 1 14 17 -21.9 -6039 4.4 hour >20 hour >10 hour 100 0 0 32047258 Cell Mol Immunol. 2020 Jul;17(7):765-767. "Xia S, Zhu Y, Liu M, Lan Q, Xu W, Wu Y, Ying T, Liu S, Shi Z, Jiang S, Lu L." Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. 10.1038/s41423-020-0374-2 Anti-SARS-CoV-2 DRAVPe01766 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSGC 42 EK1-GSGSGC Synthetic construct Q8BB25 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae "Cell-cell fusion assay,infectivity assay" "[Ref.33082259]SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50=293±60 nM,IC90>900 nM),inhibition of infection in Vero E6 cells(IC50~ 41 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=261±136 nM,IC90=892±100 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50=286±104 nM,IC90>1000 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50=194±107 nM,IC90=893±77 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50>1000 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 2 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=36±5 nM,IC90>1000 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.33082259]Human embryonic kidney HEK293T cells:<5% Cytotoxicity at 10 µM;Vero E6 cells:18% Cytotoxicity at 10 µM. No predicted structure available DRAVPe01766.cif Linear Free Free None L membrane The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. 4780.43 C211H341N49O72S2 HPRW EL 4.36 5 10 -5 12 13 -37.86 -6573 1.9 hour >20 hour >10 hour 102.14 2980 72.68 33082259 mBio. 2020 Oct 20;11(5):e01935-20. "Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M." Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain. 10.1128/mBio.01935-20 Anti-SARS-CoV-2 DRAVPe01765 SLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGSGSGC 42 MERS-CoV-HR2P-GSGSGC Synthetic construct "R9UQ53,K9N5Q8" Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "Cell-cell fusion assay,infectivity assay" "[Ref.33082259]SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50>650 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 36 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=1000 nM,IC90>1000 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50>1000,IC90>1000 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50>700 nM,IC90>1000 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50=417±180 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 4 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=40±34 nM,IC90>700 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.33082259]Human embryonic kidney HEK293T cells:<10% Cytotoxicity at 10 µM;Vero E6 cells:12% Cytotoxicity at 10 µM. No predicted structure available DRAVPe01765.cif Linear Free Free None L membrane The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. 4590.23 C200H331N49O69S2 FHPRW L 4.18 2 5 -3 17 14 10.48 -3597 1.9 hour >20 hour >10 hour 118.33 2980 72.68 33082259 mBio. 2020 Oct 20;11(5):e01935-20. "Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M." Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain. 10.1128/mBio.01935-20 Anti-SARS-CoV-2 DRAVPe01764 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSGSGC 42 SARS-CoV-2-S(1168–1203)-GSGSGC Synthetic construct P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "Cell-cell fusion assay,infectivity assay" "[Ref.33082259]SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50=10±8 nM,IC90=98±57 nM),inhibition of infection in Vero E6 cells(IC50~ 6 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=8±4 nM,IC90=96±50 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50=6±4 nM,IC90=75±42 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50=9±7 nM,IC90=78±59 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50=35±10 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 3 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=7±5 nM,IC90=43±6 nM)." No hemolysis information or data found in the reference(s) presented in this entry "[Ref.33082259]Human embryonic kidney HEK293T cells:18% Cytotoxicity at 10 µM;Vero E6 cells:12% Cytotoxicity at 1 µM,30% Cytotoxicity at 10 µM;Human airway epithelial cells:25% Cytotoxicity at 1 µM." No predicted structure available DRAVPe01764.cif Linear Free Free None L membrane The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. 4456.95 C187H316N54O69S FHMPTWY ILNS 4.2 3 7 -4 15 15 -15.95 -7072 1.1 hour 3 min >10 hour 118.33 0 0 33082259##33597220 mBio. 2020 Oct 20;11(5):e01935-20.##Science. 2021 Mar 26;371(6536):1379-1382. "Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M.##de Vries RD, Schmitz KS, Bovier FT, Predella C, Khao J, Noack D, Haagmans BL, Herfst S, Stearns KN, Drew-Bear J, Biswas S, Rockx B, McGill G, Dorrello NV, Gellman SH, Alabi CA, de Swart RL, Moscona A, Porotto M." Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain.##Intranasal fusion inhibitory lipopeptide prevents direct-contact SARS-CoV-2 transmission in ferrets. 10.1128/mBio.01935-20##10.1126/science.abf4896 Anti-SARS-CoV-2 DRAVPe01763 NGAICWGPCPTAFRQIGNCGRFRVRCCRIR 30 8P9R(branched P9R) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Plaque reduction assay [Ref.33750821]SARS-CoV-2:inhibition of replication in high salt condition(IC50 = 0.3 μg/ml) [Ref.33750821]No obvious hemolysis was observed when turkey red blood cells were treated at 200 μg/ml. [Ref.33750821]Vero-E6 cells:the cytotoxicity indicated that TC50 of 8P9R was higher than 200 μg/ml. No predicted structure available DRAVPe01763.cif Branched Free Free None L Not found Have dual-antiviral mechanisms of cross-linking viruses to stop viral entry (mediated by TMPRSS2 for SARS-CoV-2) and of reducing endosomal acidification to inhibit viral entry through endocytic pathway. 3412.05 C144H232N52O35S5 DEHKLMSY R 10.46 6 0 6 12 9 -15 -7004 1.4 hour 3 min >10 hour 55.33 5750 198.28 33750821 Nat Commun. 2021 Mar 9;12(1):1517. "Zhao H, To KKW, Lam H, Zhou X, Chan JF, Peng Z, Lee ACY, Cai J, Chan WM, Ip JD, Chan CC, Yeung ML, Zhang AJ, Chu AWH, Jiang S, Yuen KY." Cross-linking peptide and repurposed drugs inhibit both entry pathways of SARS-CoV-2. 10.1038/s41467-021-21825-w Anti-SARS-CoV-2 DRAVPe01762 NGAICWGPCPTAFRQIGNCGRFRVRCCRIR 30 "MBD-4 (11-40) (P9 [H21R,K23R,K28R], P9R)" Synthetic construct P82019 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 6M56 SARS-CoV-2 Coronaviridae Plaque reduction assay [Ref.32843628]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=0.9 µg/ml);##SARS-CoV:Inhibition of infection in Vero E6 cells(IC50=4.2 µg/ml);##MERS-CoV:Inhibition of infection in Vero E6 cells(IC50=22 µg/ml);##Human rhinovirus (HRV):inhibition of infection in RD cells(IC50=5.7 µg/ml);##Human parainfluenza virus 3:Inhibition of infection in LLC-MK2 cells(IC50>25 µg/ml);##Human Influenza A Virus H1N1:Inhibition of infection In MDCK cells(IC50=0.6 µg/ml);##Human Influenza A Virus H7N9:Inhibition of infection In MDCK cells(IC50=0.9 µg/ml). [Ref.32843628]P9R did not cause the hemolysis of Chicken red blood cells. "[Ref.32843628]The CC50 of P9R was >300 μg/ml for MDCK, VeroE6 and A549 cells." No predicted structure available DRAVPe01762.cif Linear Free Free None L Not found Mechanistic studies show that positively charged P9R broadly inhibits viral replication by binding to different viruses and then inhibits virus–host endosomal acidification to prevent the endosomal release of pH-dependent viruses. 3412.05 C144H232N52O35S5 DEHKLMSY R 10.46 6 0 6 12 9 -15 -7004 1.4 hour 3 min >10 hour 55.33 5750 198.28 32843628 Nat Commun. 2020 Aug 25;11(1):4252. "Zhao H, To KKW, Sze KH, Yung TT, Bian M, Lam H, Yeung ML, Li C, Chu H, Yuen KY." A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2. 10.1038/s41467-020-17986-9 Anti-SARS-CoV-2 DRAVPe01761 NGAICWGPCPTAFRQIGNCGHFKVRCCKIR 30 MBD-4 (11-40)(P9) Synthetic construct P82019 Experimentally Validated 10090 Defb4 AF155882.2 Not available pfam00711 AF155882 mRNA "Chromosome 8, Location: NC_000074.7 (19213172..19245342)" 6M56 SARS-CoV-2 Coronaviridae Plaque reduction assay [Ref.32843628]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=2.4 µg/ml);##SARS-CoV:Inhibition of infection in Vero E6 cells(IC50=6.2 µg/ml);##MERS-CoV:Inhibition of infection in Vero E6 cells(IC50=8.8 µg/ml);##Human rhinovirus (HRV):inhibition of infection in RD cells(IC50=34 µg/ml);##Human parainfluenza virus 3:Inhibition of infection in LLC-MK2 cells(IC50>25 µg/ml);##Human Influenza A Virus H1N1:Inhibition of infection In MDCK cells(IC50=1.6 µg/ml);##Human Influenza A Virus H7N9:Inhibition of infection In MDCK cells(IC50=3.3 µg/ml).##[Ref.26911565]Human Influenza A Virus H1N1(IC50=1.2 µg/ml);Human Influenza A Virus H3N2(IC50=1.2 µg/ml);Human Influenza A Virus H5N1(IC50=2.4 µg/ml);Human Influenza A Virus H7N7(IC50=0.8 µg/ml);Human Influenza A Virus H7N9(IC50=4.6 µg/ml);MERS-CoV(IC50=4.8 µg/ml);SARS-CoV(IC50=4.8 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry [Ref.26911565]Cytotoxicity against Madin-Darby canine kidney cells(TC50=380 μg/ml). No predicted structure available DRAVPe01761.cif Linear Free Free None L Not found Mechanistic studies show that positively charged P9 broadly inhibits viral replication by binding to different viruses and then inhibits virus–host endosomal acidification to prevent the endosomal release of pH-dependent viruses. 3336.98 C144H227N47O35S5 DELMSY C 9.41 6 0 6 12 9 -6.67 -4104 1.4 hour 3 min >10 hour 55.33 5750 198.28 26911565##32843628 Sci Rep. 2016 Feb 25;6:22008. ##Nat Commun. 2020 Aug 25;11(1):4252. "Zhao H, Zhou J, Zhang K, Chu H, Liu D, Poon VK, Chan CC, Leung HC, Fai N, Lin YP, Zhang AJ, Jin DY, Yuen KY, Zheng BJ.##Zhao H, To KKW, Sze KH, Yung TT, Bian M, Lam H, Yeung ML, Li C, Chu H, Yuen KY." A novel peptide with potent and broad-spectrum antiviral activities against multiple respiratory viruses. ##A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2. 10.1038/srep22008##10.1038/s41467-020-17986-9 Anti-SARS-CoV-2 DRAVPe01760 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 "2019-nCoV-HR2P(SARS-CoV-2-S(1168-1203),SARS-HR2P)" Synthetic construct Q5DIC5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae Cell-cell fusion assay "[Ref.32047258]SARS-CoV-2:ihibition of cell-cell fusion in Huh-7 cells(IC50=0.18 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.98 µM).##[Ref.30989115]SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=0.52±0.11 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=2.81 µM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##CoV-WIV1:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=2.73 µM);##CoV-Rs3367:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.05 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01760.cif Linear Free Free None L membrane 2019-nCoV HR1 and HR2 regions are able to interact with each other to form 6-HB and suggest that 2019-nCoV-HR2P may inhibit 2019-nCoV fusion with and entry into the target cell. 4008.5 C172H292N48O61 CFHMPTWY ILN 4.2 3 7 -4 9 15 -17.78 -6802 1.1 hour 3 min >10 hour 138.06 0 0 30989115##32047258 Sci Adv. 2019 Apr 10;5(4):eaav4580.##Cell Mol Immunol. 2020 Jul;17(7):765-767. "Xia S, Yan L, Xu W, Agrawal AS, Algaissi A, Tseng CK, Wang Q, Du L, Tan W, Wilson IA, Jiang S, Yang B, Lu L.##Xia S, Zhu Y, Liu M, Lan Q, Xu W, Wu Y, Ying T, Liu S, Shi Z, Jiang S, Lu L." A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike.##Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. 10.1126/sciadv.aav4580##10.1038/s41423-020-0374-2 Anti-SARS-CoV-2 DRAVPe01758 AWDFGSLGGVFTSIGKALHQVFGAIYGAA 29 DENV2 Ep (419-447) Synthetic construct Q9WDA6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV-2 Flaviviridae Plaque assay [Ref.20881042]DENV2(dengue virus type 2): Inhibition of DENV-2 infection in BHK-21 cells (IC90~250µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01758.cif Linear Free Free None L low-pH endosome "an initial, nonspecific interaction of the hydrophobicC terminus of the peptide inhibitor with the viral membranecarries it with the virion into the endosome, allowing aspecific interaction of the peptide with domain II as theprotein reconfigures, inhibiting the final zipping of thestem" 2941.34 C139H202N34O37 CEMNPR G 6.79 2 1 1 10 15 73.79 1974 4.4 hour >20 hour >10 hour 91.03 6990 249.64 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-Anti-DENV-2 DRAVPe01759 GDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG 38 SARS-CoV-S (1149–1186) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Fusion inhibition assay "[Ref.15158473]SARS-CoV: inhibition of SARS-CoV cytopathic effect in Vero E6 cells ( synthetic HR2-38 IC50=0.5-5nM, GST-HR2-38 IC50=66.2nM)" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01759.cif Linear Free Free None L GST as GST-fusion polypeptide 4122.6 C176H298N50O63 CFHMPTWY ILN 4.2 3 7 -4 11 15 -18.95 -6614 30 hour >20 hour >10 hour 130.79 0 0 15158473 Biochem Biophys Res Commun. 2004 Jun 18;319(1):283-8. "Zhu J, Xiao G, Xu Y, Yuan F, Zheng C, Liu Y, Yan H, Cole DK, Bell JI, Rao Z, Tien P, Gao GF." Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. 10.1016/j.bbrc.2004.04.141 Anti-SARS-CoV DRAVPe01757 AWDFGSLGGVFTSIGKALHQVFGGAFGAA 29 "DENV2 Ep (419-447)[A24G,I25A,Y26F]" Synthetic construct Q9WDA6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV-2 Flaviviridae Plaque assay [Ref.20881042]DENV2(dengue virus type 2): Inhibition of DENV-2 infection in BHK-21 cells (IC90~2µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01757.cif Linear Free Free None L low-pH endosome "an initial, nonspecific interaction of the hydrophobicC terminus of the peptide inhibitor with the viral membranecarries it with the virion into the endosome, allowing aspecific interaction of the peptide with domain II as theprotein reconfigures, inhibiting the final zipping of thestem" 2869.23 C135H194N34O36 CEMNPRY G 6.79 2 1 1 10 15 71.03 1888 4.4 hour >20 hour >10 hour 77.59 5500 196.43 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-Anti-DENV-2 DRAVPe01756 ALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFEL 33 SARS-CoV Sgp (471-503) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay [Ref.16153058]SARS-CoV(Severe acute respiratory syndrome): inhibition of SARS-CoV infction in Vero cells (EC50=41.6µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01756.cif Linear Free Free None L not found "block the binding between the RBD and angiotensin-convertingenzyme 2, resulting in the inhibition of SARS-CoV entrance into host cells in vitro" 3864.39 C184H260N40O50S HKM Y 4.37 1 2 -1 15 12 16.67 -1016 4.4 hour >20 hour >10 hour 88.48 12950 404.69 16153058 J Comb Chem. 2005 Sep-Oct;7(5):648-56. "Hu H, Li L, Kao RY, Kou B, Wang Z, Zhang L, Zhang H, Hao Z, Tsui WH, Ni A, Cui L, Fan B, Guo F, Rao S, Jiang C, Li Q, Sun M, He W, Liu G." Screening and identification of linear B-cell epitopes and entry-blocking peptide of severe acute respiratory syndrome (SARS)-associated coronavirus using synthetic overlapping peptide library. 10.1021/cc0500607 Anti-SARS-CoV DRAVPe01755 SLTQINTTLLDLEYEMRSLQQVVKALNESYIDLKEL 36 "MERS-CoV-HR2P [T1263E,L1267R]" Synthetic construct K9N5Q8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–cell fusion [Ref.24473083]MERS-COV(Middle East respiratory syndrome coronavirus): inhibition of cell–cell fusion infection in Huh-7 and 293T/MERS/EGFP cells (IC50=0.93±0.15µM); inhibition of MERS-CoV infection in Vero cells (IC50=0.6µM); inhibition of MERS-CoV infection in Calu-3 cells (IC50=0.6µM); inhibition of MERS-CoV infection in HFL cells (IC50=13.9µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24473083]HR2P has low or no in vitro toxic effect. No predicted structure available DRAVPe01755.cif Linear Free Free None L HR1 domain "interact with the viral HR1 domain to form heterologous 6-HB and block viral fusion coreformation, resulting in inhibition of MERS-CoV S protein-mediated membrane fusion." 4212.82 C186H308N46O62S CFGHPW L 4.36 3 6 -3 10 13 -17.78 -5735 1.9 hour >20 hour >10 hour 127.22 2980 85.14 24473083 Nat Commun. 2014;5:3067. "Lu L, Liu Q, Zhu Y, Chan KH, Qin L, Li Y, Wang Q, Chan JF, Du L, Yu F, Ma C, Ye S, Yuen KY, Zhang R, Jiang S." Structure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitor. 10.1038/ncomms4067 Anti-MERS-CoV DRAVPe01754 LTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 35 MERS-S (1252-1286) Synthetic construct K9N5Q8##R9UQ53 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV PsV Coronaviridae pseudovirus entry inhibition assay [Ref.24067982]MERS-COV(Middle East respiratory syndrome coronavirus): inhibition of MERS-CoV PsV infection in 293T/Huh7 cells (EC50~3.013µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01754.cif Linear Free Free None L membrane inhibit MERS-CoV fusion and entry by using a pseudotyped-virus system 4054.71 C182H302N42O59S CFGHPRW L 4.18 2 5 -3 10 14 15.71 -2987 5.5 hour 3 min 2 min 142 2980 87.65 24067982 J Virol. 2013 Dec;87(24):13134-40. "Gao J, Lu G, Qi J, Li Y, Wu Y, Deng Y, Geng H, Li H, Wang Q, Xiao H, Tan W, Yan J, Gao GF." Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus. 10.1128/JVI.02433-13 Anti-MERS-CoV DRAVPe01753 RIQQIEQKIHHIEQRIQQIEQRISGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARIL 59 T21N36 Synthetic construct A1YNW7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV-1 Retroviridae Cell-cell fusion assay [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=81.8±5.69nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01753.cif Linear Acetylation Free None L gp41 function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds 7070.23 C312H526N100O87 CDFMPY Q 10.78 10 4 6 6 24 -45.25 -12299 1 hour 2 min 2 min 133.9 5500 94.83 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. "Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z." Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. 10.1016/j.bmc.2019.115214 Anti-HIV-1 DRAVPe01752 RIQQIEQKIHHIEQRIQQIEQRAIEAQQHLLQLTVWGIKQLQARIL 46 T21N23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV-1 Retroviridae Cell-cell fusion assay [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=38.9±35.8nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01752.cif Linear Acetylation Free None L gp41 function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds 5605.54 C249H417N79O68 CDFMNPSY Q 9.97 9 4 5 2 19 -52.83 -9943 1 hour 2 min 2 min 131.52 5500 122.22 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. "Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z." Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. 10.1016/j.bmc.2019.115214 Anti-HIV-1 DRAVPe01751 RIQQIEQKIHHIEQRIQQIEQLLQLTVWGIKQLQARIL 38 T21N17 Synthetic construct NoneNo entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Cell-cell fusion assay [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=251±41.1nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01751.cif Linear Acetylation Free None L gp41 function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds 4671.52 C210H354N64O56 CDFMNPSY Q 9.98 7 3 4 2 16 -37.37 -7050 1 hour 2 min 2 min 143.68 5500 148.65 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. "Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z." Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. 10.1016/j.bmc.2019.115214 Anti-HIV-1 DRAVPe01750 LHQNIVDVQYMYGLS 15 "HCV gp (696–710), E2-79" Synthetic construct Q99IB8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae HCV infection assay [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM No predicted structure available DRAVPe01750.cif Linear Free Free None L Envelope protein "Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release." 1780.03 C80H122N20O24S ACEFKPRTW LQVY 5.08 1 1 0 5 5 9.33 -865 5.5 hour 3 min 2 min 116.67 2980 212.86 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. "Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W." A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. 10.1038/s41598-017-04274-8 Anti-HCV DRAVPe01749 GLLHLHQNIVDVQYM 15 "HCV gp (692–706), E2-78" Synthetic construct Q99IB8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae HCV infection assay [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM No predicted structure available DRAVPe01749.cif Linear Free Free None L Envelope protein "Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release." 1780.07 C80H126N22O22S ACEFKPRSTW L 5.97 2 1 1 3 6 27.33 -485 30 hour >20 hour >10 hour 142.67 1490 106.43 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. "Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W." A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. 10.1038/s41598-017-04274-8 Anti-HCV DRAVPe01748 FGCTWMNSTGFTKTC 15 "HCV gp (552–566), E2-43" Synthetic construct Q99IB8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae HCV infection assay [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM No predicted structure available DRAVPe01748.cif Linear Free Free None L Envelope protein "Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release." 1683.93 C73H106N18O22S3 ADEHILPQRVY T 8.06 1 0 1 10 3 -1.33 -1079 1.1 hour 3 min 2 min 0 5625 401.79 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. "Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W." A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. 10.1038/s41598-017-04274-8 Anti-HCV DRAVPe01747 QGSWFGCTWMNSTGF 18 "HCV gp (548–562), E2-42" Synthetic construct Q99IB8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae HCV infection assay [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM No predicted structure available DRAVPe01747.cif Linear Free Free None L Envelope protein "Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release." 1708.88 C77H101N19O22S2 ADEHIKLPRVY G 5.52 0 0 0 9 4 -20 -705 0.8 hour 10 min >10 hour 0 11000 785.71 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. "Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W." A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. 10.1038/s41598-017-04274-8 Anti-HCV DRAVPe01746 VEPGQLKLNWFKK 13 P7(DENV-2 gp (662-674)) Synthetic construct P14340 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "DENV-1, DENV-2" Flaviviridae Plaque assay "[Ref.29709564]DENV-2(dengue virus serotype 2): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(65 ± 6% inhibition at 40 μM,55± 12% inhibition at 20 μM,41± 13% inhibition at 10 μM,IC50=12.86±5.96µM);##DENV-1(dengue virus serotype 1): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(65 ± 12% inhibition at 40 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.29709564]No toxic effect on HUVEC(Human umbilical vein endothelial cells) at concentrations up to 100 µM No predicted structure available DRAVPe01746.cif Linear Free Free None L β3 integrin might be involved in blocking viral entry via occupying the binding site in the receptor on the host cell(β3 integrin). 1586.9 C76H119N19O18 ACDHIMRSTY K 9.7 3 1 2 2 5 -80.77 -1551 100 hour >20 hour >10 hour 82.31 5500 458.33 29709564 Antiviral Res. 2018 Jul;155:20-27. "Cui X, Wu Y, Fan D, Gao N, Ming Y, Wang P, An J." Peptides P4 and P7 derived from E protein inhibit entry of dengue virus serotype 2 via interacting with β3 integrin. 10.1016/j.antiviral.2018.04.018 "Anti-Anti-DENV-1, Anti-Anti-DENV-2" DRAVPe01745 CKIPFEIMDLEKRHV 15 P4(DENV-2 gp (613-627)) Synthetic construct P14340 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV-2 Flaviviridae Plaque assay "[Ref.29709564]DENV-2(dengue virus serotype 2): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(70 ± 9% inhibition at 40 μM,44 ± 10% inhibition at 20 μM,40± 6% inhibition at 10 μM,IC50=19.08±2.52µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.29709564]No toxic effect on HUVEC(Human umbilical vein endothelial cells) at concentrations up to 100 µM No predicted structure available DRAVPe01745.cif Linear Free Free None L β3 integrin might be involved in blocking viral entry via occupying the binding site in the receptor on the host cell(β3 integrin). 1858.25 C83H136N22O22S2 AGNQSTWY EIK 6.75 4 3 1 1 5 -22.67 -2761 1.2 hour >20 hour >10 hour 97.33 0 0 29709564 Antiviral Res. 2018 Jul;155:20-27. "Cui X, Wu Y, Fan D, Gao N, Ming Y, Wang P, An J." Peptides P4 and P7 derived from E protein inhibit entry of dengue virus serotype 2 via interacting with β3 integrin. 10.1016/j.antiviral.2018.04.018 Anti-Anti-DENV-2 DRAVPe01744 DLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKE 39 MHV-S (1216-1254) Synthetic construct P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM);##MHV(mouse hepatitis virus): inhibition of MHV infection in Vero 118 cells (EC50=0.9±0.1µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01744.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 4644.31 C207H337N51O67S CGHPW L 4.51 5 8 -3 10 14 -42.56 -7826 1.1 hour 3 min >10 hour 120 2980 78.42 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01742 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 60 SARS-CoV-S (1134-1185) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=34±4.0µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01742.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 6817.53 C298H478N78O104 CMW LDE 4.27 7 14 -7 15 21 -56.17 -13509 1 hour 30 min >10 hour 107.17 1490 25.25 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01743 NQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLIT 46 SARS-CoV-S (935-980) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01743.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 5040.71 C218H369N63O73 CHMPWY L 4.86 4 5 -1 13 20 -0.43 -7678 1.4 hour 3 min >10 hour 127.17 0 0 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01741 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 68 SARS-CoV-S (1134-1193) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=17±3.0µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01741.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 7827.69 C346H549N89O117 CMW ELDK 4.46 9 15 -6 18 22 -69.12 -15296 1 hour 30 min >10 hour 100.29 4470 66.72 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01740 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 40 SARS-CoV-S (1150-1189) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01740.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 4486.01 C194H323N53O68 CFHMPTW EILN 4.33 4 8 -4 11 15 -38.75 -7958 1.1 hour 3 min >10 hour 124.25 1490 38.21 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01739 LDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 56 SARS-CoV-S (1134-1189) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01739.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 6317.03 C277H446N74O94 CMW LDN 4.5 7 11 -4 16 19 -54.82 -11645 5.5 hour 3 min 2 min 107.86 2980 54.18 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01738 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 64 SARS-CoV (1126-1189)[F5P] Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=43±6.4µM);##MHV(mouse hepatitis virus): inhibition of MHV infection in Vero 118 cells (EC50>50µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01738.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 7244.99 C316H507N83O111 CMW ELD 4.34 8 15 -7 17 20 -73.75 -14963 1 hour 30 min >10 hour 100.47 2980 47.3 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01737 PKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 60 SARS-CoV (1130-1189)[F1P] Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV, MHV" Coronaviridae Infection inhibition assay [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=24±2.8µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01737.cif Linear Free Free None L membrane Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). 6800.55 C298H479N79O102 CMW ELDKN 4.49 8 13 -5 16 19 -72 -13562 >20 hour >20 hour ? 100.67 2980 50.51 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 "Anti-SARS-CoV, Anti-MHV" DRAVPe01736 DVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI 48 SARS-Cov-S (1145-1192) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV PsV Coronaviridae HIV‐luc/SARS Pseudotyped Virus Entry Inhibition Assay [Ref.18442051]SARS-CoV PsV: inhibition of HIV-luc/SARS PsV infection in Vero-E6 cells (EC50=2.15μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01736.cif Linear Free Free None L not found No machanism information found in the reference(s) presented in this entry 5390 C235H384N62O82 CFHMPTW IL 4.11 4 10 -6 13 18 -31.67 -8788 1.1 hour 3 min >10 hour 125.83 2980 63.4 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. "Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM." Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors. 10.1002/jcb.21790 Anti-SARS-CoV DRAVPe01735 YENQKQIANQFNKAISQIQESLTTTSTA 28 SARS-Cov-S (899-926) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV PsV Coronaviridae HIV‐luc/SARS Pseudotyped Virus Entry Inhibition Assay [Ref.18442051]SARS-CoV PsV: inhibition of HIV-luc/SARS PsV infection in Vero-E6 cells (EC50=1.16μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01735.cif Linear Free Free None L not found No machanism information found in the reference(s) presented in this entry 3157.44 C135H218N38O49 CDGHMPRVW Q 6.14 2 2 0 11 8 -85 -6487 2.8 hour 10 min 2 min 66.43 1490 55.19 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. "Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM." Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors. 10.1002/jcb.21790 Anti-SARS-CoV DRAVPe01733 GNHILSLVQNAPYGLYFIHFSW 22 MHV (1096–1117)[Y1117W] Synthetic construct P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MHV Plaque reduction assay [Ref.16616792]MHV(murine hepatitis virus): inhibition of virus infection in L2 cells(22% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on L2 cells No predicted structure available DRAVPe01733.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2576.94 C125H174N30O30 CDEKMRT L 6.92 2 0 2 8 10 34.55 540 30 hour >20 hour >10 hour 106.36 8480 403.81 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-MHV DRAVPe01734 GYFVQDDGEWKFTGSSYYY 19 MHV (1144–1162) Synthetic construct P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MHV Plaque reduction assay "[Ref.16616792]MHV(murine hepatitis virus): inhibition of virus infection in L2 cells(98% inhibition at 30 Μm, IC50=4 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on L2cells No predicted structure available DRAVPe01734.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2312.43 C110H138N22O34 ACHILMNPR Y 4.03 1 3 -2 10 4 -93.16 -3012 30 hour >20 hour >10 hour 15.26 11460 636.67 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-MHV DRAVPe01732 AACEVAKNLNESLIDLQELGKYEQYIKW 28 AAC-SARS-CoV (1170–1194) Synthetic construct Q19QX0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(42% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells No predicted structure available DRAVPe01732.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 3269.72 C147H230N36O46S FHMPRT EL 4.59 3 5 -2 7 11 -41.43 -3711 4.4 hour >20 hour >10 hour 104.64 8480 314.07 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01731 GVFVFNGTSWFITQRNFFS 19 SARS-CoV (1075–1093) Synthetic construct Q19QX0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay "[Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(83% inhibition at 30 μM,IC50~2 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells No predicted structure available DRAVPe01731.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2254.53 C109H148N26O27 ACDEHKLMPY F 9.75 1 0 1 8 9 37.89 -1357 30 hour >20 hour >10 hour 51.05 5500 305.56 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01730 GYHLMSFPQAAPHGVVFLHVTW 22 SARS-CoV (1028–1049)[Y1049W] Synthetic construct Q19QX0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay "[Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(90% inhibition at 30 μM,IC50~2 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells No predicted structure available DRAVPe01730.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2607.98 C120H166N30O26S CDEIKNR HV 7.02 3 0 3 5 10 45.65 1247 30 hour >20 hour >10 hour 80.43 6990 317.73 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01729 ATAGWTFGAGAALQIPFAMQMAY 23 SARS-CoV (864-886) Synthetic construct Q19QX0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(39% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells No predicted structure available DRAVPe01729.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2374.76 C110H160N26O29S2 CDEHKNRSV A 5.57 0 0 0 6 12 73.48 2196 4.4 hour >20 hour >10 hour 64.35 6990 317.73 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01727 TLKPIFKLPLGINITNFR 18 "SARS-CoV-S (215-232), peptide 9626" Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV PsV Coronaviridae western blot [Ref.19853613]SARS-COV: inhibition of SARS-CoV/HIV PsV virus infection in 293T/ACE2 cells (IC50=11µM); inhibition of SARS-CoV/HIV PsV virus entry in 293T/ACE2 cells(80% at 50µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01727.cif Linear Free Free None L not found "Presumably inhibit virus entry by binding to Spike protein, hACE2, or an unknown co-receptor." 2085.56 C100H165N25O23 ACDEHMQSVWY IL 11.17 3 0 3 5 8 34.44 -802 7.2 hour >20 hour >10 hour 130 0 0 19853613 J Mol Biol. 2009 Dec 11;394(4):600-5. "Guo Y, Tisoncik J, McReynolds S, Farzan M, Prabhakar BS, Gallagher T, Rong L, Caffrey M." Identification of a new region of SARS-CoV S protein critical for viral entry. 10.1016/j.jmb.2009.10.032 Anti-SARS-CoV PsV DRAVPe01728 MWKTPTLKYFGGFNFSQIL 19 SARS-CoV (770-788)[Y771W] Synthetic construct Q19QX0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque reduction assay [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(58% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells No predicted structure available DRAVPe01728.cif Linear Free Free None L cell membrane inhibits viral entry through coiled coil interactions. 2278.7 C111H160N24O26S ACDEHRV F 9.7 2 0 2 7 7 4.21 -170 30 hour >20 hour >10 hour 61.58 6990 388.33 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF." Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01726 QNQSANQFQKEISQINEVLTTTNTSLGKLQDDVNQNNQSLNTLQKE 46 "N46eg(SARS-CoV (902-947)[K2N,I4S,N9Q,A11E,Q16N,S18V,S23N,A25S,V32D,A37N,A39S,V44Q,Q46E])" Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae cell fusion inhibition assay [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=5.07 ± 0.17 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. No predicted structure available DRAVPe01726.cif Linear Free Free None L membrane "Binding to the HR2 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry." 5205.59 C216H356N66O83 CHMPRWY Q 4.51 3 5 -2 18 11 -119.13 -13570 0.8 hour 10 min >10 hour 74.13 0 0 18983873 Antiviral Res. 2009 Jan;81(1):82-7. "Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK." Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. 10.1016/j.antiviral.2008.10.001 Anti-SARS-CoV DRAVPe01725 QKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQ 46 N46(SARS-CoV (902-947)) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae cell fusion inhibition assay [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=3.97 ± 1.40 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. No predicted structure available DRAVPe01725.cif Linear Free Free None L membrane "Binding to the HR2 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry." 5027.67 C216H366N64O73 CHMPRWY Q 9.53 4 2 2 14 17 -45.65 -7939 0.8 hour 10 min >10 hour 97.61 0 0 18983873 Antiviral Res. 2009 Jan;81(1):82-7. "Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK." Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. 10.1016/j.antiviral.2008.10.001 Anti-SARS-CoV DRAVPe01723 GINASVVNIQKEIDRLNEVAKNLNESLIDL 30 P4(SARS-CoV (1153–1182)) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae cell fusion inhibition assay [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=0.80 ± 0.21 μM);inhibition of SARS-CoV infection in Vero-E6 cells (IC50=3.17 ± 0.24 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. No predicted structure available DRAVPe01723.cif Linear Free Free None L membrane "Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry." 3322.76 C143H245N41O49 CFHMPTWY N 4.51 3 5 -2 8 13 -11.33 -5339 30 hour >20 hour >10 hour 139.67 0 0 18983873 Antiviral Res. 2009 Jan;81(1):82-7. "Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK." Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. 10.1016/j.antiviral.2008.10.001 Anti-SARS-CoV DRAVPe01724 GINASVVNIQKEIDRLNEVAKNL 23 P6(SARS-CoV (1153–1175)) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae cell fusion inhibition assay [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=1.04 ± 0.22 μM); inhibition of SARS-CoV infection in Vero-E6 cells (IC50=2.28 ± 0.81 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. No predicted structure available DRAVPe01724.cif Linear Free Free None L membrane "Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry." 2537.9 C109H189N33O36 CFHMPTWY N 6.18 3 3 0 6 10 -18.26 -4258 30 hour >20 hour >10 hour 131.3 0 0 18983873 Antiviral Res. 2009 Jan;81(1):82-7. "Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK." Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. 10.1016/j.antiviral.2008.10.001 Anti-SARS-CoV DRAVPe01722 GINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 37 P1(SARS-CoV (1153-1189)) Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae cell fusion inhibition assay [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=0.62 ± 0.20 μM);inhibition of SARS-CoV infection in Vero-E6 cells (IC50=3.04 ± 0.06 μM).##[Ref.15043961]SARS-CoV:inhibition of the cytopathic effect in Vero E6 cells(IC50~19 μM/L). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. No predicted structure available DRAVPe01722.cif Linear Free Free None L membrane "Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry." 4170.69 C181H302N50O62 CFHMPTW ELN 4.49 4 7 -3 10 14 -42.43 -7238 30 hour >20 hour >10 hour 123.78 1490 41.39 18983873##15043961 Antiviral Res. 2009 Jan;81(1):82-7.##Lancet. 2004 Mar 20;363(9413):938-47. "Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK.##Liu S, Xiao G, Chen Y, He Y, Niu J, Escalante CR, Xiong H, Farmar J, Debnath AK, Tien P, Jiang S." Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors.##Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. 10.1093/infdis/jiv325.##10.1016/j.antiviral.2008.10.001.##10.1016/S0140-6736(04)15788-7. Anti-SARS-CoV DRAVPe01721 AWDFGSVGGVFNSLGKGIHQIFGAAFKSL 29 ZIKV Ep (424-452) Synthetic construct Q32ZE1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None ZIKV Flaviviridae "qRT-PCR, western blotting, the plaque assay" [Ref.28232248]Zika virus (ZIKV):inhibition of Zika virus (ZIKV) infection in Vero cells (IC50=1.32μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01721.cif Linear Free Free None L membrane Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. 3011.43 C142H208N36O37 CEMPRTY G 8.64 3 1 2 10 14 49.66 622 4.4 hour >20 hour >10 hour 84.14 5500 196.43 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 Anti-ZIKV DRAVPe01719 AWDFGSIGGVFNSIGRAVHQVFGGAFRTL 29 JEV Ep (424–452) Synthetic construct P0DOH7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None JEV Flaviviridae "qRT-PCR, western blotting, the plaque assay" [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=7.66 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01719.cif Linear Free Free None L membrane Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. 3067.46 C142H208N40O37 CEKMPY G 9.65 3 1 2 10 14 47.24 -1257 4.4 hour >20 hour >10 hour 80.69 5500 196.43 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 Anti-JEV DRAVPe01720 AWDFGSIGGVFNSIGRAVHQVF 22 JEV Ep (424–445) Synthetic construct P0DOH7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "JEV, ZIKV" Flaviviridae "qRT-PCR, western blotting, the plaque assay" [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=3.93 nM);##Zika virus (ZIKV):inhibition of Zika virus (ZIKV) infection in Vero cells (IC50=3.27μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01720.cif Linear Free Free None L membrane "The peptide prevented JEV infection in mice by reducing viral load and the inflammatory response in the brain, thereby improving the survival rate." 2364.65 C110H158N30O29 CEKLMPTY G 6.79 2 1 1 7 11 51.36 -667 4.4 hour >20 hour >10 hour 84.09 5500 261.9 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 "Anti-JEV, Anti-ZIKV" DRAVPe01718 AALGDTAWDFGSIGGVFNSIGRAVHQVFGGAFRTL 35 JEV Ep (418–452) Synthetic construct P0DOH7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None JEV Flaviviridae "qRT-PCR, western blotting, the plaque assay" [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=58.07 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01718.cif Linear Free Free None L membrane Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. 3596.02 C164H244N46O46 CEKMPY G 6.79 3 2 1 12 17 47.14 -1438 4.4 hour >20 hour >10 hour 83.71 5500 161.76 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 Anti-JEV DRAVPe01717 SIGGVFNSIGRAVHQVFGGAFRTL 24 JEV Ep (428–452) Synthetic construct P0DOH7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None JEV Flaviviridae "qRT-PCR, western blotting, the plaque assay" [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=94.10 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01717.cif Linear Free Free None L membrane Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. 2490.85 C113H176N34O30 CDEKMPWY G 12 3 0 3 9 11 57.92 -1191 1.9 hour >20 hour >10 hour 93.33 0 0 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 Anti-JEV DRAVPe01716 STLGKAFSTTLKGAQRLAALGDTAWDFG 28 JEV Ep (401–428) Synthetic construct P0DOH7 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None JEV Flaviviridae "qRT-PCR, western blotting, the plaque assay, immunofluorescence analysis" [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=3790.71 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01716.cif Linear Free Free None L membrane Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. 2884.24 C129H203N35O40 CEHIMNPVY A 8.31 3 2 1 10 12 0.36 -2530 1.9 hour >20 hour >10 hour 73.57 5500 203.7 28232248 Antiviral Res. 2017 May;141:140-149. "Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W." Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. 10.1016/j.antiviral.2017.02.009 Anti-JEV DRAVPe01714 LDLSDEMAMLLQEVVKQLNDSYIDLKELGNYTYYNKW 37 HKU4-HR2P3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref.30646495]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=0.55 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.48 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.52 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. No predicted structure available DRAVPe01714.cif Linear Free Free None L membrane The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. 4457.05 C201H308N46O64S2 CFHPR L 4.14 3 7 -4 11 12 -47.03 -5567 5.5 hour 3 min 2 min 102.7 11460 318.33 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 "Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L." Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. 10.3390/v11010056 Anti-MERS-CoV DRAVPe01715 GGGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 39 MERS-HR2P Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref.30646495]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.07 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=1.14 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=1.71 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. No predicted structure available DRAVPe01715.cif Linear Free Free None L membrane The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. 4312.94 C191H316N46O64S CFHPRW L 4.18 2 5 -3 14 14 8.97 -3045 30 hour >20 hour >10 hour 127.44 2980 78.42 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 "Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L." Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. 10.3390/v11010056 Anti-MERS-CoV DRAVPe01713 EISKINTTLLDLSDEMAMLLQEVVKQLNDSYIDLKEL 37 HKU4-HR2P2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref.30646495]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=0.38 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.34 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.44 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. No predicted structure available DRAVPe01713.cif Linear Free Free None L membrane The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. 4266.93 C187H314N44O64S2 CFGHPRW L 4.07 3 8 -5 8 14 -2.43 -4990 1 hour 30 min >10 hour 134.32 1490 41.39 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 "Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L." Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. 10.3390/v11010056 Anti-MERS-CoV DRAVPe01712 GPNFAEISKINTTLLDLSDEMAMLLQEVVKQLNDSYI 37 HKU4-HR2P1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref.30646495]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.09 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=2.15 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=2.72 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. No predicted structure available DRAVPe01712.cif Linear Free Free None L membrane The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. 4154.76 C183H298N44O61S2 CHRW L 4.02 2 6 -4 10 14 4.05 -3957 30 hour >20 hour >10 hour 115.95 1490 41.39 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 "Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L." Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. 10.3390/v11010056 Anti-MERS-CoV DRAVPe01711 ISLTPLLVCVAALLLLEQ 18 E1P52-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01711.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1909.4 C89H157N19O24S DFGHKMNRWY L 4 0 1 -1 3 12 197.22 3402 20 hour 30 min >10 hour 216.67 0 0 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01709 GVISLTPLLVCVAALLLL 18 E1P52 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=55.7± 5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01709.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1808.34 C86H154N18O21S DEFHKMNQRWY L 5.52 0 0 0 4 13 257.22 5135 30 hour >20 hour >10 hour 232.78 0 0 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01710 VISLTPLLVCVAALLLLE 18 E1P52-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01710.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1880.4 C89H158N18O23S DFGHKMNQRWY L 4 0 1 -1 3 13 240 4360 100 hour >20 hour >10 hour 232.78 0 0 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01708 RGVISLTPLLVCVAALLL 18 E1P51-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01708.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1851.36 C86H155N21O21S DEFHKMNQWY L 8.25 1 0 1 4 12 211.11 3151 1 hour 2 min 2 min 211.11 0 0 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01707 WRGVISLTPLLVCVAALL 18 E1P51-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01707.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1924.42 C91H154N22O21S DEFHKMNQY L 8.25 1 0 1 4 12 185 2892 2.8 hour 3 min 2 min 189.44 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01705 DFWRGVISLTPLLVCVAA 18 E1P50-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01705.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1960.36 C92H146N22O23S EHKMNQY LV 5.83 1 1 0 4 11 138.89 1334 1.1 hour 3 min >10 hour 146.11 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01706 FWRGVISLTPLLVCVAAL 18 E1P51 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01706.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1958.44 C94H152N22O21S DEHKMNQY L 8.25 1 0 1 4 12 179.44 2698 1.1 hour 3 min 2 min 167.78 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01704 FDFWRGVISLTPLLVCVA 18 E1P50-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01704.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2036.46 C98H150N22O23S EHKMNQY LV 5.83 1 1 0 4 11 144.44 1451 1.1 hour 3 min 2 min 140.56 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01703 PFDFWRGVISLTPLLVCV 18 E1P50 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01703.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2062.5 C100H152N22O23S AEHKMNQY LV 6.22 1 1 0 4 10 125.56 1270 >20 hour >20 hour ? 135 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01702 VPFDFWRGVISLTPLLVC 18 E1P49-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01702.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2062.5 C100H152N22O23S AEHKMNQY LV 5.8 1 1 0 4 10 125.56 1270 100 hour >20 hour >10 hour 135 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01701 KVPFDFWRGVISLTPLLV 18 E1P49-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=63.3 ± 5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01701.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2087.54 C103H159N23O23 ACEHMNQY LV 8.75 2 1 1 3 10 90 587 1.3 hour 3 min 2 min 135 5500 323.53 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01699 LWKVPFDFWRGVISLTPL 18 E1P48-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=14.7 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01699.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2174.62 C109H160N24O23 ACEHMNQY L 8.75 2 1 1 3 10 61.67 416 5.5 hour 3 min 2 min 118.89 11000 647.06 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01700 WKVPFDFWRGVISLTPLL 18 E1P49 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=17.3 ± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01700.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2174.62 C109H160N24O23 ACEHMNQY L 8.75 2 1 1 3 10 61.67 416 2.8 hour 3 min 2 min 118.89 11000 647.06 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01697 EYLWKVPFDFWRGVISLT 18 E1P48 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=44.7 ± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01697.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2256.63 C112H158N24O26 ACHMNQ FLVW 6.17 2 2 0 4 9 22.78 -771 1 hour 30 min >10 hour 97.22 12490 734.71 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01698 YLWKVPFDFWRGVISLTP 18 E1P48-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=70.7 ±9.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01698.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2224.63 C112H158N24O24 ACEHMNQ FLPVW 8.59 2 1 1 4 9 33.33 -90 2.8 hour 10 min 2 min 97.22 12490 734.71 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01695 ILEYLWKVPFDFWRGVIS 18 E1P47-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=5.4 ± 0.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01695.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2268.69 C114H162N24O25 ACHMNQT FILVW 6.07 2 2 0 3 10 51.67 -22 20 hour 30 min >10 hour 118.89 12490 734.71 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01696 LEYLWKVPFDFWRGVISL 18 E1P47-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=6.6± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01696.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2268.69 C114H162N24O25 ACHMNQT L 6.07 2 2 0 3 10 47.78 -22 5.5 hour 3 min 2 min 118.89 12490 734.71 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01694 WILEYLWKVPFDFWRGVI 18 E1P47 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=2.7 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01694.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2367.82 C122H167N25O24 ACHMNQST W 6.07 2 2 0 2 11 51.11 551 2.8 hour 3 min 2 min 118.89 17990 1058.24 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01692 NYWILEYLWKVPFDFWRG 18 E1P46-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=12.3 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01692.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2432.81 C124H162N26O26 ACHMQST W 6.07 2 2 0 4 9 -23.89 -1023 1.4 hour 3 min >10 hour 81.11 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01693 YWILEYLWKVPFDFWRGV 18 E1P46-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=32.3 ± 11.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01693.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2417.84 C125H165N25O25 ACHMNQST W 6.07 2 2 0 3 10 18.89 45 2.8 hour 10 min 2 min 97.22 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01691 SNYWILEYLWKVPFDFWR 18 E1P46 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=19.7 ± 8.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01691.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2462.84 C125H164N26O27 ACGHMQT W 5.79 2 2 0 4 9 -26.11 -1457 1.9 hour >20 hour >10 hour 81.11 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01690 ASNYWILEYLWKVPFDFW 18 E1P45-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=11.3 ± 3.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01690.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2377.73 C122H157N23O27 CGHMQRT W 4.37 1 2 -1 4 10 8.89 216 4.4 hour >20 hour >10 hour 86.67 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01689 LASNYWILEYLWKVPFDF 18 E1P45-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=12.7 ±1.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01689.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2304.67 C117H158N22O27 CGHMQRT L 4.37 1 2 -1 4 10 35 475 5.5 hour 3 min 2 min 108.33 13980 822.35 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01688 QLASNYWILEYLWKVPFD 18 E1P45 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=27.7 ±5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01688.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2285.63 C113H157N23O28 CGHMRT L 4.37 1 2 -1 4 9 0 -377 0.8 hour 10 min >10 hour 108.33 13980 822.35 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01686 TEQLASNYWILEYLWKVP 18 E1P44-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01686.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2253.58 C109H157N23O29 CDFGHMR L 4.53 1 2 -1 5 8 -19.44 -741 7.2 hour >20 hour >10 hour 108.33 13980 822.35 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01687 EQLASNYWILEYLWKVPF 18 E1P44-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=90.3 ± 15.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01687.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2299.65 C114H159N23O28 CDGHMRT L 4.53 1 2 -1 4 9 0 -186 1 hour 30 min >10 hour 108.33 13980 822.35 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01685 WTEQLASNYWILEYLWKV 18 E1P44 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01685.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2342.68 C115H160N24O29 CDFGHMPR LW 4.53 1 2 -1 5 9 -15.56 -508 2.8 hour 3 min 2 min 108.33 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01684 RWTEQLASNYWILEYLWK 18 E1P43-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=19.7 ± 9.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01684.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2399.73 C116H163N27O29 CDFGHMPV LW 6.14 2 2 0 5 8 -63.89 -2404 1 hour 2 min 2 min 92.22 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01683 WRWTEQLASNYWILEYLW 18 E1P43-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=6.8 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01683.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2457.77 C121H161N27O29 CDFGHKMPV W 4.53 1 2 -1 5 9 -47.22 -1616 2.8 hour 3 min 2 min 92.22 24980 1469.41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01682 FWRWTEQLASNYWILEYL 18 E1P43 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=43.0 ± 10.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01682.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2418.74 C119H160N26O29 CDGHKMPV LW 4.53 1 2 -1 5 9 -26.67 -1551 1.1 hour 3 min 2 min 92.22 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01680 SEFWRWTEQLASNYWILE 18 E1P42-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=31.0 ± 3.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01680.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2358.59 C112H152N26O31 CDGHKMPV EW 4.25 1 3 -2 5 8 -64.44 -3050 1.9 hour >20 hour >10 hour 70.56 17990 1058.24 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01681 EFWRWTEQLASNYWILEY 18 E1P42-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01681.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2434.69 C118H156N26O31 CDGHKMPV EW 4.25 1 3 -2 5 8 -67.22 -2724 1 hour 30 min >10 hour 70.56 19480 1145.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01679 ESEFWRWTEQLASNYWIL 18 E1P42 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=50.0 ± 8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01679.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2358.59 C112H152N26O31 CDGHKMPV EW 4.25 1 3 -2 5 8 -64.44 -3050 1 hour 30 min >10 hour 70.56 17990 1058.24 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01677 KWESEFWRWTEQLASNYW 18 E1P41-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=66.7 ± 20.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01677.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2446.66 C117H152N28O31 CDGHIMPV W 4.79 2 3 -1 5 7 -137.22 -4356 1.3 hour 3 min 2 min 27.22 23490 1381.76 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01678 WESEFWRWTEQLASNYWI 18 E1P41-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=22.0 ± 0.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01678.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2431.65 C117H151N27O31 CDGHKMPV W 4.25 1 3 -2 5 8 -90.56 -3309 2.8 hour 3 min 2 min 48.89 23490 1381.76 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01676 LKWESEFWRWTEQLASNY 18 E1P41 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01676.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2373.61 C112H153N27O31 CDGHIMPV EW 4.79 2 3 -1 5 7 -111.11 -4097 5.5 hour 3 min 2 min 48.89 17990 1058.24 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01675 ELKWESEFWRWTEQLASN 18 E1P40-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01675.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2339.55 C108H151N27O32 CDGHIMPVY E 4.49 2 4 -2 4 7 -123.33 -4764 1 hour 30 min >10 hour 48.89 16500 970.59 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01674 CELKWESEFWRWTEQLAS 18 E1P40-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=34.0 ± 15.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01674.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2328.58 C107H150N26O31S DGHIMNPVY E 4.49 2 4 -2 4 7 -90 -3972 1.2 hour >20 hour >10 hour 48.89 16500 970.59 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01673 ACELKWESEFWRWTEQLA 18 E1P40 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01673.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2312.58 C107H150N26O30S DGHIMNPVY E 4.49 2 4 -2 3 8 -75.56 -3451 4.4 hour >20 hour >10 hour 54.44 16500 970.59 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01671 AVACELKWESEFWRWTEQ 18 E1P39-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=44.0 ± 13.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01671.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2298.56 C106H148N26O30S DGHIMNPY E 4.49 2 4 -2 3 8 -73.33 -3539 4.4 hour >20 hour >10 hour 48.89 16500 970.59 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01672 VACELKWESEFWRWTEQL 18 E1P39-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=37.7 ± 7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01672.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2340.64 C109H154N26O30S DGHIMNPY E 4.49 2 4 -2 3 8 -62.22 -3228 100 hour >20 hour >10 hour 65 16500 970.59 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01670 CAVACELKWESEFWRWTE 18 E1P39 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=11.3 ± 1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01670.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2273.57 C104H145N25O29S2 DGHIMNPQY E 4.49 2 4 -2 4 8 -40 -2857 1.2 hour >20 hour >10 hour 48.89 16625 977.94 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01668 LTCAVACELKWESEFWRW 18 E1P38-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01668.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2257.61 C105H149N25O27S2 DGHIMNPQY EW 4.79 2 3 -1 4 9 0.56 -1684 5.5 hour 3 min 2 min 70.56 16625 977.94 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01669 TCAVACELKWESEFWRWT 18 E1P38-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01669.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2245.56 C103H145N25O28S2 DGHIMNPQY EW 4.78 2 3 -1 5 8 -24.44 -2433 7.2 hour >20 hour >10 hour 48.89 16625 977.94 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01667 NLTCAVACELKWESEFWR 18 E1P38 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01667.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2185.5 C98H145N25O28S2 DGHIMPQY E 4.79 2 3 -1 5 8 -13.89 -2581 1.4 hour 3 min >10 hour 70.56 11125 654.41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01665 VPNLTCAVACELKWESEF 18 E1P37-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=80.0 ± 62.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01665.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2039.35 C91H139N21O28S2 DGHIMQRY E 4.25 1 3 -2 5 8 30.56 -918 100 hour >20 hour >10 hour 86.67 5625 330.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01666 PNLTCAVACELKWESEFR 18 E1P37-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=99.0 ± 22.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01666.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 2096.4 C92H142N24O28S2 DGHIMQY E 4.79 2 3 -1 5 7 -17.78 -2814 >20 hour >20 hour ? 70.56 5625 330.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01664 PVPNLTCAVACELKWESE 18 E1P37 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Fluorescence resonance energy transfer (FRET) assay [Ref.26905802]HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=41.0 ± 8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01664.cif Linear Free Free None L gp41 The peptide inhibits HIV-1 Env-mediated cell fusion thus inhibits virus infection. 1989.29 C87H137N21O28S2 DFGHIMQRY E 4.25 1 3 -2 5 7 6.11 -1216 >20 hour >20 hour ? 86.67 5625 330.88 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. "Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I." Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. 10.1016/j.bbagen.2016.02.008 Anti-HIV DRAVPe01663 yAIIXYNKYXNC 12 compound 6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=3.2 ± 0.4 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01663.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation "The 'X' at position 5 indicates N-methyl-4-O-methyl-tyrosine, position 10 indicates N-methyl-leucine." Mixed(D-Tyr1) NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1487.12 C50H70N12O11S DEFGHLMPQRSTVW INYX 8.15 1 0 1 5 3 -1.67 -618 73.33 2980 270.91 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01662 YTLPFHNXTFFC 12 compound 5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥50 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01662.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 8 indicates N-methyl-glycine. L NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1500.92 C68H86N14O15S ADEGIKMQRSVW F 6.73 1 0 1 5 4 30.83 -144 2.8 hour 10 min 2 min 32.5 1490 135.45 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01661 YXIAKYNXXIPC 12 compound 4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=4.6 ± 0.3 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01661.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation "The 'X' at position 2 indicates N-methyl-glycine, position 8 and 9 indicates N-methyl-4-O-methyl-tyrosine." L NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1418.29 C51H71N11O10S DEFGHLMQRSTVW X 8.18 1 0 1 4 3 14.17 46 2.8 hour 10 min 2 min 73.33 2980 270.91 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01660 YTNFYLYPYXFC 12 compound 3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=2.2 ± 0.1 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01660.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 10 indicates MeYMe(N-methyl-4-O-methyl-tyrosine). L NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1605.03 C76H90N12O17S ADEGHIKMQRSVW Y 5.52 0 0 0 7 3 7.5 239 2.8 hour 10 min 2 min 32.5 5960 541.82 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01659 YXKXKXXKXXKC 12 compound 2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=0.25 ± 0.01 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=1.7 ± 0.1 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=3.9 ± 0.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01659.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation "The 'X' at position 2,7,9 and 10 indicates MeYMe(N-methyl-4-O-methyl-tyrosine), position 4 indicates MeF(N-methyl-phenylalanine), position 6 indicates MeS(N-methyl-serine)." L NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1465.01 C36H52N10O2S ADEFGHILMNPQRSTVW X 9.87 4 0 4 2 0 -120 -2106 2.8 hour 10 min 2 min 0 1490 135.45 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01658 YWKIXNTLVNIC 12 compound 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "ZIKV,DENV,WNV" Flaviviridae protease enzymatic inhibition assay [Ref.30783498]Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=1.5 ± 0.1 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM);##West Nile virus: inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01658.cif Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 4 indicates MeYMe(N-methyl-4-O-methyl-tyrosine). L NS2B-NS3 protease No machanism information found in the reference(s) presented in this entry 1477.97 C64H97N15O15S ADEFGHMPQRS IN 8.2 1 0 1 5 5 47.5 87 2.8 hour 10 min 2 min 121.67 6990 635.45 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. "Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. " De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. 10.1021/acsmedchemlett.8b00535 "Anti-ZIKV,Anti-DENV,Anti-WNV" DRAVPe01657 GVLV 4 Peptide 6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HCMV,VZV" "Coronaviridae, Herpesviridae" Cytopathic effect assay [Ref.34502335]SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>4 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34502335]Vero cell:CC50=77.4 ±0.7 µM. No predicted structure available DRAVPe01657.cif Linear Acylation Methyl amidation None L Main protease No machanism information found in the reference(s) presented in this entry 386.49 C18H34N4O5 ACDEFHIKMNPQRSTWY V 5.52 0 0 0 1 3 295 1394 30 hour >20 hour >10 hour 242.5 0 0 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. "Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A." "Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation." 10.3390/ijms22179427 "Anti-SARS-CoV-2,Anti-HCMV,Anti-VZV" DRAVPe01656 GVLVQ 5 Peptide 5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HCMV,VZV" "Coronaviridae, Herpesviridae" Cytopathic effect assay [Ref.34502335]SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=59.80 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34502335]Vero cell:CC50=75.0 ±2.2 µM. No predicted structure available DRAVPe01656.cif Linear Acylation Methyl amidation None L Main protease No machanism information found in the reference(s) presented in this entry 514.62 C23H42N6O7 ACDEFHIKMNPRSTWY V 5.52 0 0 0 1 3 166 840 30 hour >20 hour >10 hour 194 0 0 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. "Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A." "Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation." 10.3390/ijms22179427 "Anti-SARS-CoV-2,Anti-HCMV,Anti-VZV" DRAVPe01655 GGVLVQPG 8 Peptide 4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HCMV,VZV" "Coronaviridae, Herpesviridae" Cytopathic effect assay [Ref.34502335]SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=78.20 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34502335]Vero cell:CC50=74.9 ± 4.9 µM. No predicted structure available DRAVPe01655.cif Linear Pivaloylation Methyl amidation None L Main protease No machanism information found in the reference(s) presented in this entry 725.84 C32H55N9O10 ACDEFHIKMNRSTWY G 5.52 0 0 0 3 3 73.75 1028 30 hour >20 hour >10 hour 121.25 0 0 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. "Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A." "Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation." 10.3390/ijms22179427 "Anti-SARS-CoV-2,Anti-HCMV,Anti-VZV" DRAVPe01653 GGVLVQPG 8 Peptide 2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HCMV,VZV" "Coronaviridae, Herpesviridae" Cytopathic effect assay [Ref.34502335]SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥17.6 ± 2.4 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=50.05 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=48.42 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34502335]Vero cell:CC50=83.0 ± 17.0 µM. No predicted structure available DRAVPe01653.cif Linear Acylation Amidation None L Main protease No machanism information found in the reference(s) presented in this entry 725.84 C32H55N9O10 ACDEFHIKMNRSTWY G 5.52 0 0 0 3 3 73.75 1028 30 hour >20 hour >10 hour 121.25 0 0 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. "Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A." "Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation." 10.3390/ijms22179427 "Anti-SARS-CoV-2,Anti-HCMV,Anti-VZV" DRAVPe01654 GGVLVQPG 8 Peptide 3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HCMV,VZV" "Coronaviridae, Herpesviridae" Cytopathic effect assay [Ref.34502335]SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50>20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=58.09 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=81.09 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34502335]Vero cell:CC50=81.8 ± 2.1 µM. No predicted structure available DRAVPe01654.cif Linear Acylation Methyl amidation None L Main protease No machanism information found in the reference(s) presented in this entry 725.84 C32H55N9O10 ACDEFHIKMNRSTWY G 5.52 0 0 0 3 3 73.75 1028 30 hour >20 hour >10 hour 121.25 0 0 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. "Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A." "Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation." 10.3390/ijms22179427 "Anti-SARS-CoV-2,Anti-HCMV,Anti-VZV" DRAVPe01652 SAHS 4 Ac-SAHS-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Neutralization assay [Ref.34681184]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=5.77 ± 0.01 × 10−7 μM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=4.3 ± 0.3 × 10−10 μM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=9.36 ± 0.1 × 10−7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01652.cif Linear Acylation Amidation None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 400.39 C15H24N6O7 CDEFGIKLMNPQRTVWY S 6.46 1 0 1 2 1 -75 -965 1.9 hour >20 hour >10 hour 25 0 0 34681184 Pharmaceuticals (Basel). 2021 Sep 23;14(10):959.  "Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M." "Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies." 10.3390/ph14100959 Anti-Influenza virus DRAVPe01651 SKHS 4 Peptide 17(lactoferrin 418–421) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=3 ± 0.61 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=0.048 ± 0.0012 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.0 ± 0.02 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01651.cif Linear Acylation Amidation None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 457.49 C18H31N7O7 ACDEFGILMNPQRTVWY S 8.49 2 0 2 2 0 -217.5 -1701 1.9 hour >20 hour >10 hour 0 0 0 28878220##34681184 Sci Rep. 2017 Sep 6;7(1):10593.##Pharmaceuticals (Basel). 2021 Sep 23;14(10):959. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P.##Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M." "Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors.##Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies." 10.1038/s41598-017-10492-x##10.3390/ph14100959 Anti-Influenza virus DRAVPe01650 SLDC 4 Peptide 15(lactoferrin 422-425) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.5 ± 0.001 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=4.6 ± 0.05 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=4.3 ± 0.03 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01650.cif Linear Acylation Amidation None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 436.48 C16H28N4O8S AEFGHIKMNPQRTVWY CDLS 3.8 0 1 -1 2 1 50 -592 1.9 hour >20 hour >10 hour 97.5 0 0 28878220##34681184 Sci Rep. 2017 Sep 6;7(1):10593.##Pharmaceuticals (Basel). 2021 Sep 23;14(10):959. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P.##Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M." "Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors.##Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies." 10.1038/s41598-017-10492-x##10.3390/ph14100959 Anti-Influenza virus DRAVPe01649 SKHSSLDC 8 Peptide 16(lactoferrin 418-425) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=80 ± 0.19 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=0.1 ± 0.001 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.0 ± 0.45 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01649.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 875.95 C34H57N11O14S AEFGIMNPQRTVWY S 6.46 2 1 1 4 1 -83.75 -2293 1.9 hour >20 hour >10 hour 48.75 0 0 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01648 VLRP 4 Peptide 14(lactoferrin 426–429) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.45 ± 0.1 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=1 ± 0.05 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=250 ± 0.42 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01648.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 483.61 C22H41N7O5 ACDEFGHIKMNQSTWY LPRV 9.72 1 0 1 0 2 47.5 -596 100 hour >20 hour >10 hour 170 0 0 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01647 SLDCVLRP 8 Peptide 13(lactoferrin 422–429) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.3 ± 0.5 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=2.5± 0.37 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=300± 0.2 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01647.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 902.08 C38H67N11O12S AEFGHIKMNQTWY L 5.55 1 1 0 2 3 48.75 -1188 1.9 hour >20 hour >10 hour 133.75 0 0 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01646 KSETKN 6 Peptide 8(lactoferrin 633-638) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.5 ± 0.01 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=500 ± 0.46 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=400.000 ± 210 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01646.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 705.77 C28H51N9O12 ACDFGHILMPQRVWY K 8.59 2 1 1 3 0 -271.67 -3052 1.3 hour 3 min 2 min 0 0 0 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01645 TNGESTADWAKN 12 Peptide 6(lactoferrin 552-563) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=400 ±0.02 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=50.000 ± 230 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=10.000± 120 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01645.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 1293.31 C53H80N16O22 CFHILMPQRVY ANT 4.37 1 2 -1 6 3 -148.33 -3601 7.2 hour >20 hour >10 hour 16.67 5500 500 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01644 KANEGLTWNSLKDK 14 Peptide 4(lactoferrin 441–454) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=1± 0.15 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=50.000 ± 250 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=1.000 ± 360 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01644.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 1603.8 C70H114N20O23 CFHIMPQRVY K 8.5 3 2 1 5 4 -136.43 -3651 1.3 hour 3 min 2 min 62.86 5500 423.08 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01643 SKHSSLDCVLRP 12 Peptide 1(lactoferrin 418–429) Synthetic construct P24627 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 3IB0 Influenza virus Orthomyxoviridae Neutralization assay [Ref.28878220]A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=4 ± 0.37 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=3.1 ± 0.12 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.8 ± 0.7 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01643.cif Linear Free Free None L hemagglutinin (HA) "Hemagglutinin is the major glycoprotein component of the viral envelope along with neuraminidase (NA), peptide derived from Lactoferrin binds Influenza A virus hemagglutinin (HA) inhibiting the hemagglutination and infection of major virus subtypes." 1341.55 C56H96N18O18S AEFGIMNQTWY S 7.97 3 1 2 4 3 -40 -2889 1.9 hour >20 hour >10 hour 89.17 0 0 28878220 Sci Rep. 2017 Sep 6;7(1):10593. "Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P." Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. 10.1038/s41598-017-10492-x Anti-Influenza virus DRAVPe01642 AGVSGHGQHGVHG 13 Alloferon-1 [H1A] Synthetic construct P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HHV,CBV2" "Herpesviridae, Picornaviridae" Antiviral assay(cytopathic effect) [Ref.21766388]Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=358.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 187.50 µg/ml." No predicted structure available DRAVPe01642.cif Linear Free Free None L Not found The peptide may inhibit the replication of DNA and RNA viruses. 1199.25 C49H74N20O16 CDEFIKLMNPRTWY G 7.06 3 0 3 6 3 -43.85 -833 4.4 hour >20 hour >10 hour 52.31 0 0 21766388 J Pept Sci. 2011 Nov;17(11):715-9. "Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D." Further studies on the antiviral activity of alloferon and its analogues. 10.1002/psc.1388 "Anti-HHV,Anti-CBV2" DRAVPe01641 RGVSGHGQHGVHG 13 Alloferon-1 [H1R] Synthetic construct P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HHV,CBV2" "Herpesviridae, Picornaviridae" Antiviral assay(cytopathic effect) [Ref.21766388]HHV-1 McIntyre strain:inhibition of virus replication in Vero cells(IC50=321.10 µg/ml);##HHV-1:inhibition of virus replication in Vero cells(IC50=277.50 µg/ml);inhibition of virus replication in HEp-2 cells(IC50=602.18 µg/ml);##Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=577.73 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=167.71 µg/ml);##CVB2:inhibition of virus replication in LLC-MK2 cells(IC50=355.18 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 143.75 µg/ml." No predicted structure available DRAVPe01641.cif Linear Free Free None L Not found The peptide may inhibit the replication of DNA and RNA viruses. 1284.36 C52H81N23O16 ACDEFIKLMNPTWY G 9.77 4 0 4 6 2 -92.31 -2506 1 hour 2 min 2 min 44.62 0 0 21766388 J Pept Sci. 2011 Nov;17(11):715-9. "Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D." Further studies on the antiviral activity of alloferon and its analogues. 10.1002/psc.1388 "Anti-HHV,Anti-CBV2" DRAVPe01640 KGVSGHGQHGVHG 13 Alloferon-1 [H1K] Synthetic construct P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HHV,CBV2" "Herpesviridae, Picornaviridae" Antiviral assay(cytopathic effect) [Ref.21766388]HHV-1 McIntyre strain:inhibition of virus replication in Vero cells(IC50=147.09 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=241.90 µg/ml);##HHV-1:inhibition of virus replication in Vero cells(IC50=9.19 µg/ml);inhibition of virus replication in HEp-2 cells(IC50=12.98 µg/ml);##Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=157.73 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=107.04 µg/ml);##CVB2:inhibition of virus replication in LLC-MK2 cells(IC50=190.67 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=74.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 218.75 µg/ml." No predicted structure available DRAVPe01640.cif Linear Free Free None L Not found The peptide may inhibit the replication of DNA and RNA viruses. 1256.35 C52H81N21O16 ACDEFILMNPRTWY G 8.77 4 0 4 6 2 -87.69 -1569 1.3 hour 3 min 2 min 44.62 0 0 21766388 J Pept Sci. 2011 Nov;17(11):715-9. "Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D." Further studies on the antiviral activity of alloferon and its analogues. 10.1002/psc.1388 "Anti-HHV,Anti-CBV2" DRAVPe01639 GQGKAHNGRLITANP 15 DENV Envelope glycoprotein (340 – 354) Synthetic construct(derived from DENV Envelope glycoprotein) Q5UB51##P17763 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Focus-forming assay (FFA) "[Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(83%±3.72% inhibition at 50 μM,IC50=33 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. No predicted structure available DRAVPe01639.cif Linear Free Free None L E protein "The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry." 1533.71 C64H108N24O20 CDEFMSVWY G 11 3 0 3 6 4 -91.33 -3024 30 hour >20 hour >10 hour 65.33 0 0 30508603 Virus Res. 2019 Jan 15;260:142-150. "John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P." In vitro analysis of synthetic peptides in blocking the entry of dengue virus. 10.1016/j.virusres.2018.11.016 Anti-DENV DRAVPe01638 DRGWGNGCGLFG 12 DENV Envelope glycoprotein (98-109) Synthetic construct(derived from DENV Envelope glycoprotein) Q5UB51##P17763 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus-forming assay (FFA) "[Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(88%±3.89% inhibition at 50 μM,IC50=10 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. No predicted structure available DRAVPe01638.cif Linear Free Free None L E protein "The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry." 1238.34 C53H75N17O16S AEHIKMPQSTVY G 5.83 1 1 0 7 3 -44.17 -1407 1.1 hour 3 min >10 hour 32.5 5500 500 30508603 Virus Res. 2019 Jan 15;260:142-150. "John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P." In vitro analysis of synthetic peptides in blocking the entry of dengue virus. 10.1016/j.virusres.2018.11.016 Anti-DENV DRAVPe01637 LEHGSCVTTMAKDKPTL 17 DENV Envelope glycoprotein (25-41) Synthetic construct(derived from DENV Envelope glycoprotein) Q5UB51##P17763 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus-forming assay (FFA) "[Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(58%±2.55% inhibition at 50 μM,IC50=10 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. No predicted structure available DRAVPe01637.cif Linear Free Free None L E protein "The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry." 1831.13 C77H131N21O26S2 FINQRWY T 6.74 3 2 1 6 4 -28.82 -2214 5.5 hour 3 min 2 min 68.82 0 0 30508603 Virus Res. 2019 Jan 15;260:142-150. "John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P." In vitro analysis of synthetic peptides in blocking the entry of dengue virus. 10.1016/j.virusres.2018.11.016 Anti-DENV DRAVPe01636 RRRRRRRXPLSPPLRNTHPQAMQWNSTTF 29 7R-Ahx-HBV Large envelope protein (96-116) Synthetic construct P03138 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae FQ-PCR [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=6.5 ± 1.5 μM;EC90=41.4 ±8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21144865]HepG2.2.15:LC50=515.9± 43.8 μM. No predicted structure available DRAVPe01636.cif Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L DNA The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. 3628.37 C150H245N59O37S CDEGIKVY R 12.85 9 0 9 7 5 -172.76 -14358 1 hour 2 min 2 min 30.34 5500 196.43 21144865 Antiviral Res. 2011 Jan;89(1):109-14. "Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X." Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. 10.1016/j.antiviral.2010.12.001 Anti-HBV DRAVPe01635 RRRRRRRXLDPAFR 14 7R-Ahx-HBV Large envelope protein (19-24) Synthetic construct P03138 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae FQ-PCR [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=3.0 ± 1.0 μM;EC90=10.9 ± 3.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21144865]No cytotoxicity was observed at 1mM of peptide concentration against HepG2.2.15. No predicted structure available DRAVPe01635.cif Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L DNA The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. 1922.47 C75H133N37O15 CEGHIKMNQSTVWY R 12.48 8 1 7 0 3 -233.57 -11837 1 hour 2 min 2 min 35 0 0 21144865 Antiviral Res. 2011 Jan;89(1):109-14. "Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X." Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. 10.1016/j.antiviral.2010.12.001 Anti-HBV DRAVPe01633 RRRRRRRXPTSNHSPTSCPPTCPGYRWMCLRRF 33 7R-Ahx-HBV Large envelope protein (219-243) Synthetic construct P03138 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae FQ-PCR [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=12.8 ± 2.0 μM;EC90=85.6 ± 9.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21144865]HepG2.2.15:LC50=457.9 ± 41.0 μM. No predicted structure available DRAVPe01633.cif Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L DNA The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. 4099.99 C167H270N66O40S4 ADEIKQV R 12 11 0 11 12 3 -153.94 -16119 1 hour 2 min 2 min 11.82 7115 222.34 21144865 Antiviral Res. 2011 Jan;89(1):109-14. "Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X." Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. 10.1016/j.antiviral.2010.12.001 Anti-HBV DRAVPe01634 RRRRRRRXGSLLGRMKGA 18 7R-Ahx-P3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HBV Hepadnaviridae FQ-PCR [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=2.5 ±1.0 μM;EC90=8.6± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21144865]HepG2.2.15:LC50=828.7 ± 50.3 μM. No predicted structure available DRAVPe01634.cif Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L DNA The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. 2193.84 C83H158N42O18S CDEFHINPQTVWY R 12.85 9 0 9 4 3 -170 -11149 1 hour 2 min 2 min 48.89 0 0 21144865 Antiviral Res. 2011 Jan;89(1):109-14. "Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X." Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. 10.1016/j.antiviral.2010.12.001 Anti-HBV DRAVPe01632 EEQAKTFLDKFNHEAEDLFYQSSGLGKGDFR 31 P6(ACE2 (4-26)-G-ACE2 (333-339)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=0.1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01632.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 3607.89 C161H236N42O53 CIMPVW EF 4.7 5 7 -2 8 9 -106.45 -8374 1 hour 30 min >10 hour 44.19 1490 49.67 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01631 EEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEE 36 P5(ACE2 (4-39)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=6 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01631.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 4313.57 C192H275N47O67 CGMPRV E 4.16 3 8 -5 12 11 -106.39 -9351 1 hour 30 min >10 hour 51.67 8480 242.29 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01630 EEQAKTFLDKFNHEAEDLFYQSS 23 P4(ACE2 (4-26)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=50 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01630.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 2776.95 C124H178N30O43 CGIMPRVW E 4.35 3 6 -3 5 7 -115.22 -6527 1 hour 30 min >10 hour 42.61 1490 67.73 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01629 NHEAEDLFY 9 P3(ACE2 (15-23)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(30% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01629.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 1137.17 C51H68N12O18 CGIKMPQRSTVW E 4.13 1 3 -2 2 3 -112.22 -2407 1.4 hour 3 min >10 hour 54.44 1490 186.25 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01628 DKFNHEAED 9 P2(ACE2 (12-20)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(40% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01628.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 1104.1 C46H65N13O19 CGILMPQRSTVWY DE 4.31 2 4 -2 1 2 -222.22 -4312 1.1 hour 3 min >10 hour 11.11 0 0 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01627 EEQAKTFLDK 10 P1(ACE2 (4-13)) Synthetic construct(derived from angiotensin-converting enzyme 2) Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Pseudovirus infection assay [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(25% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01627.cif Linear Free Free None L spike glycoprotein "Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry." 1208.33 C53H85N13O19 CGHIMNPRSVWY EK 4.68 2 3 -1 1 3 -141 -3184 1 hour 30 min >10 hour 49 0 0 16510163 Virology. 2006 Jun 20;350(1):15-25. "Han DP, Penn-Nicholson A, Cho MW." Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. 10.1016/j.virol.2006.01.029 Anti-SARS-CoV DRAVPe01625 HAKFWW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01625.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 874.01 C46H55N11O7 CDEGILMNPQRSTVY W 8.76 2 0 2 0 4 -71.67 -76 3.5 hour 10 min >10 hour 16.67 11000 2200 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01626 HCAFWW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=49 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01626.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 848.98 C43H48N10O7S DEGIKLMNPQRSTVY W 6.73 1 0 1 1 4 35 607 3.5 hour 10 min >10 hour 16.67 11000 2200 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe00001 EEHEKYHSNW 10 NL1 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00001 DRAVPe00001.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1358.39 C60H79N17O20 ACDFGILMPQRTV E 5.33 3 3 0 3 1 -273 -4315 1 hour 30 min >10 hour 0 6990 776.67 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00002 ASCDKCQLKG 10 NL2 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00002 DRAVPe00002.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1052.23 C41H73N13O15S2 EFHIMNPRTVWY CK 8.09 2 1 1 4 2 -54 -1853 4.4 hour >20 hour >10 hour 49 125 13.89 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00003 HGQVDCSPGIWQLDCTH 17 NL3 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=1000 µM);inhibition of strand transfer catalyzed by integrase(IC50=1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00003 DRAVPe00003.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1896.08 C80H118N24O26S2 AEFKMNRY CDGHQ 5.05 2 2 0 6 4 -45.29 -2316 3.5 hour 10 min >10 hour 62.94 5625 351.56 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00004 VHVASGY 7 NL4 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00004 DRAVPe00004.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 731.81 C33H49N9O10 CDEFIKLMNPQRTW V 6.71 1 0 1 3 3 64.29 263 100 hour >20 hour >10 hour 97.14 1490 248.33 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00005 PAETGQET 8 NL5 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00005 DRAVPe00005.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 831.83 C33H53N9O16 CDFHIKLMNRSVWY ET 3.8 0 2 -2 3 1 -151.25 -2155 >20 hour >20 hour ? 12.5 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00006 TAYFLLKLAGRW 12 NL-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=21±7 µM);inhibition of strand transfer catalyzed by integrase(IC50=2.7±1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00006 DRAVPe00006.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1438.74 C71H107N17O15 CDEHIMNPQSV L 9.99 2 0 2 3 7 50.83 145 7.2 hour >20 hour >10 hour 114.17 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00007 GRWPVKT 7 NL7 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00007 DRAVPe00007.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 843 C39H62N12O9 ACDEFHILMNQSY GKPRTVW 11 2 0 2 2 2 -111.43 -1573 30 hour >20 hour >10 hour 41.43 5500 916.67 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00008 HTDNGSNF 8 NL8 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00008 DRAVPe00008.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 890.86 C36H50N12O15 ACEIKLMPQRVWY N 5.08 1 1 0 5 1 -160 -2871 3.5 hour 10 min >10 hour 0 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00009 ACWWAGIKQEF 11 NL-9 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=95±9 µM);inhibition of strand transfer catalyzed by integrase(IC50=56±5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00009 DRAVPe00009.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1338.55 C64H87N15O15S DHLMNPRSTVY AW 6.04 1 1 0 2 6 2.73 50 4.4 hour >20 hour >10 hour 53.64 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00010 FGIPYNPQSQ 10 NL10 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00010 DRAVPe00010.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1150.26 C53H75N13O16 ACDEHKLMRTVW PQ 5.52 0 0 0 4 2 -89 -1242 1.1 hour 3 min 2 min 39 1490 165.56 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00011 ESMNKELKKI 10 NL11 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00011 DRAVPe00011.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1219.46 C52H94N14O17S ACDFGHPQRTVWY K 8.59 3 2 1 2 2 -128 -2812 1 hour 30 min >10 hour 78 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00012 VRDQAEHLKT 10 NL12 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00012 DRAVPe00012.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1196.33 C50H85N17O17 CFGIMNPSWY ADEHKLQRTV 6.72 3 2 1 1 3 -130 -3800 100 hour >20 hour >10 hour 78 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00013 FIHNFKRK 8 NL13 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00013 DRAVPe00013.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1089.31 C52H80N16O10 ACDEGLMPQSTVWY FK 11.17 4 0 4 1 3 -111.25 -2644 1.1 hour 3 min 2 min 48.75 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00014 GYSAGERIVD 10 NL14 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00014 DRAVPe00014.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1066.14 C45H71N13O17 CFHKLMNPQTW G 4.37 1 2 -1 4 3 -39 -2134 30 hour >20 hour >10 hour 78 1490 165.56 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00015 WKGPAKLLWK 10 NL15 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00015 DRAVPe00015.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1226.53 C62H95N15O11 CDEFHIMNQRSTVY K 10.3 3 0 3 1 5 -61 60 2.8 hour 3 min 2 min 88 11000 1222.22 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00016 VPRRKAKI 8 NL16 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00016 DRAVPe00016.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 967.23 C43H82N16O9 CDEFGHLMNQSTWY KR 12.02 4 0 4 0 3 -98.75 -3017 100 hour >20 hour >10 hour 97.5 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00017 AAYFLLKLAGRW 12 NL6-T1A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=100±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=47±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00017 DRAVPe00017.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1408.71 C70H105N17O14 CDEHIMNPQSTV AL 9.99 2 0 2 2 8 71.67 583 4.4 hour >20 hour >10 hour 122.5 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00018 TAAFLLKLAGRW 12 NL6-Y3A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=193±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=119±11 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00018 DRAVPe00018.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1346.64 C65H103N17O14 CDEHIMNPQSVY AL 11 2 0 2 2 8 76.67 340 7.2 hour >20 hour >10 hour 122.5 5500 500 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00019 TAYALLKLAGRW 12 NL6-F4A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00019 DRAVPe00019.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1362.64 C65H103N17O15 CDEFHIMNPQSV AL 9.99 2 0 2 3 7 42.5 28 7.2 hour >20 hour >10 hour 122.5 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00020 TAYFALKLAGRW 12 NL6-L5A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=115±21 µM);inhibition of strand transfer catalyzed by integrase(IC50=51±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00020 DRAVPe00020.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1396.65 C68H101N17O15 CDEHIMNPQSV A 9.99 2 0 2 3 7 34.17 -166 7.2 hour >20 hour >10 hour 90 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00021 TAYFLAKLAGRW 12 NL6-L6A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00021 DRAVPe00021.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1396.65 C68H101N17O15 CDEHIMNPQSV A 9.99 2 0 2 3 7 34.17 -166 7.2 hour >20 hour >10 hour 90 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00022 TAYFLLALAGRW 12 NL6-K7A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=113±15 µM);inhibition of strand transfer catalyzed by integrase(IC50=56±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00022 DRAVPe00022.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1381.64 C68H100N16O15 CDEHIKMNPQSV AL 8.41 1 0 1 3 8 98.33 881 7.2 hour >20 hour >10 hour 122.5 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00023 TAYFLLKAAGRW 12 NL6-L8A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50=106±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00023 DRAVPe00023.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1396.65 C68H101N17O15 CDEHIMNPQSV A 9.99 2 0 2 3 7 34.17 -166 7.2 hour >20 hour >10 hour 90 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00024 TAYFLLKLAARW 12 NL6-G10A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=118±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=19±6 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00024 DRAVPe00024.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1452.76 C72H109N17O15 CDEGHIMNPQSV AL 9.99 2 0 2 2 8 69.17 232 7.2 hour >20 hour >10 hour 122.5 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00025 TAYFLLKLAGAW 12 NL6-R11A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=83±15 µM);inhibition of strand transfer catalyzed by integrase(IC50=80±8 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00025 DRAVPe00025.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1353.63 C68H100N14O15 CDEHIMNPQRSV AL 8.26 1 0 1 3 8 103.33 1818 7.2 hour >20 hour >10 hour 122.5 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00026 TAYFLLKLAGRA 12 NL6-W12A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00026 DRAVPe00026.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1323.6 C63H102N16O15 CDEHIMNPQSVW AL 9.99 2 0 2 3 7 73.33 93 7.2 hour >20 hour >10 hour 122.5 1490 135.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00027 AAWWAGIKQEF 11 NL9-C2A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=277±47 µM);inhibition of strand transfer catalyzed by integrase(IC50=311±19 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00027 DRAVPe00027.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1306.49 C64H87N15O15 CDHLMNPRSTVY A 6.05 1 1 0 1 7 -3.64 103 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00028 ACAWAGIKQEF 11 NL9-W3A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=33±6 µM);inhibition of strand transfer catalyzed by integrase(IC50=34±8 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00028 DRAVPe00028.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1223.41 C56H82N14O15S DHLMNPRSTVY A 6.04 1 1 0 2 6 27.27 -2 4.4 hour >20 hour >10 hour 62.73 5500 550 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00029 ACWAAGIKQEF 11 NL9-W4A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00029 DRAVPe00029.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1223.41 C56H82N14O15S DHLMNPRSTVY A 6.04 1 1 0 2 6 27.27 -2 4.4 hour >20 hour >10 hour 62.73 5500 550 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00030 ACWWAAIKQEF 11 NL9-G6A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=90±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=43±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00030 DRAVPe00030.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1352.57 C65H89N15O15S DGHLMNPRSTVY A 6.04 1 1 0 1 7 22.73 137 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00031 ACWWAGAKQEF 11 NL9-I7A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00031 DRAVPe00031.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1296.47 C61H81N15O15S DHILMNPRSTVY A 6.04 1 1 0 2 6 -21.82 -261 4.4 hour >20 hour >10 hour 27.27 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00032 ACWWAGIAQEF 11 NL9-K8A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=62±13 µM);inhibition of strand transfer catalyzed by integrase(IC50=55±7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00032 DRAVPe00032.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1281.45 C61H80N14O15S DHKLMNPRSTVY A 4 0 1 -1 2 7 54.55 786 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00033 ACWWAGIKAEF 11 NL9-Q9A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00033 DRAVPe00033.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1281.49 C62H84N14O14S DHLMNPQRSTVY A 6.04 1 1 0 2 7 50.91 785 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00034 ACWWAGIKQAF 11 NL9-E10A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00034 DRAVPe00034.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1280.51 C62H85N15O13S DEHLMNPRSTVY A 8.27 1 0 1 2 7 50.91 912 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00035 ACWWAGIKQEA 11 NL9-F11A Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=245±13 µM);inhibition of strand transfer catalyzed by integrase(IC50=206±12 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00035 DRAVPe00035.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1262.45 C58H83N15O15S DFHLMNPRSTVY A 6.04 1 1 0 2 6 -6.36 -67 4.4 hour >20 hour >10 hour 62.73 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00036 TASFLLKLAGRW 12 NL6-1 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=186±23 µM);inhibition of strand transfer catalyzed by integrase(IC50=11±2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00036 DRAVPe00036.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1362.64 C65H103N17O15 CDEHIMNPQVY L 11 2 0 2 3 7 55 -181 7.2 hour >20 hour >10 hour 114.17 5500 500 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00037 TAYFLLILAGRW 12 NL6-2 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=4.1±0.7 µM);inhibition of strand transfer catalyzed by integrase(IC50=3.0±1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00037 DRAVPe00037.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1423.72 C71H106N16O15 CDEHKMNPQSV L 8.41 1 0 1 3 8 120.83 1192 7.2 hour >20 hour >10 hour 146.67 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00038 TAYFLLKLAGRL 12 NL6-3 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=315±30 µM);inhibition of strand transfer catalyzed by integrase(IC50=38±2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00038 DRAVPe00038.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1365.68 C66H108N16O15 CDEHIMNPQSVW L 9.99 2 0 2 3 7 90 404 7.2 hour >20 hour >10 hour 146.67 1490 135.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00039 ASWWAGIKQEF 11 NL9-1 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=294±41 µM);inhibition of strand transfer catalyzed by integrase(IC50=163±15 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00039 DRAVPe00039.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1322.49 C64H87N15O16 CDHLMNPRTVY AW 6.05 1 1 0 2 6 -27.27 -418 4.4 hour >20 hour >10 hour 53.64 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00040 ACGWAGIKQEF 11 NL9-2 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=46±5 µM);inhibition of strand transfer catalyzed by integrase(IC50=16±2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00040 DRAVPe00040.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1209.38 C55H80N14O15S DHLMNPRSTVY AG 6.04 1 1 0 3 5 7.27 -89 4.4 hour >20 hour >10 hour 53.64 5500 550 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00041 ACWGAGIKQEF 11 NL9-3 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00041 DRAVPe00041.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1209.38 C55H80N14O15S DHLMNPRSTVY AG 6.04 1 1 0 3 5 7.27 -89 4.4 hour >20 hour >10 hour 53.64 5500 550 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00042 ACWWAGIRQEF 11 NL9-4 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00042 DRAVPe00042.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1366.56 C64H87N17O15S DHKLMNPSTVY AW 6.04 1 1 0 2 6 -2.73 -887 4.4 hour >20 hour >10 hour 53.64 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00043 TAYFLL 6 NL6-4 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=500 µM);inhibition of strand transfer catalyzed by integrase(IC50=500 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00043 DRAVPe00043.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 726.87 C37H54N6O9 CDEGHIKMNPQRSVW L 5.18 0 0 0 2 4 170 1192 7.2 hour >20 hour >10 hour 146.67 1490 298 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00044 YFLLKL 6 NL6-5 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=20 µM);inhibition of strand transfer catalyzed by integrase(IC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00044 DRAVPe00044.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 796.02 C42H65N7O8 ACDEGHIMNPQRSTVW L 8.59 1 0 1 1 4 150 1205 2.8 hour 10 min 2 min 195 1490 298 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00045 KLAGRW 6 NL6-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00045 DRAVPe00045.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 729.88 C34H55N11O7 CDEFHIMNPQSTVY AGKLRW 11 2 0 2 1 3 -68.33 -1047 1.3 hour 3 min 2 min 81.67 5500 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00046 ACWWAG 6 NL9-5 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00046 DRAVPe00046.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 692.79 C33H40N8O7S DEFHIKLMNPQRSTVY AW 5.56 0 0 0 2 4 65 1050 4.4 hour >20 hour >10 hour 33.33 11000 2200 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00047 WAGIKQ 6 NL9-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00047 DRAVPe00047.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 701.82 C33H51N9O8 CDEFHLMNPRSTVY AGIKQW 8.75 1 0 1 1 3 -40 -109 2.8 hour 3 min 2 min 81.67 5500 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00048 IKQEF 5 NL9-7 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00048 DRAVPe00048.cif Linear Free Amidation None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 663.77 C31H49N7O9 ACDGHLMNPRSTVWY EFIKQ 6 1 1 0 0 2 -72 -1000 20 hour 30 min >10 hour 78 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00049 tayfllklagrw 12 DNL-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=65±8 µM);inhibition of strand transfer catalyzed by integrase(IC50=13±1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00049.cif Linear Free Free None D Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1438.74 H-22O-11 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 9.99 0 0 0 0 0 0 0 0 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00050 WRGALKLLFYAT 12 RNL-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=96±2 µM);inhibition of strand transfer catalyzed by integrase(IC50=16±4 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00050 DRAVPe00050.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1438.74 C71H107N17O15 CDEHIMNPQSV L 9.99 2 0 2 3 7 50.83 145 2.8 hour 3 min 2 min 114.17 6990 635.45 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00051 wrgalkllfyat 12 RDNL-6 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.5±1 µM);inhibition of strand transfer catalyzed by integrase(IC50=4.0±1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00051.cif Linear Free Free None D Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1438.74 H-22O-11 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 9.99 0 0 0 0 0 0 0 0 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00052 acwwagikqef 11 DNL-9 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00052.cif Linear Free Free None D Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1338.55 H-20O-10 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 6.04 0 0 0 0 0 0 0 0 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00053 FEQKIGAWWCA 11 RNL-9 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00053 DRAVPe00053.cif Linear Free Free None L Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1338.55 C64H87N15O15S DHLMNPRSTVY AW 5.99 1 1 0 2 6 2.73 50 1.1 hour 3 min 2 min 53.64 11000 1100 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00054 feqkigawwca 11 RDNL-9 Synthetic construct(derived from HIV-1 integrase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase Assay [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00054.cif Linear Free Free None D Integrase "HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer)." 1338.55 H-20O-10 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 5.99 0 0 0 0 0 0 0 0 0 0 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. "Li HY, Zawahir Z, Song LD, Long YQ, Neamati N." Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. 10.1021/jm060307u Anti-HIV DRAVPe00055 DFRELNKRTQDFWEVQLGIP 20 4277(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is very low. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00055 DRAVPe00055.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2491.79 C113H171N31O33 ACHMSY DEFLQR 4.78 3 4 -1 3 7 -95.5 -5871 1.1 hour 3 min >10 hour 73 5500 289.47 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00056 SPAIFQSSMTKILEPFRKQN 20 4285(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=35 µM);inhibition of strand transfer catalyzed by integrase(IC50=270 µM);inhibition of disintegration catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00056 DRAVPe00056.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2322.71 C104H168N28O30S CDGHVWY S 9.99 3 1 2 5 6 -52.5 -3844 1.9 hour >20 hour >10 hour 63.5 0 0 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00057 FRKQNPDIVIYQYMD 15 4286’-1(derived from the DNA-polymerase domain of HIV-1 RT (14-mer) ) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=119 µM);inhibition of strand transfer catalyzed by integrase(IC50=97 µM);inhibition of disintegration catalyzed by integrase(IC50>270 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00057 DRAVPe00057.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 1930.21 C88H132N22O25S ACEGHLSTW DIQY 5.96 2 2 0 3 4 -81.33 -3670 1.1 hour 3 min 2 min 71.33 2980 212.86 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00058 KILEPFRKQNPDIVIYQYMD 20 4286(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=4.8 µM);inhibition of strand transfer catalyzed by integrase(IC50=4.5 µM);inhibition of disintegration catalyzed by integrase(IC50=9.4 µM);##HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00058 DRAVPe00058.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2510.93 C116H180N28O32S ACGHSTW I 6.12 3 3 0 3 6 -64.5 -3922 1.3 hour 3 min 2 min 92.5 2980 156.84 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00059 PDIVIYQYMDDLYVGSDLEI 20 "4287(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),34(derived from the HIV-1 HXB2 Pol region of the viral genome)" Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot assay "[Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=22 µM);inhibition of strand transfer catalyzed by integrase(IC50=54 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM);##HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=6±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=10±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=28±2 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=23±2 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=41±2 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=20 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=5 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00059 DRAVPe00059.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2361.65 C108H161N21O36S ACFHKNRTW D 3.28 0 5 -5 5 7 18.5 -1508 >20 hour >20 hour ? 126.5 4470 235.26 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. 10.1074/jbc.M414679200##10.1016/j.bmcl.2006.07.022 Anti-HIV DRAVPe00060 DIQKLVGKLNWASQIYPGIK 20 4295(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00060 DRAVPe00060.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2271.69 C106H171N27O28 CEFHMRT IK 9.53 3 1 2 5 8 -20 -1197 1.1 hour 3 min >10 hour 117 6990 367.89 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00061 IAEIQKQGQGQWTYQIYQEP 20 4302(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00061 DRAVPe00061.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2408.65 C109H162N28O34 CDFHLMNRSV Q 4.53 1 2 -1 5 5 -116 -3448 20 hour 30 min >10 hour 63.5 8480 446.32 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00062 KQLTEAVQKITTESIVIWGK 20 "4306(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),53(derived from the HIV-1 HXB2 Pol region of the viral genome)" Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay "[Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=7±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=4±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=51±7 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=31±7 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=29±1 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=15 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=10 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00062 DRAVPe00062.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2272.67 C103H174N26O31 CDFHMNPRY IKT 8.5 3 2 1 5 8 -12 -1962 1.3 hour 3 min 2 min 112 5500 289.47 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. 10.1074/jbc.M414679200##10.1016/j.bmcl.2006.07.022 Anti-HIV DRAVPe00063 TPKFKLPIQKETWETWWTEY 20 4308(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00063 DRAVPe00063.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2611.98 C127H179N27O33 ACDGHMNRSV T 5.9 3 3 0 5 6 -123 -3323 7.2 hour >20 hour >10 hour 39 17990 946.84 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00064 ETWETWWTEYWQATWIPEWE 20 "4309(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),56(derived from the HIV-1 HXB2 Pol region of the viral genome)" Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay "[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=6±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=13±2 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=9±2 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=126±3 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=27±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=25 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=5 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00064 DRAVPe00064.cif Linear Free Free None L Integrase "Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication." 2757.95 C135H165N27O37 CDFGHKLMNRSV W 3.51 0 5 -5 5 8 -129 -2930 1 hour 30 min >10 hour 24.5 34490 1815.26 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. 10.1074/jbc.M414679200##10.1016/j.bmcl.2006.07.022 Anti-HIV DRAVPe00065 GYVTNRGRQKVVTLTDTTNQ 20 4315(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is very low No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00065 DRAVPe00065.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2251.48 C94H159N31O33 ACEFHIMPSW T 9.99 3 1 2 10 4 -98 -6254 30 hour >20 hour >10 hour 63 1490 78.42 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00066 VVTLTDTTNQKTELQAIYLA 20 4316(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00066 DRAVPe00066.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2222.52 C98H164N24O34 CFGHMPRSW T 4.37 1 2 -1 7 8 8.5 -2041 100 hour >20 hour >10 hour 117 1490 78.42 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00067 KTELQAIYLALQDSGLEVNI 20 4317(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00067 DRAVPe00067.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2218.53 C99H164N24O33 CFHMPRW L 4.14 1 3 -2 5 9 19.5 -1360 1.3 hour 3 min 2 min 141.5 1490 78.42 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00068 LQDSGLEVNIVTDSQYALGI 20 "4318(derived from the RNase H domain of HIV-1 RT (20-mes)),65(derived from the HIV-1 HXB2 Pol region of the viral genome)" Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay "[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=11±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50>167 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=36±14 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=18±3 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=4±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50>167 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=20 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00068 DRAVPe00068.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2135.36 C93H151N23O34 CFHKMPRW L 3.49 0 3 -3 7 8 26 -1511 5.5 hour 3 min 2 min 131.5 1490 78.42 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. 10.1074/jbc.M414679200##10.1016/j.bmcl.2006.07.022 Anti-HIV DRAVPe00069 VTDSQYALGIIQAQPDQSES 20 4319(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00069 DRAVPe00069.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2150.28 C91H144N24O36 CFHKMNRW Q 3.49 0 3 -3 6 6 -51.5 -3596 100 hour >20 hour >10 hour 83 1490 78.42 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00070 IQAQPDQSESELVNQIIEQL 20 4320(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50>120 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00070 DRAVPe00070.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2282.49 C97H160N26O37 CFGHKMRTWY Q 3.5 0 4 -4 3 7 -55.5 -3984 20 hour 30 min >10 hour 117 0 0 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00071 ELVNQIIEQLIKKEKVYLAW 20 "4321(derived from the RNase H domain of HIV-1 RT (20-mes)),64(derived from the HIV-1 HXB2 Pol region of the viral genome)" Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot assay "[Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=6.9 µM);inhibition of strand transfer catalyzed by integrase(IC50=5 µM);inhibition of disintegration catalyzed by integrase(IC50>100 µM);##HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=15±2 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=14±4 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=113±11 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=83±5 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=136±5 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=7±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=45 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=15 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00071 DRAVPe00071.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2457.94 C116H189N27O31 CDFGHMPRST EIKL 6.32 3 3 0 2 10 1 -1320 1 hour 30 min >10 hour 151 6990 367.89 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. 10.1074/jbc.M414679200##10.1016/j.bmcl.2006.07.022 Anti-HIV DRAVPe00072 NQIIEQLIKKEKVY 14 4321’-1( derived from the RNase H domain of HIV-1 RT (15-mer)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>240 µM);inhibition of strand transfer catalyzed by integrase(IC50>240 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00072 DRAVPe00072.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 1746.08 C80H136N20O23 ACDFGHMPRSTW IK 8.43 3 2 1 2 5 -64.29 -2441 1.4 hour 3 min >10 hour 132.14 1490 114.62 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00073 IKKEKVYLAWVPAHKGIGN 19 4322(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50>120 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00073 DRAVPe00073.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2151.58 C102H163N27O24 CDFMQRST K 9.83 5 1 4 4 8 -29.47 -978 20 hour 30 min >10 hour 102.63 6990 388.33 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00074 EQVDKLVSAGIRKVLFLDGI 20 4324(derived from the RNase H domain of HIV-1 RT (20-mes)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00074 DRAVPe00074.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 2200.61 C100H170N26O29 CHMNPTWY LV 6.22 3 3 0 3 10 48.5 -1582 1 hour 30 min >10 hour 146 0 0 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00075 ESELVSQIIEQLIKK 15 5628(derived from RNase H domain of HIV-1 RT (15-mers)) Synthetic construct(derived from HIV-1 Reverse Transcriptase) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot assay [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50=60 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00075 DRAVPe00075.cif Linear Free Free None L Integrase Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. 1757.06 C78H137N19O26 ACDFGHMNPRTWY EI 4.79 2 3 -1 2 6 -10.67 -2077 1 hour 30 min >10 hour 149.33 0 0 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. "Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A." Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. 10.1074/jbc.M414679200 Anti-HIV DRAVPe00076 LQQLLFIHFRIGCQH 15 Vpr 15 Synthetic construct(HIV-1 gene product) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.20586421]HIV-1:inhibition of strand transfer catalyzed by integrase(IC50=5.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00076 DRAVPe00076.cif Linear Free Free None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 1853.22 C86H133N25O19S ADEKMNPSTVWY LQ 8.27 3 0 3 2 7 44.67 -808 5.5 hour 3 min 2 min 130 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00077 TNWLWYIKIFIMIV 14 Env4-4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.20586421]HIV-1:inhibition of strand transfer catalyzed by integrase(IC50=1.9 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00077 DRAVPe00077.cif Linear Free Free None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 1840.3 C94H138N18O18S ACDEGHPQRS I 8.26 1 0 1 3 9 139.29 2373 7.2 hour >20 hour >10 hour 160 12490 960.77 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00078 LQQLLF 6 Vpr-1 Synthetic construct(derived from HIV-1 gene products(Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>11 µM);inhibition of strand transfer catalyzed by integrase(IC50=68±1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00078 DRAVPe00078.cif Linear Acetylation Amidation None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 760.93 C37H60N8O9 ACDEGHIKMNPRSTVWY L 5.52 0 0 0 0 4 120 666 5.5 hour 3 min 2 min 195 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00079 LQQLLFRRRRRRRR 14 Vpr-1 R8 Synthetic construct(derived from HIV-1 gene products(Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=6.1±1.1 µM);inhibition of strand transfer catalyzed by integrase(IC50>11 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00079 DRAVPe00079.cif Linear Acetylation Amidation None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 2010.43 C85H156N40O17 ACDEGHIKMNPSTVWY R 12.85 8 0 8 0 4 -205.71 -11270 5.5 hour 3 min 2 min 83.57 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00080 IHFRIGRRRRRRRR 14 Vpr-2 R8 Synthetic construct(derived from HIV-1 gene products(Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Luciferase assay [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.70±0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.83±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00080 DRAVPe00080.cif Linear Acetylation Amidation None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 1991.39 C83H151N43O15 ACDEKLMNPQSTVWY R 12.9 10 0 10 1 3 -230.71 -12518 20 hour 30 min >10 hour 55.71 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00081 LQQLLFIHFRIGRRRRRRRR 20 Vpr-3 R8 Synthetic construct(derived from HIV-1 gene products(Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase assay [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.004±0.0001 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.008±0.001 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00081 DRAVPe00081.cif Linear Acetylation Amidation None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 2734.31 C120H209N51O23 ACDEKMNPSTVWY R 12.9 10 0 10 1 7 -125.5 -11852 5.5 hour 3 min 2 min 97.5 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00082 EAIIRILQQLLFIHFRIGRRRRRRRR 26 Vpr-4 R8 Synthetic construct(derived from HIV-1 gene products(Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.005±0.002 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.006±0.006 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00082 DRAVPe00082.cif Linear Acetylation Amidation None L Integrase "IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication." 3430.17 C152H266N60O31 CDKMNPSTVWY R 12.6 11 1 10 1 11 -68.46 -12368 1 hour 30 min >10 hour 123.85 0 0 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. "Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H. " Peptide HIV-1 integrase inhibitors from HIV-1 gene products. 10.1021/jm1003528 Anti-HIV DRAVPe00083 TYGDTWAGVEAIIRI 15 Vpr 49-63 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of Rnase H(IC50>>200 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00083 DRAVPe00083.cif Linear Free Free None L Reverse Transcriptase The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1664.88 C76H117N19O23 CFHKLMNPQS I 4.37 1 2 -1 5 7 36 -910 7.2 hour >20 hour >10 hour 110.67 6990 499.29 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00084 TWAGVEAIIRILQQL 15 Vpr 53-67 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.88 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=0.88 µM);inhibit the activity of Rnase H(IC50=6.9 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM);inhibition of strand transfer catalyzed by integrase(IC50=144 µM);inhibition of disintegration catalyzed by integrase(IC50=27 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00084 DRAVPe00084.cif Linear Free Free None L "Integrase,Reverse Transcriptase" The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1711.04 C79H131N21O21 CDFHKMNPSY I 5.66 1 1 0 2 9 79.33 15 7.2 hour >20 hour >10 hour 162.67 5500 392.86 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00085 VEAIIRILQQLLFIH 15 Vpr 57-71 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of Rnase H(IC50=2 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=7.8 µM);inhibition of strand transfer catalyzed by integrase(IC50=16 µM);inhibition of disintegration catalyzed by integrase(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00085 DRAVPe00085.cif Linear Free Free None L "Integrase,Reverse Transcriptase" The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1806.22 C86H144N22O20 CDGKMNPSTWY I 6.72 2 1 1 0 10 133.33 580 100 hour >20 hour >10 hour 208 0 0 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00086 IRILQQLLFIHFRIG 15 Vpr 61-75 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.7 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=1.3 µM);inhibit the activity of Rnase H(IC50=5.25 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=1.3 µM);inhibition of strand transfer catalyzed by integrase(IC50=1 µM);inhibition of disintegration catalyzed by integrase(IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00086 DRAVPe00086.cif Linear Free Free None L "Integrase,Reverse Transcriptase" The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1867.31 C90H147N25O18 ACDEKMNPSTVWY I 12 3 0 3 1 9 102.67 -424 20 hour 30 min >10 hour 182 0 0 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00087 QQLLFIHFRIGCQHS 15 Vpr 65-79 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=33 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=43 µM);inhibit the activity of Rnase H(IC50=16.5 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=76 µM);inhibition of strand transfer catalyzed by integrase(IC50=14 µM);inhibition of disintegration catalyzed by integrase(IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00087 DRAVPe00087.cif Linear Free Free None L "Integrase,Reverse Transcriptase" The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1827.14 C83H127N25O20S ADEKMNPTVWY Q 8.27 3 0 3 3 6 14 -1640 0.8 hour 10 min >10 hour 104 0 0 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00088 FIHFRIGCQHSRIGI 15 Vpr 69-83 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50>>200 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50>>200 µM);inhibit the activity of Rnase H(IC50>>200 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50>>200 µM);inhibition of strand transfer catalyzed by integrase(IC50>>200 µM);inhibition of disintegration catalyzed by integrase(IC50>>200 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00088 DRAVPe00088.cif Linear Free Free None L "Integrase,Reverse Transcriptase" The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. 1784.11 C81H126N26O18S ADEKLMNPTVWY I 10.35 4 0 4 4 6 37.33 -1930 1.1 hour 3 min 2 min 104 0 0 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00089 HFPRIWLHSLGQHIY 15 Vpr 33-47 Synthetic construct(derived from HIV-1 viral protein R (Vpr)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Dot-blot binding assay [Ref.17490682]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=187 µM);inhibition of strand transfer catalyzed by integrase(IC50=41 µM);inhibition of disintegration catalyzed by integrase(IC50=73 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00089 DRAVPe00089.cif Linear Free Free None L Integrase The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and thus inhibit the replication of HIV-1. 1904.21 C92H130N26O19 ACDEKMNTV H 8.77 4 0 4 3 6 -21.33 -1205 3.5 hour 10 min >10 hour 104 6990 499.29 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. "Gleenberg IO, Herschhorn A, Hizi A." Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). 10.1016/j.jmb.2007.03.073 Anti-HIV DRAVPe00090 QLLIRMIYKNILFYLVPGPGHGAEPERRNIKYL 33 I33 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=9 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00090 DRAVPe00090.cif Linear Free Free None L Integrase "The peptide bound tightly to the integrase(IN) and inhibited both in vitro IN activities, containing 3′ end processing and strand transfer." 3913.69 C183H291N49O44S CDSTW L 9.82 6 2 4 8 12 -12.73 -3510 0.8 hour 10 min >10 hour 118.18 4470 139.69 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00091 RMIYKNILFYLVPGPGHGAEPERRNIKYL 29 I29 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=85 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00091 DRAVPe00091.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 3446.08 C160H250N44O39S CDQSTW GILPRY 9.82 6 2 4 8 9 -44.14 -4432 1 hour 2 min 2 min 94.14 4470 159.64 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00092 QLLIRMI 7 LCD278B Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00092 DRAVPe00092.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 886.16 C40H75N11O9S ACDEFGHKNPSTVWY IL 9.75 1 0 1 0 4 150 157 0.8 hour 10 min >10 hour 222.86 0 0 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00093 AEPERRNIKYL 11 EBR24 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=50 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00093 DRAVPe00093.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1388.59 C61H101N19O18 CDFGHMQSTVW ER 8.63 3 2 1 2 3 -147.27 -4414 4.4 hour >20 hour >10 hour 80 1490 149 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00094 LFYLVPGPGH 10 EBR26 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00094 DRAVPe00094.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1099.3 C55H78N12O12 ACDEIKMNQRSTW GLP 6.74 1 0 1 3 4 61 1394 5.5 hour 3 min 2 min 107 1490 165.56 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00095 YQLLIRMIYKNI 12 EBR28 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=5 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50=40 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00095 DRAVPe00095.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1567.95 C74H122N18O17S ACDEFGHPSTVW I 9.7 2 0 2 3 5 41.67 -598 2.8 hour 10 min 2 min 162.5 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00096 YALLIRMIYKNI 12 EBR28[Q2A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=8 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00096 DRAVPe00096.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1510.9 C72H119N17O16S CDEFGHPQSTVW I 9.7 2 0 2 3 6 85.83 137 2.8 hour 10 min 2 min 170.83 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00097 YQALIRMIYKNI 12 EBR28[L3A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=165 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00097 DRAVPe00097.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1525.87 C71H116N18O17S CDEFGHPSTVW I 9.7 2 0 2 3 5 25 -909 2.8 hour 10 min 2 min 138.33 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00098 YQLAIRMIYKNI 12 EBR28[L4A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=14 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00098 DRAVPe00098.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1525.87 C71H116N18O17S CDEFGHPSTVW I 9.7 2 0 2 3 5 25 -909 2.8 hour 10 min 2 min 138.33 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00099 YQLLARMIYKNI 12 EBR28[I5A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=45 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00099 DRAVPe00099.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1525.87 C71H116N18O17S CDEFGHPSTVW ILY 9.7 2 0 2 3 5 19.17 -909 2.8 hour 10 min 2 min 138.33 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00100 YQLLIAMIYKNI 12 EBR28[R6A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=34 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00100 DRAVPe00100.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1482.84 C71H115N15O17S CDEFGHPRSTVW I 8.5 1 0 1 3 6 94.17 1075 2.8 hour 10 min 2 min 170.83 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00101 YQLLIRAIYKNI 12 EBR28[M7A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=70 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00101 DRAVPe00101.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1507.84 C72H118N18O17 CDEFGHMPSTVW I 9.7 2 0 2 3 6 40.83 -652 2.8 hour 10 min 2 min 170.83 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00102 YQLLIRMAYKNI 12 EBR28[I8A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=35 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00102 DRAVPe00102.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1525.87 C71H116N18O17S CDEFGHPSTVW ILY 9.7 2 0 2 3 5 19.17 -909 2.8 hour 10 min 2 min 138.33 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00103 YQLLIRMIAKNI 12 EBR28[Y9A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=40 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00103 DRAVPe00103.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1475.86 C68H118N18O16S CDEFGHPSTVW I 9.99 2 0 2 2 6 67.5 -403 2.8 hour 10 min 2 min 170.83 1490 135.45 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00104 YQLLIRMIYANI 12 EBR28[K10A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=11 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00104 DRAVPe00104.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1510.86 C71H115N17O17S CDEFGHKPSTVW I 8.59 1 0 1 3 6 89.17 138 2.8 hour 10 min 2 min 170.83 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00105 YQLLIRMIYKAI 12 EBR28[N11A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=7 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00105 DRAVPe00105.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1524.93 C73H121N17O16S CDEFGHNPSTVW I 9.7 2 0 2 2 6 85.83 247 2.8 hour 10 min 2 min 170.83 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00106 YQLLIRMIYKNA 12 EBR28[I12A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=11 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00106 DRAVPe00106.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1525.87 C71H116N18O17S CDEFGHPSTVW ILY 9.7 2 0 2 3 5 19.17 -909 2.8 hour 10 min 2 min 138.33 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00107 YQLLIRMIY 9 LCE41 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=5 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50=55 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00107 DRAVPe00107.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1212.52 C58H93N13O13S ACDEFGHKNPSTVW ILY 8.59 1 0 1 2 4 87.78 129 2.8 hour 10 min 2 min 173.33 2980 372.5 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00108 YQLLIRMI 8 LCE40 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=120 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00108 DRAVPe00108.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1049.34 C49H84N12O11S ACDEFGHKNPSTVW IL 8.75 1 0 1 1 4 115 143 2.8 hour 10 min 2 min 195 1490 212.86 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00109 QLLIRMIYKNI 11 LCD278C Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=21 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00109 DRAVPe00109.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1404.78 C65H113N17O15S ACDEFGHPSTVW I 9.99 2 0 2 2 5 57.27 -584 0.8 hour 10 min >10 hour 177.27 1490 149 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00110 YQLLIRPIYKNI 12 ProEBR28 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00110 DRAVPe00110.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 1533.88 C74H120N18O17 ACDEFGHMSTVW I 9.7 2 0 2 3 5 12.5 -833 2.8 hour 10 min 2 min 162.5 2980 270.91 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00111 LSELDDRADALQAGASQFETSAAKLKRKYWWKN 33 C35 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Disintegration assay [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. DRAVPe00111 DRAVPe00111.cif Linear Free Free None L Integrase Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. 3798.23 C169H262N48O52 CHIMPV A 8.38 6 5 1 7 13 -92.12 -8333 5.5 hour 3 min 2 min 65.45 12490 390.31 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. "de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B. " A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. 10.1016/S0022-2836(02)00033-5 Anti-HIV DRAVPe00112 TGEKVWDRGNVTLLCDCP 18 P11(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=439.7 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=162.1 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=484.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=208.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00112 DRAVPe00112.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2006.28 C85H136N24O28S2 AFHIMQSY CDGLTV 4.56 2 3 -1 7 5 -33.89 -3181 7.2 hour >20 hour >10 hour 75.56 5625 330.88 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00113 LPAFCQAIGWGDPITHWS 18 P19(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=369.5 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=46.0 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=194.3 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=71.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00113 DRAVPe00113.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 1999.27 C94H131N23O24S EKMNRVY AGIPW 5.08 1 1 0 5 8 23.33 429 5.5 hour 3 min 2 min 76.11 11000 647.06 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00114 FCQAIGWGDPITHWSHGQ 18 P20(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=347.6 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=70.1 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=125.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=111.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00114 DRAVPe00114.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2040.24 C93H126N26O25S EKLMNRVY G 5.97 2 1 1 6 6 -38.33 -1170 1.1 hour 3 min 2 min 48.89 11000 647.06 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00115 AIGWGDPITHWSHGQNRW 18 P21(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=832.9 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=44.9 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=529.1 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=371.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00115 DRAVPe00115.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2118.3 C97H132N30O25 CEFKLMVY GW 6.96 3 1 2 6 6 -97.78 -2965 4.4 hour >20 hour >10 hour 48.89 16500 970.59 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00116 PITHWSHGQNRWPLSCPQ 18 P23(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=508.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00116 DRAVPe00116.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2144.4 C96H138N30O25S ADEFKMVY P 8.68 3 0 3 6 4 -110.56 -3461 >20 hour >20 hour ? 43.33 11000 647.06 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00117 HGQNRWPLSCPQYVYGSV 18 P25(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=304.4 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00117 DRAVPe00117.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2091.33 C94H135N27O26S ADEFIKMT GPQSVY 8.21 2 0 2 8 4 -70 -2589 3.5 hour 10 min >10 hour 53.89 8480 498.82 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00118 SWFASTGGRDSKIDVWSL 18 P34(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=237.4 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=411.2 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=118.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00118 DRAVPe00118.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2012.21 C91H134N24O28 CEHMNPQY S 5.68 2 2 0 7 7 -26.67 -2887 1.9 hour >20 hour >10 hour 65 11000 647.06 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00119 SDRDTVVELSEWGVPCAT 18 P45(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=141.2 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=48.8 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=505.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=43.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00119 DRAVPe00119.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 1964.13 C83H130N22O31S FHIKMNQY V 3.92 1 4 -3 6 6 -20.56 -3452 1.9 hour >20 hour >10 hour 75.56 5500 323.53 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00120 DTVVELSEWGVPCATCIL 18 P46(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=428.8 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=39.9 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=462.8 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=24.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00120 DRAVPe00120.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 1935.24 C85H135N19O28S2 FHKMNQRY V 3.57 0 3 -3 6 8 88.33 364 1.1 hour 3 min >10 hour 118.89 5625 330.88 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00121 VELSEWGVPCATCILDRR 18 P47(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=330.8 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=58.6 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=140.3 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=20.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00121 DRAVPe00121.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2047.37 C88H143N25O27S2 FHKMNQY CELRV 4.68 2 3 -1 5 7 18.89 -2767 100 hour >20 hour >10 hour 102.78 5625 330.88 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00122 RFPFHRCGAGPKLTKDLE 18 P59(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=529.6 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00122 DRAVPe00122.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2072.42 C93H146N28O24S IMNQSVWY FGKLPR 9.31 5 2 3 4 5 -78.89 -4293 1 hour 2 min 2 min 48.89 0 0 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00123 LVRRRSELMGRRNPVCPG 18 P97(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=537.6 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00123 DRAVPe00123.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2096.5 C86H154N34O23S2 ADFHIKQTWY R 11.82 5 1 4 5 4 -77.22 -6802 5.5 hour 3 min 2 min 75.56 0 0 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00124 LQEVDAGNFIPPPRWLLL 18 P109(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=687.1 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=37.5 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=294.8 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=60.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00124 DRAVPe00124.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 2078.44 C99H152N24O25 CHKMSTY L 4.37 1 2 -1 2 9 21.67 -593 5.5 hour 3 min 2 min 130 5500 323.53 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00125 WVNQLAVLGLPAVDAAVA 18 P124(derived from E2 envelope protein of GB virus C) Synthetic construct(derived from E2 envelope protein of GB virus C) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Gp41-Mediated Cell-Cell Fusion Assay [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=332.7 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=94.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00125 DRAVPe00125.cif Linear Free Free None L membrane "E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner." 1807.12 C84H135N21O23 CEFHIKMRSTY A 3.8 0 1 -1 2 13 132.22 2234 2.8 hour 3 min 2 min 157.22 5500 323.53 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  "Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. " Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. 10.1021/jm100452c Anti-HIV DRAVPe00126 SVSVGMKPSPRP 12 VMI5 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Affinity binding assay [Ref.12480936]HIV-1:binding with vif proteins. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00126 DRAVPe00126.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1241.47 C53H92N16O16S ACDEFHILNQTWY PS 11 2 0 2 4 2 -47.5 -1930 1.9 hour >20 hour >10 hour 48.33 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00127 SNQGGSPLPRSV 12 VMI7 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Affinity binding assay [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=7.43 μM);##The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. DRAVPe00127 DRAVPe00127.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1198.3 C49H83N17O18 ACDEFHIKMTWY S 9.47 1 0 1 6 2 -82.5 -2646 1.9 hour >20 hour >10 hour 56.67 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00128 LPLPAPSFHRTT 12 VMI9 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Affinity binding assay [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=4.84 μM);####The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. DRAVPe00128 DRAVPe00128.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1336.56 C62H97N17O16 CDEGIKMNQVWY P 9.76 2 0 2 3 4 -20.83 -1349 5.5 hour 3 min 2 min 73.33 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00129 SPYPSWSTPAGR 12 VMI16 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Affinity binding assay [Ref.12480936]HIV-1:binding with vif proteins. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00129 DRAVPe00129.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1305.41 C59H84N16O18 CDEFHIKLMNQV PS 8.46 1 0 1 6 2 -110 -2275 1.9 hour >20 hour >10 hour 8.33 6990 635.45 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00130 KPKQIKPPLPSV 12 vif 155-166 Synthetic construct(derived from the proline-enriched C terminus of Vif) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=17.39 μM);####The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. DRAVPe00130 DRAVPe00130.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1331.66 C63H110N16O15 ACDEFGHMNRTWY P 10.3 3 0 3 1 3 -82.5 -1171 1.3 hour 3 min 2 min 89.17 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00131 WQVMIVWQVDRMRIR 15 vif 5-19 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00131 DRAVPe00131.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 2016.46 C91H146N28O20S2 ACEFGHKLNPSTY RV 11.7 3 1 2 0 7 -2.67 -3324 2.8 hour 3 min 2 min 110 11000 785.71 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00132 RHHYESTHPRISSEV 15 vif 41-55 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00132 DRAVPe00132.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1834.97 C78H119N27O25 ACDFGKLMNQW HS 7.03 5 2 3 5 2 -152.67 -6139 1 hour 2 min 2 min 45.33 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00133 ESTHPRISSEVHIPL 15 vif 45-59 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00133 DRAVPe00133.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1701.9 C74H120N22O24 ACDFGKMNQWY S 6.01 3 2 1 4 4 -48 -3183 1 hour 30 min >10 hour 97.33 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00134 HTGERDWHLGQGVSI 15 vif 73-87 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00134 DRAVPe00134.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1691.82 C73H110N24O23 ACFKMNPY G 5.99 3 2 1 5 4 -83.33 -3225 3.5 hour 10 min >10 hour 71.33 5500 392.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00135 RDWHLGQGVSIEWRK 15 vif 77-91 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00135 DRAVPe00135.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1867.1 C84H127N27O22 ACFMNPTY GRW 8.75 4 2 2 3 5 -116.67 -4410 1 hour 2 min 2 min 71.33 11000 785.71 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00136 LGQGVSIEWRKKRYS 15 vif 81-95 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00136 DRAVPe00136.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1807.09 C81H131N25O22 ACDFHMNPT GKRS 10.28 4 1 3 5 4 -106 -4214 5.5 hour 3 min 2 min 71.33 6990 499.29 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00137 RYSTQVDPDLADQLI 15 vif 93-107 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00137 DRAVPe00137.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1733.9 C75H120N20O27 CEFGHKMNW D 3.93 1 3 -2 3 5 -55.33 -3766 1 hour 2 min 2 min 104 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00138 QVDPDLADQLIHLYY 15 vif 97-111 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00138 DRAVPe00138.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1803 C83H123N19O26 CEFGKMNRSTW DL 3.93 1 3 -2 2 6 -20 -1665 0.8 hour 10 min >10 hour 130 2980 212.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00139 DLADQLIHLYYFDCF 15 vif 101-115 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00139 DRAVPe00139.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1876.11 C89H122N18O25S EGKMNPRSTVW DL 3.93 1 3 -2 3 7 40 -791 1.1 hour 3 min >10 hour 110.67 2980 212.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00140 QLIHLYYFDCFSESA 15 vif 105-119 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00140 DRAVPe00140.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1836.05 C86H118N18O25S GKMNPRTVW FLSY 4.35 1 2 -1 5 6 27.33 -900 0.8 hour 10 min >10 hour 84.67 2980 212.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00141 LYYFDCFSESAIRKA 15 vif 109-123 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00141 DRAVPe00141.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1813.06 C84H121N19O24S GHMNPQTVW AFSY 6.06 2 2 0 5 6 2.67 -2238 5.5 hour 3 min 2 min 65.33 2980 212.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00142 ESAIRKAILGHIVSP 15 vif 117-131 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00142 DRAVPe00142.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1590.89 C71H123N21O20 CDFMNQTWY I 8.85 3 1 2 3 7 42.67 -1046 1 hour 30 min >10 hour 136.67 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00143 RKAILGHIVSPRCEY 15 vif 121-135 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00143 DRAVPe00143.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1742.07 C77H128N24O20S DFMNQTW IR 9.31 4 1 3 4 5 -16 -2757 1 hour 2 min 2 min 104 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00144 VSPRCEYQAGHNKVG 15 vif 129-143 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00144 DRAVPe00144.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1644.83 C69H109N23O22S DFILMTW GV 8.18 3 1 2 6 3 -92.67 -3461 100 hour >20 hour >10 hour 45.33 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00145 CEYQAGHNKVGSLQY 15 vif 133-147 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00145 DRAVPe00145.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1696.85 C73H109N21O24S DFIMPRTW GQY 6.74 2 1 1 7 3 -86.67 -2449 1.2 hour >20 hour >10 hour 52 2980 212.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00146 AGHNKVGSLQYLALA 15 vif 137-151 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00146 DRAVPe00146.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1541.77 C69H112N20O20 CDEFIMPRTW AL 8.64 2 0 2 5 7 26.67 18 4.4 hour >20 hour >10 hour 117.33 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00147 KVGSLQYLALAALIT 15 vif 141-155 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00147 DRAVPe00147.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1560.9 C73H125N17O20 CDEFHMNPRW L 8.59 1 0 1 4 9 124.67 1781 1.3 hour 3 min 2 min 169.33 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00148 LQYLALAALITPKKI 15 vif 145-159 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00148 DRAVPe00148.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1656.08 C80H138N18O19 CDEFGHMNRSVW L 9.7 2 0 2 2 9 98 1560 5.5 hour 3 min 2 min 176 1490 106.43 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00149 ALAALITPKKIKPPL 15 vif 149-163 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00149 DRAVPe00149.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1574.03 C76H136N18O17 CDEFGHMNQRSVWY AKLP 10.3 3 0 3 1 8 57.33 1081 4.4 hour >20 hour >10 hour 150 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00150 LITPKKIKPPLPSVT 15 vif 153-167 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00150 DRAVPe00150.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1632.06 C78H138N18O19 ACDEFGHMNQRWY P 10.3 3 0 3 3 5 3.33 -147 5.5 hour 3 min 2 min 123.33 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00151 KKIKPPLPSVTKLTE 15 vif 157-171 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00151 DRAVPe00151.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1679.08 C78H139N19O21 ACDFGHMNQRWY K 10 4 1 3 3 4 -65.33 -1875 1.3 hour 3 min 2 min 97.33 0 0 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00152 PPLPSVTKLTEDRWN 15 vif 161-175 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00152 DRAVPe00152.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1752.99 C79H125N21O24 ACFGHIMQY P 6.49 2 2 0 4 4 -100 -3497 >20 hour >20 hour ? 71.33 5500 392.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00153 SVTKLTEDRWNKPQK 15 vif 165-179 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00153 DRAVPe00153.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1830.07 C80H132N24O25 ACFGHIMY K 9.7 4 2 2 4 3 -179.33 -5653 1.9 hour >20 hour >10 hour 45.33 5500 392.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00154 LTEDRWNKPQKTKGH 15 vif 169-183 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00154 DRAVPe00154.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1838.06 C80H128N26O24 ACFIMSVY K 9.7 5 2 3 4 2 -226 -6089 5.5 hour 3 min 2 min 26 5500 392.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00155 RWNKPQKTKGHRGSH 15 vif 173-187 Synthetic construct(derived from HIV-1 Vif protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00155 DRAVPe00155.cif Linear Free Free None L Vif proteins "Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication." 1817.05 C78H125N31O20 ACDEFILMVY K 12.02 7 0 7 5 1 -259.33 -6975 1 hour 2 min 2 min 0 5500 392.86 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. "Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H." Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. 10.1074/jbc.M210164200 Anti-HIV DRAVPe00156 PTGERVWDRGNVTLLCDCPN 20 P4 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=15.07 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=18.28 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00156 DRAVPe00156.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2245.51 C94H149N29O31S2 AFHIKMQSY CDGLNPRTV 4.56 2 3 -1 8 5 -59 -4782 >20 hour >20 hour ? 68 5625 296.05 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00157 WDRGNVTLLCDCPNGPWVWV 20 P4-7 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=2.59 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=2.66 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00157 DRAVPe00157.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2330.66 C106H152N28O28S2 AEFHIKMQSY VW 4.21 1 2 -1 7 8 -3.5 -1482 2.8 hour 3 min 2 min 82.5 16625 875 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00158 WDRGNVTLLCDCPNGPWVWV 20 P4-7 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(NL4-3):inhibition of HIV replication(IC50=3.0 μM);##HIV-1(YU-2):inhibition of HIV replication(IC50=5.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00158.cif Linear Acetylation Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2330.66 C106H152N28O28S2 AEFHIKMQSY VW 4.21 1 2 -1 7 8 -3.5 -1482 2.8 hour 3 min 2 min 82.5 16625 875 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00159 GPWVWVPAFCQAVGWGDPIT 20 P6 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=16.80 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=3.57 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00159 DRAVPe00159.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2186.52 C106H144N24O25S EHKLMNRSY GPVW 3.8 0 1 -1 5 10 48 1790 30 hour >20 hour >10 hour 73 16500 868.42 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00160 TLLCDCPNGPWVWVPAFCQA 20 P6-1 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=2.36 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=1.29 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00160 DRAVPe00160.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2220.61 C102H146N24O26S3 EHIKMRSY CP 3.8 0 1 -1 6 9 58.5 1049 7.2 hour >20 hour >10 hour 78 11125 585.53 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00161 LCDCPNGPWVWVPAFCQAVG 20 P6-2 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=3.33 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=1.32 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00161 DRAVPe00161.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2162.53 C99H140N24O25S3 EHIKMRSTY CPV 3.8 0 1 -1 6 9 62 1312 5.5 hour 3 min 2 min 73 11125 585.53 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00162 LCDCPNGPWVWVPAFCQAVG 20 P6-2 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(NL4-3):inhibition of HIV replication(IC50=2.3 μM);##HIV-1(YU-2):inhibition of HIV replication(IC50=2.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00162.cif Linear Acetylation Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2162.53 C99H140N24O25S3 EHIKMRSTY CPV 3.8 0 1 -1 6 9 62 1312 5.5 hour 3 min 2 min 73 11125 585.53 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00163 DCPNGPWVWVPAFCQAVGWG 20 P6-3 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=4.00 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=2.00 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00163 DRAVPe00163.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2189.49 C103H137N25O25S2 EHIKLMRSTY GPVW 3.8 0 1 -1 6 9 24 1019 1.1 hour 3 min >10 hour 53.5 16625 875 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00164 PNGPWVWVPAFCQAVGWGDP 20 P6-4 Synthetic construct(derived from region of GB virus C glycoprotein E2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Luciferase assay [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=11.88 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=8.04 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00164 DRAVPe00164.cif Linear Free Free None L membrane The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. 2183.47 C105H139N25O25S EHIKLMRSTY P 3.8 0 1 -1 5 9 3.5 891 >20 hour >20 hour ? 53.5 16500 868.42 21543477 J Virol. 2011 Jul;85(14):7037-47. "Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H. " Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. 10.1128/JVI.02366-10 Anti-HIV DRAVPe00165 RGTKALTEVIPLTEEAEC 18 PepA Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =35 ± 5 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00165 DRAVPe00165.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1960.23 C83H142N22O30S DFHMNQSWY E 4.49 2 4 -2 5 6 -22.78 -3078 1 hour 2 min 2 min 92.22 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00166 GTKALTEVIPLTEEAEC 17 P1 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =7.5±2.3 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=78.2 nM,associated with Pep-1).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00166 DRAVPe00166.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1804.04 C77H130N18O29S DFHMNQRSWY E 4.09 1 4 -3 5 6 2.35 -1586 30 hour >20 hour >10 hour 97.65 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00167 ATKALTEVIPLTEEAEC 17 P2 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =28 ±11 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00167 DRAVPe00167.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1818.07 C78H132N18O29S DFGHMNQRSWY E 4.09 1 4 -3 4 7 15.29 -1499 4.4 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00168 GAKALTEVIPLTEEAEC 17 P3 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =10.3 ± 2.1 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00168 DRAVPe00168.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1774.02 C76H128N18O28S DFHMNQRSWY E 4.09 1 4 -3 4 7 17.06 -1148 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00169 GTAALTEVIPLTEEAEC 17 P4 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =15 ± 2.9 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00169 DRAVPe00169.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1746.95 C74H123N17O29S DFHKMNQRSWY E 3.58 0 4 -4 5 7 35.88 -850 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00170 GTKGLTEVIPLTEEAEC 17 P5 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =20 ± 3.7 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00170 DRAVPe00170.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1790.02 C76H128N18O29S DFHMNQRSWY E 4.09 1 4 -3 6 5 -10.59 -1673 30 hour >20 hour >10 hour 91.76 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00171 GTKAATEVIPLTEEAEC 17 P6 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =5.7 ± 2.3 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=170 nM,associated with Pep-1).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00171 DRAVPe00171.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1761.96 C74H124N18O29S DFHMNQRSWY E 4.09 1 4 -3 5 6 -9.41 -1897 30 hour >20 hour >10 hour 80.59 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00172 GTKALAEVIPLTEEAEC 17 P7 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =13.5 ± 2.1 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00172 DRAVPe00172.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1774.02 C76H128N18O28S DFHMNQRSWY E 4.09 1 4 -3 4 7 17.06 -1148 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00173 GTKALTAVIPLTEEAEC 17 P8 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =57 ± 19 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=290 nM,associated with Pep-1).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00173 DRAVPe00173.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1746.01 C75H128N18O27S DFHMNQRSWY AET 4.25 1 3 -2 5 7 33.53 -724 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00174 GTKALTEAIPLTEEAEC 17 P9 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =15 ±7.3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00174 DRAVPe00174.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1775.99 C75H126N18O29S DFHMNQRSVWY E 4.09 1 4 -3 5 6 -11.76 -1809 30 hour >20 hour >10 hour 86.47 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00175 GTKALTEVAPLTEEAEC 17 P10 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =7.3 ± 2.9 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=140 nM,associated with Pep-1).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00175 DRAVPe00175.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1761.96 C74H124N18O29S DFHIMNQRSWY E 4.09 1 4 -3 5 6 -13.53 -1897 30 hour >20 hour >10 hour 80.59 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00176 GTKALTEVIALTEEAEC 17 P11 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =7 ± 1.4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00176 DRAVPe00176.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1778 C75H128N18O29S DFHMNPQRSWY E 4.09 1 4 -3 5 7 22.35 -1405 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00177 GTKALTEVIPATEEAEC 17 P12 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =22 ± 3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00177 DRAVPe00177.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1761.96 C74H124N18O29S DFHMNQRSWY E 4.09 1 4 -3 5 6 -9.41 -1897 30 hour >20 hour >10 hour 80.59 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00178 GTKALTEVIPLAEEAEC 17 P13 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =10.2 ± 2.5 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00178 DRAVPe00178.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1774.02 C76H128N18O28S DFHMNQRSWY E 4.09 1 4 -3 4 7 17.06 -1148 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00179 GTKALTEVIPLTAEAEC 17 P14 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00179 DRAVPe00179.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1746.01 C75H128N18O27S DFHMNQRSWY AET 4.25 1 3 -2 5 7 33.53 -724 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00180 GTKALTEVIPLTEAAEC 17 P15 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 2.2 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00180 DRAVPe00180.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1746.01 C75H128N18O27S DFHMNQRSWY AET 4.25 1 3 -2 5 7 33.53 -724 30 hour >20 hour >10 hour 103.53 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00181 GTKWLTEVWPLC 12 P16 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00181 DRAVPe00181.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1432.7 C68H101N15O17S ADFHIMNQRSY LTW 5.99 1 1 0 4 5 14.17 326 30 hour >20 hour >10 hour 89.17 11000 1000 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00182 GTKAWTEVWPLC 12 P17 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =35 ± 11 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00182 DRAVPe00182.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1390.62 C65H95N15O17S DFHIMNQRSY TW 5.99 1 1 0 4 5 -2.5 15 30 hour >20 hour >10 hour 65 11000 1000 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00183 GTKALTEVIPLTC 13 P18 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50>1000 nM,associated with Pep-1);inhibition of polymerase activity of HIV-1 RT(Ki =53± 12 μM).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00183 DRAVPe00183.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1345.62 C59H104N14O19S DFHMNQRSWY T 5.99 1 1 0 5 5 70 276 30 hour >20 hour >10 hour 120 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00184 GTKAATEVIPLTC 13 P19 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =49 ± 9 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00184 DRAVPe00184.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1303.54 C56H98N14O19S DFHMNQRSWY T 5.99 1 1 0 5 5 54.62 -35 30 hour >20 hour >10 hour 97.69 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00185 GTKWLTEWIPLC 12 P24 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=2.3 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =0.7 ± 0.05 μM).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00185 DRAVPe00185.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1446.73 C69H103N15O17S ADFHMNQRSVY LTW 5.99 1 1 0 4 5 16.67 414 30 hour >20 hour >10 hour 97.5 11000 1000 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00186 KWLTEWIPLTAEAEC 15 P26 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50>1000 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =1.8± 0.7 μM).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00186 DRAVPe00186.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1790.06 C83H124N18O24S DFGHMNQRSVY E 4.25 1 3 -2 3 7 -6.67 -680 1.3 hour 3 min 2 min 91.33 11000 785.71 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00187 GTKWLTEWIPLTAEC 15 P27 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50<0.32 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =0.05 ± 0.01 μM).##NOTE:Ki: inhibition constants " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00187 DRAVPe00187.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1748.03 C81H122N18O23S DFHMNQRSVY T 4.53 1 2 -1 5 6 -2.67 -343 30 hour >20 hour >10 hour 84.67 11000 785.71 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00188 GTKWATEWAPLTAEAEC 17 P28 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =2 ± 0.6 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00188 DRAVPe00188.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1864.06 C83H122N20O27S DFHIMNQRSVY A 4.25 1 3 -2 5 7 -40 -1465 30 hour >20 hour >10 hour 46.47 11000 687.5 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00189 KWLTEWIPLTAEC 13 P29 Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =1 ± 0.4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00189 DRAVPe00189.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1589.87 C75H112N16O20S DFGHMNQRSVY ELTW 4.53 1 2 -1 3 6 5.38 -180 1.3 hour 3 min 2 min 97.69 11000 916.67 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00190 GTKWLTEWIPLTAEAEC 17 PAW Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae RT-Polymerase Assay "[Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =0.7 ± 0.2 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=1.8 nM,associated with Pep-1)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00190 DRAVPe00190.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1948.22 C89H134N20O27S DFHMNQRSVY ET 4.25 1 3 -2 5 7 -12.35 -843 30 hour >20 hour >10 hour 80.59 11000 687.5 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00191 GAKTETLVIPETELEAC 17 Pscr Synthetic construct(derived from Pep-A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae RT-Polymerase Assay [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =61 ± 12 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00191 DRAVPe00191.cif Linear Free Free None L Reverse Transcriptase "HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase." 1804.04 C77H130N18O29S DFHMNQRSWY E 4.09 1 4 -3 5 6 2.35 -1586 30 hour >20 hour >10 hour 97.65 0 0 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. "Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G." A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. 10.1074/jbc.M802199200 Anti-HIV DRAVPe00192 LEAIPMSIPPEVKFNKPFVF 20 VIRIP Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=14.79±2.56 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. DRAVPe00192 DRAVPe00192.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2303.79 C112H171N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 39 118 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00193 AEAIPMSIPPEVKFNKPFVF 20 VIRIP[A1] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00193 DRAVPe00193.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2261.71 C109H165N23O27S CDGHLQRTWY P 6.19 2 2 0 2 9 29 -193 4.4 hour >20 hour >10 hour 78 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00194 LAAIPMSIPPEVKFNKPFVF 20 VIRIP[A2] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00194 DRAVPe00194.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2245.75 C110H169N23O25S CDGHQRTWY P 8.59 2 1 1 2 10 65.5 980 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00195 LEAAPMSIPPEVKFNKPFVF 20 VIRIP[A4] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00195 DRAVPe00195.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2261.71 C109H165N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 25.5 -193 5.5 hour 3 min 2 min 78 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00196 LEAIAMSIPPEVKFNKPFVF 20 VIRIP[A5] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=23.50±5.19 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00196 DRAVPe00196.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2277.75 C110H169N23O27S CDGHQRTWY FP 6.14 2 2 0 2 10 56 299 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00197 LEAIPASIPPEVKFNKPFVF 20 VIRIP[A6] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=13.00±1.04 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00197 DRAVPe00197.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2243.67 C110H167N23O27 CDGHMQRTWY P 6.14 2 2 0 2 10 38.5 64 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00198 LEAIPMSAPPEVKFNKPFVF 20 VIRIP[A8] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=23.46±0.28 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00198 DRAVPe00198.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2261.71 C109H165N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 25.5 -193 5.5 hour 3 min 2 min 78 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00199 LEAIPMSIAPEVKFNKPFVF 20 VIRIP[A9] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=16.33±4.34 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00199 DRAVPe00199.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2277.75 C110H169N23O27S CDGHQRTWY FP 6.14 2 2 0 2 10 56 299 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00200 LEAIPMSIPAEVKFNKPFVF 20 VIRIP[A10] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=9.72±1.66 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00200 DRAVPe00200.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2277.75 C110H169N23O27S CDGHQRTWY FP 6.14 2 2 0 2 10 56 299 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00201 LEAIPMSIPPAVKFNKPFVF 20 VIRIP[A11] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=11.00±4.75 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00201 DRAVPe00201.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2245.75 C110H169N23O25S CDGHQRTWY P 8.59 2 1 1 2 10 65.5 980 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00202 LEAIPMSIPPEAKFNKPFVF 20 VIRIP[A12] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=10.64±2.23 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00202 DRAVPe00202.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2275.73 C110H167N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 27 -105 5.5 hour 3 min 2 min 83 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00203 LEAIPMSIPPEVAFNKPFVF 20 VIRIP[A13] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=4.73±0.61 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00203 DRAVPe00203.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2246.69 C109H164N22O27S CDGHQRTWY P 4.53 1 2 -1 2 10 67.5 854 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00204 LEAIPMSIPPEVKANKPFVF 20 VIRIP[A14] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=4.62±1.32 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00204 DRAVPe00204.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2227.69 C106H167N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 34 1 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00205 LEAIPMSIPPEVKFAKPFVF 20 VIRIP[A15] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=17.41±3.66 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00205 DRAVPe00205.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2260.76 C111H170N22O26S CDGHNQRTWY P 6.14 2 2 0 1 10 65.5 963 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00206 LEAIPMSIPPEVKFNAPFVF 20 VIRIP[A16] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=10.81±0.68 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00206 DRAVPe00206.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2246.69 C109H164N22O27S CDGHQRTWY P 4.53 1 2 -1 2 10 67.5 854 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00207 LEAIPMSIPPEVKFNKAFVF 20 VIRIP[A17] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=12.72±10.17 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00207 DRAVPe00207.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2277.75 C110H169N23O27S CDGHQRTWY FP 6.14 2 2 0 2 10 56 299 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00208 LEAIPMSIPPEVKFNKPAVF 20 VIRIP[A18] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00208 DRAVPe00208.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2227.69 C106H167N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 34 1 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00209 LEAIPMSIPPEVKFNKPFAF 20 VIRIP[A19] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00209 DRAVPe00209.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2275.73 C110H167N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 27 -105 5.5 hour 3 min 2 min 83 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00210 LEAIPMSIPPEVKFNKPFVA 20 VIRIP[A20] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00210 DRAVPe00210.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2227.69 C106H167N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 34 1 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00211 LEAIPMSIPPEVKFNKPFVF 20 N-Ac-VIRIP Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00211.cif Linear Acetylation Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2303.79 C112H171N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 39 118 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00212 LEAIPMSIPPEVKFNKPFVF 20 VIRIP-amide Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00212.cif Linear Free Amidation None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2303.79 C112H171N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 39 118 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00213 LEAIPMSIPPEVKFNKPFVF 20 N-Ac-VIRIP-amide Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00213.cif Linear Acetylation Amidation None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2303.79 C112H171N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 39 118 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00214 LEAIPMSIPPEVAFAKPFVF 20 "VIRIP[A13,A15]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=3.45±0.44 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00214 DRAVPe00214.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2203.67 C108H163N21O26S CDGHNQRTWY P 4.53 1 2 -1 1 11 94 1699 5.5 hour 3 min 2 min 102.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00215 LEAIPMSIPPEVFFNKPFVF 20 VIRIP[F13] Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.66±0.06 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00215 DRAVPe00215.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2322.79 C115H168N22O27S CDGHQRTWY FP 4.53 1 2 -1 2 10 72.5 971 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00216 LEAIPMCIPPECAFNKPFVF 20 "VIRIP[A13,C7,C12]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=1.00±0.21 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00216 DRAVPe00216.cif Cyclic Free Free Disulfide bond between Cys7 and Cys12 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2266.76 C107H160N22O26S3 DGHQRSTWY P 4.53 1 2 -1 3 9 75.5 1046 5.5 hour 3 min 2 min 83 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00217 LEAIPCSIPPCVAFNKPFVF 20 "VIRIP[A13,C6,C11]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.18±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00217 DRAVPe00217.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2192.66 C105H158N22O25S2 DGHMQRTWY P 5.99 1 1 0 4 10 100.5 1556 5.5 hour 3 min 2 min 97.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00218 LEAIPCSIPpCVAFNKPFVF 20 "VIRIP[A13,C6,C11,p10]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.94±0.54 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00218.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2192.66 C100H149N21O23S2 DGHMQRTWY FP 5.99 1 1 0 4 10 108.5 1556 5.5 hour 3 min 2 min 97.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00219 LEAIPCSIPPCVGFGKPFVF 20 "VIRIP[C6,C11,G13,G15]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.73±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00219 DRAVPe00219.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2121.58 C102H153N21O24S2 DHMNQRTWY P 5.99 1 1 0 5 9 105 2227 5.5 hour 3 min 2 min 92.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00220 LEAIPCSIPPCVLFNKPFVF 20 "VIRIP[C6,C11,L13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.84±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00220 DRAVPe00220.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2234.74 C108H164N22O25S2 DGHMQRTWY P 5.99 1 1 0 4 10 110.5 1867 5.5 hour 3 min 2 min 112 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00221 LEAIPCSIPPCVFFNKPFVF 20 "VIRIP[C6,C11,F13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.93±0.05 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. DRAVPe00221 DRAVPe00221.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2268.76 C111H162N22O25S2 DGHMQRTWY FP 5.99 1 1 0 4 10 105.5 1673 5.5 hour 3 min 2 min 92.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00222 LEAIPCSIPPCFAFNKPFVF 20 "VIRIP[A13,C6,C11,F12]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.27±0.04 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. DRAVPe00222 DRAVPe00222.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2240.71 C109H158N22O25S2 DGHMQRTWY FP 5.99 1 1 0 4 10 93.5 1450 5.5 hour 3 min 2 min 83 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00223 LEAIPMSIPPEFLFGKPFVF 20 "VIRIP[F12,L13,G15]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=1.34±0.42 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. DRAVPe00223 DRAVPe00223.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2279.77 C114H167N21O26S CDHNQRTWY FP 4.53 1 2 -1 2 10 86 1817 5.5 hour 3 min 2 min 97.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00224 LEAIPCSIPPCVFFGKPFVF 20 "VIRIP[C6,C11,F13,G15]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.28±0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00224 DRAVPe00224.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2211.71 C109H159N21O24S2 DHMNQRTWY FP 5.99 1 1 0 4 10 121 2431 5.5 hour 3 min 2 min 92.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00225 LEAIPCSIPPCFLFGKPFVF 20 "VIRIP[C6,C11,F12,L13,G15]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.39±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00225 DRAVPe00225.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2225.73 C110H161N21O24S2 DHMNQRTWY FP 5.99 1 1 0 4 10 119 2519 5.5 hour 3 min 2 min 97.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00226 LEAIPCSIPpCVFFNKPFVF 20 "VIRIP[C6,C11,p10,F13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.33±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00226.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2268.76 C106H153N21O23S2 DGHMQRTWY F 5.99 1 1 0 4 10 113.5 1673 5.5 hour 3 min 2 min 92.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00227 LEAIPCSIPpCFLFNKPFVF 20 "VIRIP[C6,C11,p10,F12,L13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.20±0.04 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. No predicted structure available DRAVPe00227.cif Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2282.79 C107H155N21O23S2 DGHMQRTWY F 5.99 1 1 0 4 10 111.5 1761 5.5 hour 3 min 2 min 97.5 125 6.58 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00228 LEAIPMGIPpEVXFNKPFVF 20 "VIRIP[G7,p10,L-Tic13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.28±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. No predicted structure available DRAVPe00228.cif Linear Free Free The 'X' at position 13 is L-tetrahydro-isoquinoline-3-carboxylic acid(Tic). Mixed(D-Pro10) membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2256.92 C100H146N20O22S CDHQRSTWY FP 4.53 1 2 -1 2 9 68.5 1107 5.5 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00229 LEKIPMSIPpEVXFNKPFVF 20 "VIRIP[K3,p10,L-Tic13]" Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.41±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00229.cif Linear Free Free The 'X' at position 13 is L-tetrahydro-isoquinoline-3-carboxylic acid(Tic). Mixed(D-Pro10) membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2344.04 C104H155N21O23S ACDGHQRTWY FP 6.14 2 2 0 2 8 38 -63 5.5 hour 3 min 2 min 87.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00230 KVINPEPIVEPFMSKPFALF 20 scrambled VIRIP Synthetic construct(derived from α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. DRAVPe00230 DRAVPe00230.cif Linear Free Free None L membrane The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. 2303.79 C112H171N23O27S CDGHQRTWY P 6.14 2 2 0 2 9 39 118 1.3 hour 3 min 2 min 92.5 0 0 17448989 Cell. 2007 Apr 20;129(2):263-75. "Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F." Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. 10.1016/j.cell.2007.02.042 Anti-HIV DRAVPe00231 YTSLIHSLIEEGQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138G] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=1.3± 0.5 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=65± 8.8 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=141±26 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=185±68 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00231 DRAVPe00231.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4420.86 C201H296N50O63 CMPRV EL 4.3 3 7 -4 9 13 -86.39 -6825 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00232 YTSLIHSLIEEAQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138A] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.6 ± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=3.6± 1.7 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=3.5 ±0.9 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=3.2 ± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00232 DRAVPe00232.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4434.89 C202H298N50O63 CGMPRV EL 4.3 3 7 -4 8 14 -80.28 -6738 2.8 hour 10 min 2 min 92.22 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00233 YTSLIHSLIEEVQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138V] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.4 ± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=31 ± 14 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=22 ± 3.5 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=23 ± 5.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00233 DRAVPe00233.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4462.94 C204H302N50O63 CGMPR EL 4.3 3 7 -4 8 14 -73.61 -6515 2.8 hour 10 min 2 min 97.5 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00234 YTSLIHSLIEELQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138L] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.7± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=13± 6 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=2.9 ±0.7 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=2.2± 0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00234 DRAVPe00234.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4476.97 C205H304N50O63 CGMPRV L 4.3 3 7 -4 8 14 -74.72 -6427 2.8 hour 10 min 2 min 100.28 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00235 YTSLIHSLIEEIQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138I] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.5 ± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=4.9± 2 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=2.9 ±0.8 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=2.4 ± 0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00235 DRAVPe00235.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4476.97 C205H304N50O63 CGMPRV EL 4.3 3 7 -4 8 14 -72.78 -6427 2.8 hour 10 min 2 min 100.28 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00236 YTSLIHSLIEEMQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138M] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.7± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=4.4± 0.1 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=1.7±0.5 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=1.2± 0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00236 DRAVPe00236.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4495 C204H302N50O63S CGPRV EL 4.3 3 7 -4 8 13 -80 -6684 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00237 YTSLIHSLIEEPQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138P] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=446± 167 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00237 DRAVPe00237.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4460.92 C204H300N50O63 CGMRV EL 4.3 3 7 -4 8 13 -89.72 -6919 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00238 YTSLIHSLIEETQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138T] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.9± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=39± 8.5 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=161±35 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=124±43nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00238 DRAVPe00238.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4464.91 C203H300N50O64 CGMPRV EL 4.3 3 7 -4 9 13 -87.22 -7176 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00239 YTSLIHSLIEEFQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138F] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=9.4± 2.6 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=203± 89 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=393 ± 119 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=478 ± 116 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00239 DRAVPe00239.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4510.98 C208H302N50O63 CGMPRV EL 4.3 3 7 -4 8 14 -77.5 -6621 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00240 YTSLIHSLIEEYQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138Y] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=25 ±9nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=516 ±223 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00240 DRAVPe00240.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4526.98 C208H302N50O64 CGMPRV EL 4.3 3 7 -4 9 13 -88.89 -6933 2.8 hour 10 min 2 min 89.44 19480 556.57 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00241 YTSLIHSLIEEWQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138W] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=29± 14 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00241 DRAVPe00241.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4550.02 C210H303N51O63 CGMPRV EL 4.3 3 7 -4 8 14 -87.78 -6686 2.8 hour 10 min 2 min 89.44 23490 671.14 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00242 YTSLIHSLIEENQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138N] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=19± 4 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00242 DRAVPe00242.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4477.91 C203H299N51O64 CGMPRV EL 4.3 3 7 -4 9 13 -95 -7583 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00243 YTSLIHSLIEEQQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138Q] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=34± 11 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00243 DRAVPe00243.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4491.94 C204H301N51O64 CGMPRV EL 4.3 3 7 -4 8 13 -95 -7473 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00244 YTSLIHSLIEEDQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138D] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=210± 94 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00244 DRAVPe00244.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4478.89 C203H298N50O65 CGMPRV EL 4.16 3 8 -5 8 13 -95 -7791 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00245 YTSLIHSLIEEEQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138E] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=283± 80 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00245 DRAVPe00245.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4492.92 C204H300N50O65 CGMPRV E 4.21 3 8 -5 8 13 -95 -7600 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00246 YTSLIHSLIEEHQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138H] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=210± 85 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00246 DRAVPe00246.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4500.95 C205H300N52O63 CGMPRV EL 4.53 4 7 -3 8 13 -94.17 -7385 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00247 YTSLIHSLIEEKQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138K] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=708±145 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00247 DRAVPe00247.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4491.98 C205H305N51O63 CGMPRV EL 4.54 4 7 -3 8 13 -96.11 -7474 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00248 YTSLIHSLIEERQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138R] Synthetic construct(derived from Enfuvirtide) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=362± 114 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00248 DRAVPe00248.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4519.99 C205H305N53O63 CGMPV EL 4.54 4 7 -3 8 13 -97.78 -8411 2.8 hour 10 min 2 min 89.44 17990 514 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00249 WMEWDREINNYTSLIHSLIEEAQNQQEKNEQELL 34 C34S[138A] Synthetic construct(derived from C34) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=2.0± 0.4 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=1.7± 0.3 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=2.0 ±0.6 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=1.3 ±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00249 DRAVPe00249.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4232.6 C184H280N50O63S CFGPV E 4.21 3 8 -5 8 10 -119.41 -9649 2.8 hour 3 min 2 min 83.24 12490 378.48 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00250 WMEWDREINNYTSLIHSLIEELQNQQEKNEQELL 34 C34S[138L] Synthetic construct(derived from C34) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=1.5± 0.4 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=1.2± 0.6 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=0.5 ±0.2 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=0.4±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00250 DRAVPe00250.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4274.68 C187H286N50O63S ACFGPV E 4.21 3 8 -5 8 10 -113.53 -9338 2.8 hour 3 min 2 min 91.76 12490 378.48 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00251 WMEWDREINNYTSLIHSLIEETQNQQEKNEQELL 34 C34S[138T] Synthetic construct(derived from C34) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=2.6± 0.2 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=4.8± 1.3 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=32 ± 5.5 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=24 ±6.6nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00251 DRAVPe00251.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4262.63 C185H282N50O64S ACFGPV E 4.21 3 8 -5 9 9 -126.76 -10087 2.8 hour 3 min 2 min 80.29 12490 378.48 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00252 WMEWDREINNYTSLIHSLIEEWQNQQEKNEQELL 34 C34S[138W] Synthetic construct(derived from C34) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00252 DRAVPe00252.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4347.74 C192H285N51O63S ACFGPV E 4.21 3 8 -5 8 10 -127.35 -9597 2.8 hour 3 min 2 min 80.29 17990 545.15 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00253 WMEWDREINNYTSLIHSLIEEPQNQQEKNEQELL 34 C34S[138P] Synthetic construct(derived from C34) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=46±11 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=436± 125 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=250 ± 80 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=176±50 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00253 DRAVPe00253.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4258.64 C186H282N50O63S ACFGV E 4.21 3 8 -5 8 9 -129.41 -9830 2.8 hour 3 min 2 min 80.29 12490 378.48 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M." Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. 10.1074/jbc.M807169200 Anti-HIV DRAVPe00254 WQEWEQKITALLEQAQIQQEKNEYELQKLDKWASLWEWF 39 1249 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.003 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.013 μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.022 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.363 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=8.140 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00254.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4995.58 C233H338N56O67 CGHMPRV EQ 4.43 4 8 -4 4 16 -109.49 -7562 2.8 hour 3 min 2 min 77.69 28990 762.89 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 DRAVPa0873 Anti-HIV DRAVPe00255 MTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELL 36 651 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.008 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.033μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.060 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.151 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=7.599 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00255 DRAVPe00255.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4480.9 C193H296N52O67S2 ACFGPV E 4.21 3 8 -5 10 9 -116.67 -10192 30 hour >20 hour >10 hour 75.83 12490 356.86 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 DRAVPa0971 Anti-HIV DRAVPe00256 MTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLEL 38 2410 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.008 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.032μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.039 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.137 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=4.975 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00256 DRAVPe00256.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4723.18 C204H314N54O71S2 ACFGPV E 4.14 3 9 -6 10 10 -109.74 -10381 30 hour >20 hour >10 hour 82.11 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00257 TTWEEWDREINEYTSRIESLIRESQEQQEKNEQELREL 38 2429 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.012 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.021μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.056 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.037 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.167 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00257 DRAVPe00257.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4826.14 C205H319N59O76 ACFGHMPV E 4.29 5 12 -7 9 8 -177.89 -16817 7.2 hour >20 hour >10 hour 61.58 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00258 MTWMAWDRAIANYAALIHALIEAAQNQQEKNEAALLEL 38 2638 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.061 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.079μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.079 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.120 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.250 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00258 DRAVPe00258.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4312.93 C192H300N52O57S2 CFGPSV A 4.57 3 5 -2 5 20 1.05 -3352 30 hour >20 hour >10 hour 108.42 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00259 TTWEAWDRAIAEYAARIEALIRASQEQQEKNEAELREL 38 290676 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.006 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.013μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.022 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.072 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=1.314 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00259 DRAVPe00259.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4489.93 C195H307N57O65 CFGHMPV AE 4.52 5 9 -4 5 16 -87.89 -11171 7.2 hour >20 hour >10 hour 82.63 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00260 MTWEAWDRAIAEYAARIEALIRAAQEQQEKNEAALREL 38 2544 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.007 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.026μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.033 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.014 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.021 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00260 DRAVPe00260.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4445.98 C194H307N57O61S CFGHPSV A 4.64 5 8 -3 3 18 -60.26 -9296 30 hour >20 hour >10 hour 87.89 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00261 TTWEAWDRAIAEYAARIEALIRAAQEQQEKNEAILREL 38 267209 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.007 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.021μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.034 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.024 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.039 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00261 DRAVPe00261.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4457.97 C196H311N57O62 CFGHMPSV A 4.64 5 8 -3 4 18 -60 -9477 7.2 hour >20 hour >10 hour 95.53 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00262 TTWEAWDRAIAEYAARIEALIRALQEQQEKNEAALREL 38 267221 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.011 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.035μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.028 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.035 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.050 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00262 DRAVPe00262.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4457.97 C196H311N57O62 CFGHMPSV A 4.64 5 8 -3 4 18 -61.84 -9477 7.2 hour >20 hour >10 hour 95.53 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 DRAVPa1316 Anti-HIV DRAVPe00263 TTWEAWDRAIAEYAARIEALIRAAQELQEKNEAALREL 38 267226 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.007 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.021μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.035 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.030 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.020 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00263 DRAVPe00263.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4400.92 C194H308N56O61 CFGHMPSV A 4.64 5 8 -3 4 19 -47.89 -8742 7.2 hour >20 hour >10 hour 98.16 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00264 TTWEAWDRAIAEYAARIEALIRALQEQQEKNEAILREL 38 267225 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.019 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.043μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.079 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.038 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.196 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00264 DRAVPe00264.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4500.05 C199H317N57O62 CFGHMPSV A 4.64 5 8 -3 4 18 -54.74 -9166 7.2 hour >20 hour >10 hour 103.16 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00265 TTWEAWDRAIAEYAARIEALIRAAQEQQEKLEAALREL 38 267227 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.012 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.045μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.028 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.025 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.044 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00265 DRAVPe00265.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4414.94 C195H310N56O61 CFGHMNPSV A 4.64 5 8 -3 3 19 -47.89 -8632 7.2 hour >20 hour >10 hour 98.16 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 DRAVPa1317 Anti-HIV DRAVPe00266 TTWEAWDRAIAEYAARIEALIRAAQEQQEKLEAVLREL 38 291022 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.022 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.049μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.093 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.046 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.242 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00266 DRAVPe00266.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4443 C197H314N56O61 CFGHMNPS A 4.64 5 8 -3 3 19 -41.58 -8409 7.2 hour >20 hour >10 hour 103.16 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00267 TTWEAWDRAIAEYAARIEALIRALQELQEKNEAALREL 38 290822 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.030 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.054μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.084 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.147 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.242 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00267 DRAVPe00267.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4443 C197H314N56O61 CFGHMPSV A 4.64 5 8 -3 4 19 -42.63 -8431 7.2 hour >20 hour >10 hour 105.79 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00268 TTWEAWDRAIAEYAARIEALIRALQELQEKNEAILREL 38 290821 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.065 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.118μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.154 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.192 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50>20 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00268 DRAVPe00268.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4485.08 C200H320N56O61 CFGHMPSV A 4.64 5 8 -3 4 19 -35.53 -8120 7.2 hour >20 hour >10 hour 113.42 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00269 TTWEAWDRAIAEYAARIEALIRAAQELQEKLEAALREL 38 267228 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.172 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.600μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.416 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.555 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.987 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00269 DRAVPe00269.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4399.97 C196H313N55O60 CFGHMNPSV A 4.64 5 8 -3 3 20 -28.68 -7586 7.2 hour >20 hour >10 hour 108.42 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00270 TTWEAWDRAIAEYAARIEALIRALQELQEKLEAILREL 38 267229 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=3.162 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50>20μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50>20 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50>20 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50>20 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00270 DRAVPe00270.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4484.13 C202H325N55O60 CFGHMNPSV A 4.64 5 8 -3 3 20 -16.32 -6964 7.2 hour >20 hour >10 hour 123.68 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 Anti-HIV DRAVPe00271 AEAMSQVTN 9 p2(gag) peptide[Δ10-14] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=5 μM). DRAVPe00271 DRAVPe00271.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 950.03 C37H63N11O16S CDFGHIKLPRWY A 4 0 1 -1 3 3 -25.56 -1495 4.4 hour >20 hour >10 hour 54.44 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00272 AAAMSQVTN 9 "p2(gag) peptide[Δ10-14,E2A]" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=100 μM). DRAVPe00272 DRAVPe00272.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 891.99 C35H61N11O14S CDEFGHIKLPRWY A 5.57 0 0 0 3 4 33.33 -633 4.4 hour >20 hour >10 hour 65.56 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00273 AEAMAQVTN 9 "p2(gag) peptide[Δ10-14,S5A]" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=124 μM). DRAVPe00273 DRAVPe00273.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 934.03 C37H63N11O15S CDFGHIKLPRSWY A 4 0 1 -1 2 4 3.33 -974 4.4 hour >20 hour >10 hour 65.56 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00274 AEAMSQVTNTATIM 14 p2(gag) peptide Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=10 μM). DRAVPe00274 DRAVPe00274.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 1467.67 C59H102N16O23S2 CDFGHKLPRWY AT 4 0 1 -1 5 5 32.14 -1101 4.4 hour >20 hour >10 hour 70 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00275 AEAASQVTNTATIM 14 p2(gag) peptide[M4A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=142 μM). DRAVPe00275 DRAVPe00275.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 1407.56 C57H98N16O23S CDFGHKLPRWY A 4 0 1 -1 5 6 31.43 -1155 4.4 hour >20 hour >10 hour 77.14 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00276 AEASQVTNTATIM 13 p2(gag) peptide[ΔM4] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=126 μM). DRAVPe00276 DRAVPe00276.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 1336.48 C54H93N15O22S CDFGHKLPRWY AT 4 0 1 -1 5 5 20 -1336 4.4 hour >20 hour >10 hour 75.38 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00277 AEAMSQVANTATIM 14 p2(gag) peptide[T8A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Protease inhibition assay [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=110 μM). DRAVPe00277 DRAVPe00277.cif Linear Free Free None L autolysis The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. 1437.65 C58H100N16O22S2 CDFGHKLPRWY A 4 0 1 -1 4 6 50 -663 4.4 hour >20 hour >10 hour 77.14 0 0 15113844 J Biochem. 2004 Mar;135(3):447-53.  "Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S." Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  10.1093/jb/mvh052 Anti-HIV DRAVPe00278 GIPCGESCVWIPCISAALGCSCKNKVCYRN 30 Circulin-A (CIRA; Plant defensin) Chassalia parviflora P56871 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1BH4 HIV Retroviridae [Ref.18008336]HIV-1:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40-260 nM). [Ref.10430870] EC50 = 1020 μM against blood type A human erythrocytes. [Ref.18008336]CEM-SS cells:IC50=500 nM. DRAVPe00278 DRAVPe00278.cif Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22, Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3175.78 C134H216N38O39S6 DFHMQT C 8.33 3 1 2 15 9 41.67 -1224 30 hour >20 hour >10 hour 78 7365 253.97 18008336##10430870 Biopolymers. 2008;90(1):51-60.##Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Tam JP, Lu YA, Yang JL, Chiu KW." Cyclotides as natural anti-HIV agents.##An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. 10.1002/bip.20886##10.1073/pnas.96.16.8913 Anti-HIV DRAVPe00279 GVIPCGESCVFIPCISTLLGCSCKNKVCYRN 31 Circulin-B (CIRB; Plant defensin) Chassalia parviflora P56879 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2ERI HIV Retroviridae [Ref.18008336]HIV-1:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40-260 nM). [Ref.10430870] EC50 = 550 μM against blood type A human erythrocytes. [Ref.10430870] It caused 50% cell growth inhibition of mouse fibroblasts at 820 μM.##[Ref.18008336]CEM-SS cells:IC50=500 nM. DRAVPe00279 DRAVPe00279.cif Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) "Disulfide bonds between Cys5 and Cys19, Cys9 and Cys21, Cys14 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3307.98 C141H232N38O41S6 ADHMQW C 8.33 3 1 2 16 9 64.19 -882 30 hour >20 hour >10 hour 90.97 1865 62.17 18008336##10430870 Biopolymers. 2008;90(1):51-60.##Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Tam JP, Lu YA, Yang JL, Chiu KW." Cyclotides as natural anti-HIV agents.##An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. 10.1002/bip.20886##10.1073/pnas.96.16.8913 Anti-HIV DRAVPe00280 GIPCGESCVFIPCITSVAGCSCKSKVCYRN 30 Circulin-C (CIRC; Plant defensin) Chassalia parviflora P84641 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV-1:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM).##[Ref.10691702]HIV-1(HIV-1 IIIB):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=73 nM);##HIV-1(HIV-1 RF):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=165 nM);##HIV-1(HIV-1 214):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=213 nM);##HIV-1(HIV-1 205):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=155 nM);##HIV-1(HIV-1 G):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=111 nM);##HIV-1(HIV-1 SK1):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=51 nM);##HIV-1(HIV-1 N119):inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=241 nM);##HIV-1(HIV-1 A17):inhibition the cytopathic effects of HIV-1 infection in MT-2 cells(EC50=247 nM);##HIV-1(HIV-1G9106):inhibition the cytopathic effects of HIV-1 infection in MT-2 cells(EC50=67 nM);##HIV-1(HIV-1 H1122):inhibition the cytopathic effects of HIV-1 infection in MT-2 cells(EC50=48 nM);##HIV-1(HIV-1 IIIB):inhibition the cytopathic effects of HIV-1 infection in MT-2 cells(EC50=200 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00280 DRAVPe00280.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3125.72 C131H214N36O40S6 DHLMQW C 8.33 3 1 2 16 8 56 -1361 30 hour >20 hour >10 hour 71.33 1865 64.31 18008336##10691702 Biopolymers. 2008;90(1):51-60.##J Nat Prod. 2000 Feb;63(2):176-8. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Gustafson KR, Walton LK, Sowder RC Jr, Johnson DG, Pannell LK, Cardellina JH Jr, Boyd MR." Cyclotides as natural anti-HIV agents.##New circulin macrocyclic polypeptides from Chassalia parvifolia. 10.1002/bip.20886##10.1021/np990432r Anti-HIV DRAVPe00281 KIPCGESCVWIPCVTSIFNCKCENKVCYHD 30 Circulin-D (CIRD; Plant defensin) Chassalia parviflora P84642 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "XTT [2,3-bis-(2-methoxy-4-nitro-5-sulphophenyl)-2H-tetrazolium-5-carboxanilide]" [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00281 DRAVPe00281.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3420.03 C148H228N38O43S6 ALMQR C 6.71 4 3 1 13 8 11.33 -2563 1.3 hour 3 min 2 min 68 7365 253.97 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00282 KIPCGESCVWIPCLTSVFNCKCENKVCYHD 30 Circulin-E (CIRE; Plant defensin) Chassalia parviflora P84643 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00282 DRAVPe00282.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3420.03 C148H228N38O43S6 AMQR C 6.71 4 3 1 13 8 9 -2563 1.3 hour 3 min 2 min 68 7365 253.97 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00283 AIPCGESCVWIPCISAAIGCSCKNKVCYR 29 Circulin-F (CIRF; Plant defensin) Chassalia parviflora P84644 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00283 DRAVPe00283.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3075.7 C131H212N36O37S6 DFHLMQT C 8.34 3 1 2 13 10 65.17 -473 4.4 hour >20 hour >10 hour 84.14 7365 263.04 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00284 GVIPCGESCVFIPCISAAIGCSCKNKVCYRN 31 Cycloviolin-A (Plant defensin) Leonia cymosa (Sacha uba) P84637 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18008336]CEM-SS cells:IC50=560 nM. DRAVPe00284 DRAVPe00284.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys5 and Cys21, Cys9 and Cys23,Cys14 and Cys28." L Not found No machanism information found in the reference(s) presented in this entry 3235.88 C137H224N38O40S6 DHLMQTW C 8.33 3 1 2 15 10 68.06 -755 30 hour >20 hour >10 hour 84.84 1865 62.17 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00285 GTACGESCYVLPCFTVGCTCTSSQCFKN 28 Cycloviolin-B (Plant defensin) Leonia cymosa (Sacha uba) P84638 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18008336]CEM-SS cells:IC50=560 nM. DRAVPe00285 DRAVPe00285.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys18, Cys8 and Cys20,Cys13 and Cys25." L Not found No machanism information found in the reference(s) presented in this entry 2910.33 C120H185N31O41S6 DHIMRW C 5.96 1 1 0 18 6 38.93 -1389 30 hour >20 hour >10 hour 38.21 1865 69.07 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00286 GIPCGESCVFIPCLTTVAGCSCKNKVCYRN 30 Cycloviolin-C (Plant defensin) Leonia cymosa (Sacha uba) P84639 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18008336]CEM-SS cells:IC50=560 nM. DRAVPe00286 DRAVPe00286.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3166.77 C133H217N37O40S6 DHMQW C 8.33 3 1 2 16 8 45 -1602 30 hour >20 hour >10 hour 71.33 1865 64.31 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00287 GFPCGESCVFIPCISAAIGCSCKNKVCYRN 30 Cycloviolin-D (Plant defensin) Leonia cymosa (Sacha uba) P84640 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18008336]CEM-SS cells:IC50=560 nM. DRAVPe00287 DRAVPe00287.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27." L Not found No machanism information found in the reference(s) presented in this entry 3170.76 C135H213N37O39S6 DHLMQTW C 8.33 3 1 2 15 9 50.67 -1353 30 hour >20 hour >10 hour 65 1865 64.31 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00288 GIPCGESCVWIPCISAAIGCSCKSKVCYRN 30 Cycloviolacin-O13 (Cyclotide c3; Plant defensin) Viola odorata (Sweet violet) Q5USN8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=320 nM). [Ref.16872274] It has 50% hemolytic activity at 1.0 μM and 75% hemolytic activity at 1.5 μM against human type A red blood cells [Ref.18008336]CEM-SS cells:IC50=6400 nM. DRAVPe00288 DRAVPe00288.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L Not found No machanism information found in the reference(s) presented in this entry 3148.75 C133H215N37O39S6 DFHLMQT C 8.33 3 1 2 15 9 53 -900 30 hour >20 hour >10 hour 78 7365 253.97 18008336##16872274 Biopolymers. 2008;90(1):51-60.##Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Ireland DC, Colgrave ML, Craik DJ." "Cyclotides as natural anti-HIV agents.##A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." 10.1002/bip.20886##10.1042/BJ20060627 Anti-HIV DRAVPe00289 GSIPACGESCFKGKCYTPGCSCSKYPLCAKN 31 Cycloviolacin-O14 (Plant defensin) Viola odorata (Sweet violet) P85177 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2GJ0 HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=440 nM). [Ref:16872274] It has 3% hemolytic activity at 1.0 μM and 13% hemolytic activity at 1.5 μM against human type A red blood cells [Ref.18008336]CEM-SS cells:IC50=4800 nM. DRAVPe00289 DRAVPe00289.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys27. L Not found No machanism information found in the reference(s) presented in this entry 3203.74 C135H212N36O42S6 DHMQRVW C 8.64 4 1 3 18 5 -18.71 -2422 30 hour >20 hour >10 hour 31.61 3355 111.83 18008336##16872274 Biopolymers. 2008;90(1):51-60.##Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Ireland DC, Colgrave ML, Craik DJ." "Cyclotides as natural anti-HIV agents.##A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." 10.1002/bip.20886##10.1042/BJ20060627 Anti-HIV DRAVPe00290 GLPTCGETCFGGTCNTPGCTCDPWPVCTHN 30 Cycloviolacin-O24 (Plant defensin) Viola odorata (Sweet violet) P84637 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=308 nM). [Ref:16872274] It has 75% hemolytic activity at 25.0 μM against human type A red blood cells. [Ref.18008336]CEM-SS cells:IC50=6170 nM. DRAVPe00290 DRAVPe00290.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L Not found No machanism information found in the reference(s) presented in this entry 3072.44 C126H187N35O43S6 AIKMQRSY CT 4.35 1 2 -1 19 4 -16.33 -2224 30 hour >20 hour >10 hour 22.67 5875 202.59 18008336##16872274 Biopolymers. 2008;90(1):51-60.##Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Ireland DC, Colgrave ML, Craik DJ." "Cyclotides as natural anti-HIV agents.##A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." 10.1002/bip.20886##10.1042/BJ20060627 Anti-HIV DRAVPe00291 GGTIFDCGETCFLGTCYTPGCSCGNYGFCYGTN 33 Cycloviolacin-Y1 (Plants) Viola yedoensis (Chinese herb) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "[Ref.18081258] Anti-HIV activity:EC50=1.2μM, IC50>4.5μM. ##NOTE:EC50 refers to the values for HIV-infected cell cultures, IC50 refers to the values for uninfected cell cultures.##[Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=1210 nM)." [Ref.18081258] It has hemolytic activity. [Ref.18008336]CEM-SS cells:IC50>4470 nM. DRAVPe00291 DRAVPe00291.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys7 and Cys21; Cys11 and Cys23; Cys16 and Cys29. L Not found No machanism information found in the reference(s) presented in this entry 3412.77 C145H203N35O49S6 AHKMQRVW G 3.67 0 2 -2 25 5 14.24 -1150 30 hour >20 hour >10 hour 23.64 4845 151.41 18008336##18081258 Biopolymers. 2008;90(1):51-60.## J Nat Prod. 2008 Jan;71(1):47-52. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ." Cyclotides as natural anti-HIV agents.##Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. 10.1002/bip.20886##10.1021/np070393g Anti-HIV DRAVPe00292 GDPTFCGETCRVIPVCTYSAALGCTCDDRSDGLCKRN 37 Palicourein (Cyclotides; Plants) Palicourea condensata (Cappel) P84645 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1R1F HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=100 nM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.11430013] Cytotoxicity: human T-lymphoblastoid cell line (CEM-SS)(EC50=0.10 Μm, IC50=1.5 μM) . ##[Ref.18008336]CEM-SS cells:IC50=1500 nM." DRAVPe00292 DRAVPe00292.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys1 and Cys19; Cys5 and Cys21; Cys11 and Cys28;hydrogen bonds between the oxygen atoms of the Glu3 carboxyl group and the backbone amides of residues Thr12, Thr13, and Ser14, and the side chain of Ser14. " L Not found No machanism information found in the reference(s) presented in this entry 3928.43 C159H256N48O56S6 HMQW C 4.78 4 5 -1 18 8 -18.92 -7498 30 hour >20 hour >10 hour 52.7 1865 51.81 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00293 GVPCGESCVFIPCITGVIGCSCSSNVCYLN 30 Cycloviolacin-Y4 (Plants) Viola yedoensis (Chinese herb) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "[Ref.18618891]Effects: H. contortus( IC50=2.01μM, IC99=6.73μM) and T. colubriformis(IC50=2.27μM, IC99=5.26μM).##[Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=120 nM)." [Ref:18081258] HD50=9.3 μM against human type A red blood cells. [Ref.18008336]CEM-SS cells:IC50=1720 nM. DRAVPe00293 DRAVPe00293.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L Not found No machanism information found in the reference(s) presented in this entry 3025.55 C127H202N32O41S6 ADHKMQRW C 4 0 1 -1 18 9 104.67 1386 30 hour >20 hour >10 hour 90.67 1865 64.31 18008336##18081258 Biopolymers. 2008;90(1):51-60.## J Nat Prod. 2008 Jan;71(1):47-52. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ." Cyclotides as natural anti-HIV agents.##Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. 10.1002/bip.20886##10.1021/np070393g Anti-HIV DRAVPe00294 GIPCAESCVWIPCTVTALVGCSCSDKVCYN 30 Cycloviolacin-Y5 (Plants) Viola yedoensis (Chinese herb) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "[Ref.18618891]Effects: H. contortus( IC50=2.28μM, IC99=22.24μM) and T. colubriformis(IC50=2.40μM, IC99=10.97μM).##[Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40 nM)." [Ref:18081258] HD50=8.7 μM against human type A red blood cells. [Ref.18008336]CEM-SS cells:IC50=1760 nM. DRAVPe00294 DRAVPe00294.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L Not found No machanism information found in the reference(s) presented in this entry 3122.67 C132H209N33O42S6 FHMQR C 4.37 1 2 -1 15 10 79.33 323 30 hour >20 hour >10 hour 84.33 7365 253.97 18008336##18081258 Biopolymers. 2008;90(1):51-60.## J Nat Prod. 2008 Jan;71(1):47-52. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ." Cyclotides as natural anti-HIV agents.##Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. 10.1002/bip.20886##10.1021/np070393g Anti-HIV DRAVPe00295 SISCGESCAMISFCFTEVIGCSCKNKVCYLN 31 Leaf cyclotide 1 (Vhl-1; Plant defensin) Viola hederacea (Australian violet) P84522 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZA8 HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=870 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00295 DRAVPe00295.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L Not found No machanism information found in the reference(s) presented in this entry 3340.94 C140H223N35O45S7 DHPQRW C 5.85 2 2 0 17 9 69.03 -1027 1.9 hour >20 hour >10 hour 72.26 1865 62.17 18008336 Biopolymers. 2008;90(1):51-60. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ." Cyclotides as natural anti-HIV agents. 10.1002/bip.20886 Anti-HIV DRAVPe00296 GLPVCGETCVGGTCNTPGCTCSWPVCTRN 29 Kalata-B1 (Plant defensin) Oldenlandia affinis P56254 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2KHB##1NB1 HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=140 nM). [Ref.12779323] HD50 = 300 μM against Human type A red blood cells. [Ref.18008336]CEM-SS cells:IC50=3500 nM. DRAVPe00296 DRAVPe00296.cif Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) "Disulfide bonds between Cys5 and Cys19, Cys9 and Cys21, Cys14 and Cys26." L Not found No machanism information found in the reference(s) presented in this entry 2916.34 C117H187N35O40S6 ADFHIKMQY C 5.96 1 1 0 19 5 15.17 -1951 30 hour >20 hour >10 hour 43.45 5875 209.82 18008336##12779323 Biopolymers. 2008;90(1):51-60.##Biochemistry. 2003 Jun 10;42(22):6688-95. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Barry DG, Daly NL, Clark RJ, Sando L, Craik DJ." Cyclotides as natural anti-HIV agents.##Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity. 10.1002/bip.20886##10.1021/bi027323n Anti-HIV DRAVPe00297 GSVLNCGETCLLGTCYTTGCTCNKYRVCTKD 31 Kalata-B8 (Plant defensin) Oldenlandia affinis P85175 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2B38 HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=2500 nM). [Ref.20564013] It produced 7% hemolysis at the 62μM. [Ref.18008336]CEM-SS cells:IC50>11000 nM. DRAVPe00297 DRAVPe00297.cif Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys28. L Not found No machanism information found in the reference(s) presented in this entry 3307.81 C134H220N38O47S6 AFHIMPQW CT 7.76 3 2 1 21 5 -2.26 -3965 30 hour >20 hour >10 hour 56.45 3355 111.83 18008336##20564013 Biopolymers. 2008;90(1):51-60.##Biopolymers. 2010;94(5):647-58. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Plan MR, Rosengren KJ, Sando L, Daly NL, Craik DJ." Cyclotides as natural anti-HIV agents.##Structural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinis. 10.1002/bip.20886##10.1002/bip.21409 Anti-HIV DRAVPe00298 GLPICGETCVGGTCNTPGCSCSWPVCTRN 29 Varv peptide E (Varv E; Plant defensin) Viola arvensis (European field pansy) (Field violet) P83835 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=350 nM). [Ref.20580652] HD50=6.96 µM against human type O red blood cells. "[Ref.20580652] Cytotoxicity: U251(IC50=38.84μg/mL), MDA-MB-231(IC50>10μg/mL), A549(IC50>10μg/mL), DU145(IC50>10μg/mL), BEL-7402(IC50>10μg/mL).##[Ref.14987049] Cytotoxicity: U-937 GTB (lymphoma)(IC50 =" DRAVPe00298 DRAVPe00298.cif Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L Not found No machanism information found in the reference(s) presented in this entry 2916.34 C117H187N35O40S6 ADFHKMQY C 5.96 1 1 0 19 5 15.86 -1946 30 hour >20 hour >10 hour 46.9 5875 209.82 18008336##20580652 Biopolymers. 2008;90(1):51-60.##Peptides. 2010 Aug;31(8):1434-40. "Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N." Cyclotides as natural anti-HIV agents.##Isolation and characterization of cytotoxic cyclotides from Viola tricolor. 10.1002/bip.20886##10.1016/j.peptides.2010.05.004 Anti-HIV DRAVPe00299 ACYCRIPACIAGERRYGTCIYQGRLWAFCC 30 "Neutrophil defensin 1 (Defensin, alpha 1; HNP-1, HP-1; Human, mammals, animals)" Homo sapiens (Human) P59665##P11479##Q14125##Q6EZF6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2KHT SARS-CoV-2 Coronaviridae [Ref.34206990]SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM));##SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(67% inbibition at 50 μg/mL);##SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(58% inbibition at 50 μg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL. DRAVPe00299 DRAVPe00299.cif Cyclic Free Cyclization(Cys2 and Cys30). "Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29." L Not found No machanism information found in the reference(s) presented in this entry 3448.09 C150H228N44O38S6 DHKMNSV C 8.68 4 1 3 13 10 30 -3229 4.4 hour >20 hour >10 hour 65.33 10345 356.72 34206990 Viruses. 2021 Jun 26;13(7):1246. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL." Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry. 10.3390/v13071246 DRAVPa1304 Anti-SARS-CoV-2 DRAVPe00300 CYCRIPACIAGERRYGTCIYQGRLWAFCC 29 "Neutrophil defensin 2 (HNP-2, HP-2, HP2; Human, mammals, animals)" Homo sapiens (Human) P59665##P11479##Q14125##Q6EZF6##P59666##P11479##Q14125 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZMH##1ZMI##1ZMK SARS-CoV-2 Coronaviridae [Ref.34206990]SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM)). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00300 DRAVPe00300.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys1 and Cys29,Cys3 and Cys18,Cys8 and Cys28." L Not found No machanism information found in the reference(s) presented in this entry 3377.01 C147H223N43O37S6 DHKMNSV C 8.67 4 1 3 13 9 24.83 -3410 1.2 hour >20 hour >10 hour 64.14 10345 369.46 34206990 Viruses. 2021 Jun 26;13(7):1246. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL." Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry. 10.3390/v13071246 Anti-SARS-CoV-2 DRAVPe00301 DCYCRIPACIAGERRYGTCIYQGRLWAFCC 30 "Neutrophil defensin 3 (Defensin, alpha 3; HNP-3, HP-3, HP3; Human, mammals, animals)" Homo sapiens (Human) P59666##P11479##Q14125 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DFN##2PM4##2PM5 SARS-CoV-2 Coronaviridae [Ref.34206990]SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM)). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00301 DRAVPe00301.cif Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) "Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29." L Not found No machanism information found in the reference(s) presented in this entry 3492.1 C151H228N44O40S6 HKMNSV C 8.33 4 2 2 13 9 12.33 -4282 1.1 hour 3 min >10 hour 62 10345 356.72 34206990 Viruses. 2021 Jun 26;13(7):1246. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL." Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry. 10.3390/v13071246 Anti-SARS-CoV-2 DRAVPe00302 VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV 33 "Neutrophil defensin 4 (Defensin, alpha 4; HNP-4, HP-4; Human, mammals, animals)" Homo sapiens (Human) P12838 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZMM SARS-CoV-2 Coronaviridae [Ref.34206990]SARS-CoV-2: showed inhibition against SARS-CoV-2. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00302 DRAVPe00302.cif Cyclic Free Free "Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29." L Not found No machanism information found in the reference(s) presented in this entry 3715.46 C157H261N49O43S6 ADHKMPQW C 8.98 5 1 4 16 11 66.06 -4636 100 hour >20 hour >10 hour 91.21 1865 58.28 34206990 Viruses. 2021 Jun 26;13(7):1246. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL." Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry. 10.3390/v13071246 Anti-SARS-CoV-2 DRAVPe00303 AFTCHCRRSCYSTEYSYGTCTVMGINHRFCCL 32 "Human defensin-6 (HD-6; Defensin, alpha 6; Human, mammals, animals)" Homo sapiens (Human) Q01524 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZMQ##3QTE SARS-CoV-2 Coronaviridae "[Ref.34206990]SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(HD6 only blocked SARS-CoV-2 infection at the highest concentration tested (50 μg/mL, 13 μM))." No hemolysis information or data found in the reference(s) presented in this entry [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL. DRAVPe00303 DRAVPe00303.cif Cyclic Free Free "Disulfide bonds between Cys4 and Cys31,Cys6 and Cys20,Cys10 and Cys30." L Not found No machanism information found in the reference(s) presented in this entry 3714.27 C156H234N46O46S7 DKPQW C 8.35 5 1 4 19 6 0 -5487 4.4 hour >20 hour >10 hour 36.56 4845 156.29 34206990 Viruses. 2021 Jun 26;13(7):1246. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL." Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry. 10.3390/v13071246 Anti-SARS-CoV-2 DRAVPe00304 GWFDVVKHIAKRF 13 D70(Derived from Uperin 7.1) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=2.99 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 10.6 µM. DRAVPe00304 DRAVPe00304.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1602.9 C78H115N21O16 CELMNPQSTY FKV 9.99 4 1 3 1 7 0 -1536 30 hour >20 hour >10 hour 82.31 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00305 VDKPDYRPRPRPPNM 15 "Metalnikowin-1 (Metalnikowin I; Insects, animals)" Palomena prasina (Green shield bug) (Cimex prasinus) P80408 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>54.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >54.4 µM. DRAVPe00305 DRAVPe00305.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1838.12 C80H128N26O22S ACEFGHILQSTW P 9.98 4 2 2 2 1 -207.33 -6814 100 hour >20 hour >10 hour 19.33 1490 106.43 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00306 FLFPLITSFLSKVL 14 "Ranatuerin-9 (Frogs, amphibians, animals)" Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) P82824 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=16.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 34.6 µM. DRAVPe00306 DRAVPe00306.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1625.03 C83H129N15O18 ACDEGHMNQRWY L 8.75 1 0 1 3 9 175 2266 1.1 hour 3 min 2 min 160 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00307 INLKAIAALAKKLL 14 Mastoparan M Hornet Vespa mandarinia P04205 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>67.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >67.6 µM. DRAVPe00307 DRAVPe00307.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1479.91 C70H130N18O16 CDEFGHMPQRSTVWY AL 10.3 3 0 3 1 10 115.71 1347 20 hour 30 min >10 hour 195.71 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00308 IKWKKLLRAAKRIL 14 "DASamP2(D74,derived from polybia-MPI)" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>57.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 1.3 µM. DRAVPe00308 DRAVPe00308.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1737.25 C83H149N25O15 CDEFGHMNPQSTVY K 12.03 6 0 6 0 8 -10.71 -2149 20 hour 30 min >10 hour 153.57 5500 423.08 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00309 FRPALIVRTKGTRL 14 Hyposin-5 (frog) Phyllomedusa hypochondrialis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>61.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >61.4 µM. DRAVPe00309 DRAVPe00309.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1628 C74H130N24O17 CDEHMNQSWY R 12.3 4 0 4 3 6 0.71 -3092 1.1 hour 3 min 2 min 111.43 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00310 FFGKVLKLIRKIF 13 "DASamP1(D76,derived from temporin-PTa)" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=0.63 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 6.78 µM. DRAVPe00310 DRAVPe00310.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1609.08 C82H133N19O14 ACDEHMNPQSTWY FK 11.26 4 0 4 1 8 96.92 203 1.1 hour 3 min 2 min 142.31 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00311 GNNRPVYIPQPRPPHPRI 18 Apidaecin IA (insect) Apis mellifera L P35581 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>47.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >47.4 µM. DRAVPe00311 DRAVPe00311.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2108.44 C95H150N32O23 ACDEFKLMSTW P 11.71 4 0 4 4 3 -140.56 -5356 30 hour >20 hour >10 hour 59.44 1490 87.65 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00312 GKPRPYSPRPTSHPRPIRV 19 Drosocin (insect) Drosophila melanogaster No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 4EZR HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>45.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >45.5 µM. DRAVPe00312 DRAVPe00312.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2198.56 C98H160N34O24 ACDEFLMNQW P 12.01 6 0 6 5 2 -157.89 -6950 30 hour >20 hour >10 hour 35.79 1490 82.78 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00313 VFQFLGRIIHHVGNFVHGFSHVF 23 "Clavanin-B (His-rich; chordates, animals)" Styela clava (Sea squirt) P80711 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=7.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 37.1 µM. DRAVPe00313 DRAVPe00313.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2695.13 C131H184N36O27 ACDEKMPTWY F 9.75 5 0 5 5 12 75.22 -50 100 hour >20 hour >10 hour 101.3 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00314 TRSSRAGLQFPVGRVHRLLRK 21 Buforin II (toad) Synthetic construct(derived from buforin I after treatment with endoproteinase) P55897 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>41.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >41.1 µM. DRAVPe00314 DRAVPe00314.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2434.88 C106H184N40O26 CDEIMNWY R 12.6 7 0 7 5 7 -63.81 -7021 7.2 hour >20 hour >10 hour 88.1 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00315 GFGKAFHSVSNFAKKHKTA 19 Styelin A (tunicate) Styela clava P81469 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>48.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >48.5 µM. DRAVPe00315 DRAVPe00315.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2062.36 C95H144N28O24 CDEILMPQRWY K 10.48 6 0 6 6 7 -55.79 -2724 30 hour >20 hour >10 hour 31.05 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00316 LLKELWTKIKGAGKAVLGKIKGLL 24 "Ponericin-L2 (ants, insects, animals)" Pachycondyla goeldii (Ponerine ant) P82422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 24.7 µM. DRAVPe00316 DRAVPe00316.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2578.27 C123H217N31O28 CDFHMNPQRSY KL 10.3 6 1 5 5 12 39.58 1043 5.5 hour 3 min 2 min 150.42 5500 239.13 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00317 HVDKKVADKVLLLKQLRIMRLLTRL 25 "Spinigerin (Insects, animals)" Pseudacanthotermes spiniger (Termite) P82357 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZRW##1ZRV HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=3.05 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >33.3 µM. DRAVPe00317 DRAVPe00317.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3000.77 C136H247N41O32S CEFGNPSWY L 11.07 8 2 6 1 12 15.6 -4153 3.5 hour 10 min >10 hour 163.6 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00318 GLNTLKKVFQGLHEAIKLINNHVQ 24 Pseudin 1 (frog) Pseudis paradoxa P83188 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=35.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >36.8 µM. DRAVPe00318 DRAVPe00318.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2715.19 C123H204N36O33 CDMPRSWY L 9.7 5 1 4 6 10 -14.17 -2208 30 hour >20 hour >10 hour 125.83 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00319 RQRVEELSKFSKKGAAARRRK 21 Misgurin (fish) Misgurnus anguillicaudatus P81474 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>40.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >40.0 µM. DRAVPe00319 DRAVPe00319.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2501.92 C106H189N41O29 CDHIMNPTWY R 11.84 9 2 7 3 6 -163.81 -10445 1 hour 2 min 2 min 46.67 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00320 NLVSGLIEARKYLEQLHRKLKNRKV 25 D88 (frog) Synthetic construct(derived from chain A of distinctin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>33.3 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >33.3 µM. DRAVPe00320 DRAVPe00320.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3006.59 C134H233N43O35 CDFMPTW L 10.55 8 2 6 5 9 -74.4 -6725 1.4 hour 3 min >10 hour 120.8 1490 62.08 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00321 IWLTALKFLGKHAAKHLAKQQLSKL 25 Lycotoxin I (spider) Lycosa carolinensis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 7MMM HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>35.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 2.4 µM. DRAVPe00321 DRAVPe00321.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2844.49 C135H223N37O30 CDEMNPRVY L 10.6 7 0 7 3 13 6.4 -619 20 hour 30 min >10 hour 125.2 5500 229.17 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00322 GLFDIIKKIAESW 13 B1(derived from Aurein 1.2) Synthetic construct(derived from Aurein 1.2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=11.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 37.0 µM. DRAVPe00322 DRAVPe00322.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00323 GLWEKIDKFASII 13 B2(derived from Caerin 3.2) Synthetic construct(derived from Caerin 3.2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>65.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00323 DRAVPe00323.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00324 GIIDIAKKLFESW 13 B3(derived from Uperin 2.7) Synthetic construct(derived from Uperin 2.7) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=20.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00324 DRAVPe00324.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00325 GWFDIIKKIASEL 13 B4(derived from Uperin 7.1) Synthetic construct(derived from Uperin 7.1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=10.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 38.9 µM. DRAVPe00325 DRAVPe00325.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00326 GIFDKLAKEISIW 13 B5(derived from Brevinin-2DYd) Synthetic construct(derived from Brevinin-2DYd) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>65.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00326 DRAVPe00326.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00327 GIWSDLAEIIKKF 13 B6(derived from Ponericin W3) Synthetic construct(derived from Ponericin W3) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=11.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00327 DRAVPe00327.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00328 GFLDIIEKIAKSW 13 B7(derived from Ranatuerin 3) Synthetic construct(derived from Ranatuerin 3) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=10.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00328 DRAVPe00328.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00329 GWLKKIESIIDAF 13 B8(derived from Cecropin) Synthetic construct(derived from Cecropin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=29.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. DRAVPe00329 DRAVPe00329.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1519.8 C73H114N16O19 CHMNPQRTVY I 6.07 2 2 0 2 7 38.46 -229 30 hour >20 hour >10 hour 127.69 5500 458.33 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00330 ILGPVLGLVSDTLDDVLGIL 20 Maximin H5 Bombina maxima No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>49.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >49.7 µM. DRAVPe00330 DRAVPe00330.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2022.41 C93H160N20O29 ACEFHKMNQRWY L 3.42 0 3 -3 5 11 148 2217 20 hour 30 min >10 hour 199.5 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00331 ILGPVLGLVSRTLRRVLGIL 20 Maximin H5r3 Synthetic construct(derived from Maximin H5) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=2.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 8.7 µM. DRAVPe00331 DRAVPe00331.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2145.71 C99H181N29O23 ACDEFHKMNQWY L 12.3 3 0 3 5 11 133 357 20 hour 30 min >10 hour 199.5 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00332 GFKRIVQRIKDFLRNLV 17 GF-17 Synthetic construct(derived from LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV, EBOV" "Retroviridae, Filoviridae" Plaque assay [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=0.76 μM);##[Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.98 μM).(EC50:50% effective concentration for inhibition of virus replication);##[Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=10.1 µM);inhibition of viral infection in primary macrophages(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 10.8 µM.##[Ref.18591279]CEM-SS cells:TC50=8.9 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe00332 DRAVPe00332.cif Linear Free Amidation None L Not found "Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry." 2102.56 C97H164N30O22 ACEHMPSTWY R 11.72 5 1 4 2 8 -9.41 -4210 30 hour >20 hour >10 hour 125.88 0 0 20086159##18591279##32252021 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40. ##iScience. 2020 Apr 24;23(4):100999. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Wang G, Watson KM, Buckheit RW Jr. ##Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins.##Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. 10.1128/AAC.01448-09##10.1128/AAC.00452-08##10.1016/j.isci.2020.100999 "Anti-HIV, Anti-EBOV" DRAVPe00333 GFNEIVQDIEDFLQNLV 17 GF-17− Synthetic construct(derived from LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>25.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >25.1 µM. DRAVPe00333 DRAVPe00333.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1993.2 C90H137N21O30 ACHKMPRSTWY DEFILNQV 3.43 0 4 -4 3 8 12.94 -2076 30 hour >20 hour >10 hour 125.88 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00334 GLRSKIWLWVLLMIWQESNKFKKM 24 DRS S9 Synthetic construct(derived from Dermaseptin S9) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=31.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >32.9 µM. DRAVPe00334 DRAVPe00334.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3035.75 C145H228N36O31S2 ACDHPTY KL 10.46 5 1 4 4 11 -1.25 -1374 30 hour >20 hour >10 hour 109.58 16500 717.39 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00335 GLRSRIWLWVLLMIWQESNRFKRM 24 DRS S9r3 Synthetic construct(derived from Dermaseptin S9) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >32.1 µM. DRAVPe00335 DRAVPe00335.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3119.79 C145H228N42O31S2 ACDHPTY LR 12 5 1 4 4 11 -8.75 -4185 30 hour >20 hour >10 hour 109.58 16500 717.39 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00336 GLKKLLGKLLKKLGKLLLK 19 GLK-19 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>47.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 25.1 µM. DRAVPe00336 DRAVPe00336.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2104.82 C102H194N26O20 ACDEFHIMNPQRSTVWY L 10.78 7 0 7 3 9 30 825 30 hour >20 hour >10 hour 184.74 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00337 GLRRLLGRLLRRLGRLLLR 19 GLR-19 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=4.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 25.7 µM. DRAVPe00337 DRAVPe00337.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2300.92 C102H194N40O20 ACDEFHIKMNPQSTVWY L 12.78 7 0 7 3 9 7.89 -5734 30 hour >20 hour >10 hour 184.74 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00338 KGRGKQGGKVRAKAKTRSS 19 Parasin I (fish) Parasilurus asotus No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>50.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >50.0 µM. DRAVPe00338 DRAVPe00338.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2000.34 C82H154N34O24 CDEFHILMNPWY K 12.32 8 0 8 7 3 -171.58 -7600 1.3 hour 3 min 2 min 25.79 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00339 GIWDTIKSMGKVFAGKILQNL 21 "Brevinin-2-related peptide (Frogs, amphibians, animals)" Rana septentrionalis (mink frog) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=1.65 μM). [Ref.15556063]HC50=70 µM against human erythrocytes [Ref.20086159]CEM-SS cells:50% Cell death at 7.42 µM. DRAVPe00339 DRAVPe00339.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2319.79 C107H175N27O28S CEHPRY GIK 9.7 3 1 2 6 9 28.57 -259 30 hour >20 hour >10 hour 111.43 5500 275 20086159##15556063 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). 10.1128/AAC.01448-09##10.1016/j.cca.2004.08.019 Anti-HIV DRAVPe00340 GLLGLLGSVVSHVVPAIVGHF 21 "Maculatin-1.3 (frog, amphibia, animals)" Litoria eucnemis (Australian anurans) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=4.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 8.02 µM. DRAVPe00340 DRAVPe00340.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2071.49 C98H159N25O24 CDEKMNQRTWY V 6.92 2 0 2 6 12 162.38 3723 30 hour >20 hour >10 hour 166.67 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00341 SWKSMAKKLKEYMEKLKQRA 20 "M-zodatoxin-Lt3a (M-ZDTX-Lt3a; Latarcin-3a, Ltc-3a; spiders, Arthropods, animals)" Lachesana tarabaevi (Spider) Q1ELU3 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=32.7 μM). [Ref.16735513]20% hemolytic activity at >120 μM against rabbit erythrocytes [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >40.3 µM. DRAVPe00341 DRAVPe00341.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2484.02 C111H187N31O29S2 CDFGHINPTV K 10.12 7 2 5 3 5 -136 -5383 1.9 hour >20 hour >10 hour 49 6990 367.89 20086159##16735513 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##J Biol Chem. 2006 Jul 28;281(30):20983-209892. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV." "Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity." 10.1128/AAC.01448-09##10.1074/jbc.M602168200 Anti-HIV DRAVPe00342 GAWKNFWSSLRKGFYDGEAGRAIRR 25 D94 (bacteria) Synthetic construct(derived from chain A of plantaricin JK) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>34.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >34.1 µM. DRAVPe00342 DRAVPe00342.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2929.3 C133H198N42O34 CHMPQTV GR 10.93 6 2 4 8 9 -93.2 -7024 30 hour >20 hour >10 hour 43.2 12490 520.42 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00343 GFKDLLKGAAKALVKTVLF 19 "Ascaphin-8 (Frogs, amphibians, animals)" Ascaphus truei (Coastal tailed frog) P0CJ32 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=1.2 μM). [Ref.15207717]HC50=50 μM against human erythrocytes [Ref.20086159]CEM-SS cells:50% Cell death at 2.9 µM. DRAVPe00343 DRAVPe00343.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2019.5 C97H163N23O23 CEHIMNPQRSWY KL 10 4 1 3 3 11 73.68 754 30 hour >20 hour >10 hour 128.42 0 0 20086159##15207717 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF." "Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei." 10.1128/AAC.01448-09##10.1016/j.bbrc.2004.05.141 Anti-HIV DRAVPe00344 GLADFLNKAVGKVVDFVKS 19 Desertcolin 1 (frog) Crinia deserticola No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>49.9 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >49.9 µM. DRAVPe00344 DRAVPe00344.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2007.36 C93H151N23O26 CEHIMPQRTWY V 8.5 3 2 1 4 10 51.58 -667 30 hour >20 hour >10 hour 112.63 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00345 GFLSILKKVLPKVMAHMK 18 "Melectin (MEP; Insects, animals)" Melecta albifrons (Cuckoo bee) (Melecta punctata) P86170 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=4.34 μM). [Ref.18942691]LC50>100 μM against rat red blood cells [Ref.20086159]CEM-SS cells:50% Cell death at 7.75 µM. DRAVPe00345 DRAVPe00345.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2040.64 C96H166N24O20S2 CDENQRTWY K 10.48 5 0 5 2 8 61.67 793 30 hour >20 hour >10 hour 124.44 0 0 20086159##18942691 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Chembiochem. 2008 Nov 24;9(17):2815-2821. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Cerovský V, Hovorka O, Cvacka J, Voburka Z, Bednárová L, Borovicková L, Slaninová J, Fucík V." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Melectin: a novel antimicrobial peptide from the venom of the cleptoparasitic bee Melecta albifrons. 10.1128/AAC.01448-09##10.1002/cbic.200800476 Anti-HIV DRAVPe00346 SLSRFLRFLKIVYRRAF 17 "D98 (frog,derived from temporin-LTc)" Synthetic construct(derived from temporin-LTc) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=0.83 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 8.6 µM. DRAVPe00346 DRAVPe00346.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2172.65 C104H166N30O21 CDEGHMNPQTW R 12.01 5 0 5 3 9 32.35 -3770 1.9 hour >20 hour >10 hour 114.71 1490 93.13 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00347 RPKHPIKHQGLPQEVLNENLLRF 23 Isracidin (cow) bovine colostrum No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>36.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >36.2 µM. DRAVPe00347 DRAVPe00347.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2764.23 C125H203N39O32 ACDMSTWY L 9.99 6 2 4 3 7 -98.7 -5568 1 hour 2 min 2 min 97.39 0 0 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. 10.1128/AAC.01448-09 Anti-HIV DRAVPe00348 GIGTKILGGVKTALKGALKELASTYAN 27 "Maximin-1 (Toads, amphibians, animals)" Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) P83080##Q58T87 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "[Ref.11835991]HIV-1:inhibition the cytopathic effects of HIV-1 (IC50=15.5 µg/ml, EC50=21.4 µg/ml).##NOTE: IC50 means the concentration that can inhibit 50% growth of cells. EC50 was defined as the concentration of antiviral agent reducing HIV-1 replication by 50%." [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells No cytotoxicity information found in the reference(s) presented DRAVPe00348 DRAVPe00348.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2675.16 C120H208N32O36 CDFHMPQRW G 9.83 4 1 3 11 11 25.19 -140 30 hour >20 hour >10 hour 112.22 1490 57.31 11835991 Peptides. 2002 Mar;23(3):427-435. "Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y." Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Anti-HIV DRAVPe00349 GIGGKILSGLKTALKGAAKELASTYLH 27 "Maximin-3 (Toads, amphibians, animals)" Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) P83082##Q58T40##Q58T43##Q58T46##Q58T48##Q58T64##Q58T65##Q58T68##Q58T69 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "[Ref.11835991]HIV-1:inhibition the cytopathic effects of HIV-1 (IC50=11.4 µg/ml, EC50=1.5 µg/ml).##NOTE: IC50 means the concentration that can inhibit 50% growth of cells. EC50 was defined as the concentration of antiviral agent reducing HIV-1 replication by 50%." [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells No cytotoxicity information found in the reference(s) presented DRAVPe00349 DRAVPe00349.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2698.2 C122H209N33O35 CDFMNPQRVW GL 9.83 5 1 4 10 11 24.44 63 30 hour >20 hour >10 hour 115.93 1490 57.31 11835991 Peptides. 2002 Mar;23(3):427-435. "Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y." Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Anti-HIV DRAVPe00350 GIGGVLLSAGKAALKGLAKVLAEKYAN 27 "Maximin-4 (Toads, amphibians, animals)" Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) P83083##Q58T42##Q58T44##Q58T52##Q58T62##Q58T77##Q58T79 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2MHW HIV Retroviridae "[Ref.11835991]HIV-1:inhibition the cytopathic effects of HIV-1 (IC50=24.2 µg/ml, EC50=21.9 µg/ml).##NOTE: IC50 means the concentration that can inhibit 50% growth of cells. EC50 was defined as the concentration of antiviral agent reducing HIV-1 replication by 50%." [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells No cytotoxicity information found in the reference(s) presented DRAVPe00350 DRAVPe00350.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2613.14 C119H206N32O33 CDFHMPQRTW A 9.83 4 1 3 8 14 59.26 1397 30 hour >20 hour >10 hour 130.37 1490 57.31 11835991 Peptides. 2002 Mar;23(3):427-435. "Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y." Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Anti-HIV DRAVPe00351 SIGAKILGGVKTFFKGALKELASTYLQ 27 "Maximin-5 (Toads, amphibians, animals)" Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) P83084##Q58T60##Q58T61 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "[Ref.11835991]HIV-1:inhibition the cytopathic effects of HIV-1 (IC50=34.4 µg/ml, EC50=39.8 µg/ml).##NOTE: IC50 means the concentration that can inhibit 50% growth of cells. EC50 was defined as the concentration of antiviral agent reducing HIV-1 replication by 50%." [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells No cytotoxicity information found in the reference(s) presented DRAVPe00351 DRAVPe00351.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2841.39 C133H218N32O36 CDHMNPRW GKL 9.82 4 1 3 9 12 40.37 208 1.9 hour >20 hour >10 hour 108.52 1490 57.31 11835991 Peptides. 2002 Mar;23(3):427-435. "Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y." Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Anti-HIV DRAVPe00352 GLFGVLAKVAAHVVPAIAEHF 21 Maculatin-1.1 Litoria genimaculata (Green-eyed tree frog) P82066 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.16140737]HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=11.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00352 DRAVPe00352.cif Linear Free Amidation None L membrane "The peptide could prevent HIV infection by disrupting the integrity of the virion membrane, and inhibit the transfer of HIV from DCs to T cells." 2146.56 C103H160N26O24 CDMNQRSTWY A 6.92 3 1 2 2 14 130 2613 30 hour >20 hour >10 hour 134.76 0 0 16140737 J Virol. 2005 Sep;79(18):11598-606. "VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D." Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells. 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe00353 GLLSVLGSVAKHVLPHVVPVIAEHL 25 Caerin-1.1 Litoria splendida (Magnificent tree frog) (Litoria gilleni) (Litoria caerulea) P62568##P62569##Q800R2##P56226 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.16140737]HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=7.8 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=12.6 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00353 DRAVPe00353.cif Linear Free Amidation None L membrane "The peptide could prevent HIV infection by disrupting the integrity of the virion membrane, and inhibit the transfer of HIV from DCs to T cells." 2585.13 C121H202N32O30 CDFMNQRTWY V 7.02 4 1 3 4 14 118.8 2612 30 hour >20 hour >10 hour 171.2 0 0 16140737 J Virol. 2005 Sep;79(18):11598-606. "VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D." Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells. 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe00354 GLFGVLGSIAKHVLPHVVPVIAEKL 25 Caerin 1.9 Litoria chloris P81252 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=4 µM).##[Ref.16140737]Human immunodeficiency virus (HIV):inhibit 50% of PBS-treated HIV infection of T cells(IC50=1.2 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=1.6 μM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 20 µM." DRAVPe00354 DRAVPe00354.cif Linear Free Amidation None L virion envelope "Prevent HIV infection by disrupting the integrity of the virion membrane at concentrations that are not toxic to target cells, the peptide also inhibit the transfer of HIV from DCs to T cells." 2594.18 C124H205N31O29 CDMNQRTWY V 8.61 4 1 3 4 14 114.8 2851 30 hour >20 hour >10 hour 159.6 0 0 26026377##16140737##33008028 Peptides. 2015 Sep;71:296-303.##J Virol. 2005 Sep;79(18):11598-606.##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.1128/JVI.79.18.11598-11606.2005##10.3390/antibiotics9100661 Anti-HIV DRAVPe00355 GLFSVLGAVAKHVLPHVVPVIAEKL 25 Caerin-1.6 Litoria xanthomera (Orange-thighed frog) (Litoria chloris) P62546##P56231##P81249##P62547 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 10 µM." DRAVPe00355 DRAVPe00355.cif Linear Free Amidation None L membrane "The peptide could disrupt the viral envelope and release p24 protein.And the more effective they were at disruption of the viral envelope, the better they were at inhibiting infection." 2594.18 C124H205N31O29 CDMNQRTWY V 8.61 4 1 3 3 15 122.4 2850 30 hour >20 hour >10 hour 159.6 0 0 26026377 Peptides. 2015 Sep;71:296-303. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." Inhibition of HIV infection by caerin 1 antimicrobial peptides. 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00356 GLFKVLGSVAKHLLPHVAPVIAEKL 25 Caerin-1.7 Litoria xanthomera (Orange-thighed frog) (Litoria chloris) P62548##P62549##P56232##P81250 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 12.5 µM. DRAVPe00356 DRAVPe00356.cif Linear Free Amidation None L membrane "The peptide could disrupt the viral envelope and release p24 protein.And the more effective they were at disruption of the viral envelope, the better they were at inhibiting infection." 2637.25 C126H210N32O29 CDMNQRTWY L 9.7 5 1 4 3 14 88.4 1979 30 hour >20 hour >10 hour 152 0 0 26026377 Peptides. 2015 Sep;71:296-303. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." Inhibition of HIV infection by caerin 1 antimicrobial peptides. 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00357 GLFKVLGSVAKHLLPHVAPIIAEKL 25 Caerin-1.19 Litoria gracilenta (Dainty green tree frog) P0C2A8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00357 DRAVPe00357.cif Linear Free Amidation None L membrane "The peptide could disrupt the viral envelope and release p24 protein.And the more effective they were at disruption of the viral envelope, the better they were at inhibiting infection." 2651.28 C127H212N32O29 CDMNQRTWY L 9.7 5 1 4 3 14 89.6 2067 30 hour >20 hour >10 hour 156 0 0 26026377 Peptides. 2015 Sep;71:296-303. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." Inhibition of HIV infection by caerin 1 antimicrobial peptides. 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00358 GLLSVLGSVAKHVLPHVVPVIAEKL 25 Caerin 1.10 Litoria splendida P86502##P82104 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 22 µM." DRAVPe00358 DRAVPe00358.cif Linear Free Amidation None L virion envelope Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2576.16 C121H207N31O30 CDFMNQRTWY V 8.61 4 1 3 4 14 116 2523 30 hour >20 hour >10 hour 171.2 0 0 26026377##33008028 Peptides. 2015 Sep;71:296-303.##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.3390/antibiotics9100661 Anti-HIV DRAVPe00359 GLLGVLGSVAKHVLPHVVPVIAEHL 25 Caerin 1.2 Litoria caerulea P56227 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=5 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 22 µM." DRAVPe00359 DRAVPe00359.cif Linear Free Amidation None L virion envelope Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2555.11 C120H200N32O29 CDFMNQRTWY V 7.02 4 1 3 4 14 120.4 3046 30 hour >20 hour >10 hour 171.2 0 0 26026377##33008028 Peptides. 2015 Sep;71:296-303.##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.3390/antibiotics9100661 Anti-HIV DRAVPe00360 GLLSVLGSVVKHVIPHVVPVIAEHL 25 Caerin-1.5 Litoria caerulea (Green tree frog) P56230 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 12.5 µM. DRAVPe00360 DRAVPe00360.cif Linear Free Amidation None L membrane "The peptide could disrupt the viral envelope and release p24 protein.And the more effective they were at disruption of the viral envelope, the better they were at inhibiting infection." 2613.19 C123H206N32O30 CDFMNQRTWY V 7.02 4 1 3 4 14 131.2 2835 30 hour >20 hour >10 hour 178.8 0 0 26026377 Peptides. 2015 Sep;71:296-303. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." Inhibition of HIV infection by caerin 1 antimicrobial peptides. 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00361 GLLSVLGSVAKHVLPHVVPVIAAAL 25 "Caerin 1.1 mod 7(Caerin 1.1 [E23A,H24A])" Sythetic construct(derived from Caerin 1.1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00361 DRAVPe00361.cif Linear Free Amidation None L virion envelope [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2461.03 C116H198N30O28 CDEFMNQRTWY V 8.76 3 0 3 4 16 160 4121 30 hour >20 hour >10 hour 179.2 0 0 26026377##33008028 Peptides. 2015 Sep;71:296-303. ##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.3390/antibiotics9100661 Anti-HIV DRAVPe00362 GLLSVLGSVAKHVLPHVVPVIAKLH 25 "Caerin 1.1 mod 9(Caerin 1.1 [E23K,H24L,L25H])" Sythetic construct(derived from Caerin 1.1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 17 µM." DRAVPe00362 DRAVPe00362.cif Linear Free Amidation None L virion envelope [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2584.19 C122H207N33O28 CDEFMNQRTWY V 10 5 0 5 4 14 117.2 2738 30 hour >20 hour >10 hour 171.2 0 0 26026377 Peptides. 2015 Sep;71:296-303. Inhibition of HIV infection by caerin 1 antimicrobial peptides. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00363 GLLKVLGSVAKKVLPKVVPVIAEKL 25 "Caerin 1.1 mod 10(Caerin 1.1 [S4K;H12K,H16K,H24K])" Sythetic construct(derived from Caerin 1.1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=4 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00363 DRAVPe00363.cif Linear Free Amidation None L virion envelope [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2599.33 C124H224N30O29 CDFHMNQRTWY V 10.18 5 1 4 3 14 98 2130 30 hour >20 hour >10 hour 171.2 0 0 26026377 Peptides. 2015 Sep;71:296-303. Inhibition of HIV infection by caerin 1 antimicrobial peptides. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA." 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe00364 GLFGVLGSIAKHLLPHVVPVIAEKL 25 Caerin 1.9 sm(Caerin 1.9 [V13L]) Sythetic construct(derived from Caerin 1.9) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.26026377]CD4+ T Lymphocytes:50% cell death at 17.5 µM. DRAVPe00364 DRAVPe00364.cif Linear Free Amidation None L virion envelope [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2608.21 C125H207N31O29 CDMNQRTWY L 8.61 4 1 3 4 14 113.2 2939 30 hour >20 hour >10 hour 163.6 0 0 26026377##33008028 Peptides. 2015 Sep;71:296-303. ##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.3390/antibiotics9100661 Anti-HIV DRAVPe00365 GLFGILGSVAKHVLPHVIPVVAEHL 25 Caerin 1.20 Litoria caerulea/Litoria splendida No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 25 µM;Human endocervical cells End1/E6E7:50% cell death at 22 µM." DRAVPe00365 DRAVPe00365.cif Linear Free Amidation None L virion envelope [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). 2603.15 C124H200N32O29 CDMNQRTWY V 7.02 4 1 3 4 14 117.6 2940 30 hour >20 hour >10 hour 159.6 0 0 26026377##33008028 Peptides. 2015 Sep;71:296-303.##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. "VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK." 10.1016/j.peptides.2015.05.004##10.3390/antibiotics9100661 Anti-HIV DRAVPe00366 FLGFLKNLF 9 "Ctry2459-WT (Ctry2459, scorpions,animals)" Chaerilus tryznai (Scorpion) P0DMF3 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.23415044]Hepatitis C virus:inhibition of infection with HCV in Huh 7.5.1 cells (EC50=1.84 μg/ml). [Ref.23415044] HC50 = 137.9 μg/ml against human red blood cells. [Ref.23415044] CC50=79.8 μg/ml against Huh7.5.1 cells. DRAVPe00366 DRAVPe00366.cif Linear Free Free None L Not found "The peptide potently destabilizes the viral structural integrity, thus reducing the initiation of HCV infection" 1098.35 C57H83N11O11 ACDEHIMPQRSTVWY FL 8.75 1 0 1 2 6 133.33 1245 1.1 hour 3 min 2 min 130 0 0 23415044 Biomaterials. 2013 Apr;34(13):3511-22. "Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z." Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. 10.1016/j.biomaterials.2013.01.075 Anti-HCV DRAVPe00367 FLGFLHHLF 9 "Ctry2459-H2 (Ctry2459 peptide derivative, His-rich)" Synthetic construct( from a scorpion venom peptide library) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.23415044]Hepatitis C virus:inhibition of infection with HCV in Huh 7.5.1 cells (EC50=1.08 μg/ml). [Ref.23415044] HC50 = 203.3 μg/ml against human red blood cells. [Ref.23415044] CC50>500 μg/ml against Huh7.5.1 cells DRAVPe00367 DRAVPe00367.cif Linear Free Amidation None L Not found "The peptide effectively enter the cells, break through the endosomes, interact with the mature viral particles, and exhibit significant antiviral activities." 1130.36 C59H79N13O10 ACDEIKMNPQRSTVWY FL 6.92 2 0 2 1 6 144.44 1532 1.1 hour 3 min 2 min 130 0 0 23415044 Biomaterials. 2013 Apr;34(13):3511-22. "Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z." Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. 10.1016/j.biomaterials.2013.01.075 Anti-HCV DRAVPe00368 FLHFLHHLF 9 "Ctry2459-H3 (Ctry2459 peptide derivative, His-rich)" Synthetic construct(from a scorpion venom peptide library) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.23415044]Hepatitis C virus:inhibition of infection with HCV in Huh 7.5.1 cells (EC50=0.85 μg/ml). [Ref.23415044] HC50 = 416.4 μg/ml against human red blood cells. [Ref.23415044] CC50>500 μg/ml against Huh7.5.1 cells DRAVPe00368 DRAVPe00368.cif Linear Free Amidation None L Not found "The peptide effectively enter the cells, break through the endosomes, interact with the mature viral particles, and exhibit significant antiviral activities." 1210.45 C63H83N15O10 ACDEGIKMNPQRSTVWY FHL 7.02 3 0 3 0 6 113.33 972 1.1 hour 3 min 2 min 130 0 0 23415044 Biomaterials. 2013 Apr;34(13):3511-22. "Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z." Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. 10.1016/j.biomaterials.2013.01.075 Anti-HCV DRAVPe00369 FLPLIGRVLSGIL 13 Temporin A Rana temporaria (European common frog) P56917 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2MAA "CCV,FV3" "Herpesviridae, Iridoviridae" [Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 15 μM);##Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(reduce viral infectivity by 50% at 58 μM). No hemolysis information or data found in the reference(s) presented in this entry DRAVPe00369 DRAVPe00369.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1397.77 C68H116N16O15 ACDEHKMNQTWY L 9.75 1 0 1 3 8 180.77 2010 1.1 hour 3 min 2 min 202.31 0 0 15193922 Virology. 2004 Jun 1;323(2):268-75. "Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1016/j.virol.2004.02.029 "Anti-CCV,Anti-FV3" DRAVPe00370 GMASKAGAIAGKIAKVALKAL 21 PGLa (frog) Xenopus laevis Q99134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HIV,CCV" "Retroviridae, Herpesviridae" [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>50.8 μM).##[Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 100 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >50.8 µM. DRAVPe00370 DRAVPe00370.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1969.46 C88H161N25O23S CDEFHNPQRTWY A 10.48 4 0 4 4 12 84.29 1596 30 hour >20 hour >10 hour 121.43 0 0 20086159##15193922 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Virology. 2004 Jun 1;323(2):268-75. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1128/AAC.01448-09##10.1016/j.virol.2004.02.029 "Anti-HIV,Anti-CCV" DRAVPe00371 FFHHIFRGIVHVGKTIHRLVTG 22 Piscidin-1 Morone saxatilis (Striped bass) Q8UUG0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2JOS##2OJM "CCV,FV3" "Herpesviridae, Iridoviridae" [Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 4 μM);##Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(reduce viral infectivity by 50% at 13 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.11601906]No cytotoxicity against catfish ovary(CCO) cells at 0.25-25μg/ ml. DRAVPe00371 DRAVPe00371.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2572.06 C122H187N37O25 ACDEMNPQSWY H 12.01 7 0 7 5 10 45.45 -1561 1.1 hour 3 min 2 min 110.45 0 0 15193922 Virology. 2004 Jun 1;323(2):268-75. "Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1016/j.virol.2004.02.029 "Anti-CCV,Anti-FV3" DRAVPe00372 FFHHIFRGIVHVGKTIHKLVTG 22 Piscidin-2 Morone chrysops (White bass) Q8UUG2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "CCV,FV3" "Herpesviridae, Iridoviridae" [Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 4 μM);##Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(reduce viral infectivity by 50% at 13 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00372 DRAVPe00372.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2544.05 C122H187N35O25 ACDEMNPQSWY H 11.17 7 0 7 5 10 48.18 -624 1.1 hour 3 min 2 min 110.45 0 0 15193922 Virology. 2004 Jun 1;323(2):268-75. "Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1016/j.virol.2004.02.029 "Anti-CCV,Anti-FV3" DRAVPe00373 FIHHIFRGIVHAGRSIGRFLTG 22 Piscidin 3 (fish) Morone saxatilis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2jos "HIV,CCV,FV3" "Retroviridae, Herpesviridae, Iridoviridae" [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=2.1 μM).##[Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 11 μM);##Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(reduce viral infectivity by 50% at 16 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.20086159]CEM-SS cells:50% Cell death at 6.9 µM. DRAVPe00373 DRAVPe00373.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2491.93 C116H179N37O25 CDEKMNPQWY GI 12.3 6 0 6 6 10 45.45 -2156 1.1 hour 3 min 2 min 106.36 0 0 20086159##15193922 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6.##Virology. 2004 Jun 1;323(2):268-75. "Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr.##Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.##Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1128/AAC.01448-09##10.1016/j.virol.2004.02.029 "Anti-HIV,Anti-CCV,Anti-FV3" DRAVPe00374 GLMDTVKNVAKNLAGHMLDKLKCKITGC 28 "Ranatuerin-2P (Ranatuerin 2P; Frogs, amphibians, animals)" Rana pipiens (Northern leopard frog) Q8QFQ4##P82847 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2K10 "FV3,CCV" "Iridoviridae, Herpesviridae" [Ref.11601906]Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(90% inhibition at 500 µM);##Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(99% inhibition at 50 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00374 DRAVPe00374.cif Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys22 and Cys27. L Not found No machanism information found in the reference(s) presented in this entry 3002.66 C128H225N37O37S4 EFPQRSWY K 9.24 6 2 4 9 9 4.29 -2189 30 hour >20 hour >10 hour 97.5 125 4.63 11601906 Virology. 2001 Sep 30;288(2):351-7. "Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L." "Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin." 10.1006/viro.2001.1080 "Anti-FV3,Anti-CCV" DRAVPe00375 GFLSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC 37 "Esculentin-2P (Frogs, amphibians, animals)" Rana pipiens (northern leopard frog) P82846 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "FV3,CCV" "Iridoviridae, Herpesviridae" [Ref.11601906]##Frog Virus 3: inhibition of FV3 infection in fathead minnow(FHM) cells(90% inhibition at 500 µM);##Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells( 90% inhibition at 50 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00375 DRAVPe00375.cif Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys31 and Cys37. L Not found No machanism information found in the reference(s) presented in this entry 3896.71 C176H296N50O45S2 EHMPTWY GKL 10.21 7 1 6 11 17 48.11 -1869 30 hour >20 hour >10 hour 108.11 125 3.47 11601906 Virology. 2001 Sep 30;288(2):351-7.##Eur J Biochem. 2000 Feb;267(3):894-900. "Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L." "Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin." 10.1006/viro.2001.1080 "Anti-FV3,Anti-CCV" DRAVPe00376 FVQWFSKFLGRIL 13 Temporin L(TL) Rana temporaria (European common frog) P57104 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 6GS5 HSV Herpesviridae "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=8.55 μM,IC90=15.66 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=8.28 μM μM,IC90=16.04 μM)." [Ref.35216177]showing residual hemolytic activity against human erythrocytes only at concentrations equal or above 50 μM. [Ref.35216177]Vero cells:CC50= 19.61 μM DRAVPe00376 DRAVPe00376.cif Linear Free Amidation None L membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1640.99 C83H121N19O16 ACDEHMNPTY F 11 2 0 2 2 8 82.31 160 1.1 hour 3 min 2 min 112.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 Anti-HSV DRAVPe00377 FVPWFSKFlGRIL 13 "Temporin L[Pro3,DLeu9](TL1)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=9.99 μM,IC90=18.69 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=8.86 μM μM,IC90=16.71 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.62 μM μM,IC90=12.14 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=7.76 μM,IC90=30.07 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=7.33 μM,IC90=14.98 μM)." [Ref.35216177]showing residual hemolytic activity against human erythrocytes only at concentrations equal or above 50 μM. [Ref.35216177]Vero cells:CC50= 42.18 μM No predicted structure available DRAVPe00377.cif Linear Free Amidation None Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1609.98 C77H107N17O13 ACDEHMNQTY F 11 2 0 2 2 7 67.69 222 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00378 FVPWFSKFlPRIL 13 "Temporin L[Pro3,DLeu9,Pro10](TL2)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=7.70 μM,IC90=18.76 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=9.83 μM μM,IC90=19.20 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.82 μM μM,IC90=13.98 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=10.56 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=11.31 μM,IC90=24.13 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50= 56.52 μM No predicted structure available DRAVPe00378.cif Linear Free Amidation None Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1650.04 C80H111N17O13 ACDEGHMNQTY F 11 2 0 2 1 7 58.46 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00379 FVPWFSKFlpRIL 13 "Temporin L[Pro3,DLeu9,DPro10](TL3)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50>100 μM No predicted structure available DRAVPe00379.cif Linear Free Amidation None "Mixed(D-Leu9,D-Pro10)" membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1650.04 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00380 FVPWFSKFlXRIL 13 "Temporin L[Pro3,DLeu9,Hyp10](TL4)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=7.73 μM,IC90=15.89 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=9.61 μM μM,IC90=19.02 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=6.72 μM μM,IC90=25.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=11.74 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=11.33 μM,IC90=27.65 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50=60.90 μM No predicted structure available DRAVPe00380.cif Linear Free Amidation The 'X' at position 10 is hydroxyproline (Hyp). Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00381 FVPWFSKFlxRIL 13 "Temporin L[Pro3,DLeu9,DHyp10](TL5)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00381.cif Linear Free Amidation The 'x' at position 10 is D-hydroxyproline (Hyp). "Mixed(D-Leu9,D-Hyp10)" membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00382 FVPWFSKFlxRIL 13 "Temporin L[Pro3,DLeu9,DNle10](TL7)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.65 μM,IC90=12.83 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=3.13 μM μM,IC90=11.92 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=1.00 μM μM,IC90=17.41 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=6.21 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=8.55 μM,IC90=24.74 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50= 32.16 μM No predicted structure available DRAVPe00382.cif Linear Free Amidation The 'x' at position 10 is D-norleucine. "Mixed(D-Leu9,D-Nle10)" membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00383 FVPWFSKFlKRIL 13 "Temporin L[Pro3,DLeu9,Lys10](TL8)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.49 μM,IC90=10.48 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=1.00 μM μM,IC90=7.99 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.88 μM μM,IC90=12.93 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=40.69 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=4.39 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=2.90 μM,IC90=16.30 μM)." [Ref.35216177]About 20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50=22.32 μM No predicted structure available DRAVPe00383.cif Linear Free Amidation None Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1681.1 C81H116N18O13 ACDEGHMNQTY F 11.17 3 0 3 1 7 40.77 -427 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00384 FVPWFSKFlkRIL 13 "Temporin L[Pro3,DLeu9,DLys10](TL9)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.53 μM,IC90=12.71 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=2.80 μM μM,IC90=12.50 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.63 μM μM,IC90=25.33 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=40.64 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=5.39 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=8.29 μM,IC90=29.17 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50= 45.92 μM No predicted structure available DRAVPe00384.cif Linear Free Amidation None "Mixed(D-Leu9,D-Lys10)" membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1681.1 C75H102N16O11 ACDEGHMNQTY F 11.17 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00385 FVPWFSKFlWRIL 13 "Temporin L[Pro3,DLeu9,Trp10](TL10)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.01 μM,IC90=8.25 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.77 μM μM,IC90=12.50 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.88 μM μM,IC90=27.71 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.91 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.96 μM,IC90=24.17 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50= 35.47 μM No predicted structure available DRAVPe00385.cif Linear Free Amidation None Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1739.14 C86H114N18O13 ACDEGHMNQTY F 11 2 0 2 1 8 63.85 361 1.1 hour 3 min 2 min 82.31 11000 916.67 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00386 FVPWFSKFlwRIL 13 "Temporin L[Pro3,DLeu9,DTrp10](TL11)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=1.86 μM,IC90=7.89 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.58 μM μM,IC90=9.76 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.07 μM μM,IC90=14.85 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=41.18 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.92 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=5.10 μM,IC90=17.41 μM)." [Ref.35216177]<40% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50=24.12 μM No predicted structure available DRAVPe00386.cif Linear Free Amidation None "Mixed(D-Leu9,D-Trp10)" membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1739.14 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00387 FVPWFSKFlXRIL 13 "Temporin L[Pro3,DLeu9,Aic10](TL12)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E" "Coronaviridae, Herpesviridae, Paramyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=0.68 μM,IC90=1.58 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.54 μM μM,IC90=11.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.65 μM μM,IC90=13.85 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=33.83 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.74 μM,IC90=20.90 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.62 μM,IC90=13.18 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 12.5 μM. [Ref.35216177]Vero cells:CC50=8.28 μM No predicted structure available DRAVPe00387.cif Linear Free Amidation The 'X' at position 10 is 2-aminoindane-2-carboxylic acid. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E" DRAVPe00388 FVPWFSKFlXRIL 13 "Temporin L[Pro3,DLeu9,Nle10](TL6)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV,HCoV-OC43,HPIV-3,HCoV-229E,MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.66 μM,IC90=9.12 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.92 μM μM,IC90=6.28 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.53 μM μM,IC90=12.15 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=32.35 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=2.08 μM,IC90=13.06 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.97 μM,IC90=10.04 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=34.58 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=2.66 μM,IC90=9.12 μM)." [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. [Ref.35216177]Vero cells:CC50=64.52 μM No predicted structure available DRAVPe00388.cif Linear Free Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV,HCoV-OC43,Anti-HPIV-3,HCoV-229E,Anti-MeV,Anti-H1N1" DRAVPe00389 FVPWFSKFlXRILC 14 "Temporin L[Pro3,DLeu9,Nle10]-C-CHOL(TL6.1)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=6.4 μM,IC90=11.13 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=3.18 μM μM,IC90=12.03 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=39.1 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=5.55 μM,IC90=10.02 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00389.cif Linear Free PEG4-Cholesterol-NH2 The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1767.39 C78H107N17O12S ADEGHMNQTY F 9.51 2 0 2 2 7 83.57 256 1.1 hour 3 min 2 min 76.43 5500 423.08 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00390 FVPWFSKFlXRILGGC 16 "Temporin L[Pro3,DLeu9,Nle10]-GGC-CHOL(TL6.2)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=9.54 μM,IC90=47.95 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=12.12 μM μM,IC90=49.95 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=40.89 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=21.12 μM,IC90=49.90 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00390.cif Linear Free PEG4-Cholesterol-NH2 The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1881.5 C82H113N19O14S ADEHMNQTY F 9.51 2 0 2 4 7 68.13 444 1.1 hour 3 min 2 min 66.88 5500 366.67 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00391 CFVPWFSKFlXRIL 14 "CHOL-C-Temporin L[Pro3,DLeu9,Nle10](TL6.3)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=0.89 μM,IC90=2.19 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.76 μM μM,IC90=1.89 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=22.3 μM μM,IC90=31.10 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=2.55 μM,IC90=5.89 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00391.cif Linear Cholesterol-PEG4 Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1767.39 C78H107N17O12S ADEGHMNQTY F 9.51 2 0 2 2 7 83.57 256 1.2 hour >20 hour >10 hour 76.43 5500 423.08 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00392 CGGFVPWFSKFlXRIL 16 "CHOL-CGG-Temporin L[Pro3,DLeu9,Nle10](TL6.4)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.32 μM,IC90=8.21 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=1.02 μM μM,IC90=10.21 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=28.88 μM μM,IC90=49.90 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=6.02 μM,IC90=9.90 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00392.cif Linear Cholesterol-PEG4 Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1881.5 C82H113N19O14S ADEHMNQTY F 9.51 2 0 2 4 7 68.13 444 1.2 hour >20 hour >10 hour 66.88 5500 366.67 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00393 FVPWFSKFlXRIL 13 "Undecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.5)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50<0.10 μM,IC90<0.10 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50<0.10 μM μM,IC90<0.10 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=10.01 μM μM,IC90=29.18 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50<0.10 μM,IC90<0.10 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00393.cif Linear Undecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00394 FVPWFSKFlXRIL 13 "Tridecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.6)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=1.39 μM,IC90=2.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.39 μM μM,IC90=5.86 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=33.36 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=3.39 μM,IC90=6.66 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00394.cif Linear Tridecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00395 FVPWFSKFlXRIL 13 "Pentadecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.7)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.48 μM,IC90=4.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.48 μM μM,IC90=7.86 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=37.77 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=3.48 μM,IC90=7.10 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00395.cif Linear Pentadecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00396 FVPWFSKFlXRIL 13 "Hexadecenoic-Temporin L[Pro3,DLeu9,Nle10](TL6.8)" Synthetic construct(derived from Temporin-L) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,HSV, MeV,H1N1" "Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae" "[Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.13 μM,IC90=4.96 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.77 μM μM,IC90=6.96 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=39.4 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=4.77 μM,IC90=7.11 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.35216177]Vero cells:CC50>100.00 μM No predicted structure available DRAVPe00396.cif Linear Palmitic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) membrane "TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction." 1664.26 C75H102N16O11 ACDEGHMNQTY F 11 2 0 2 1 7 70.77 128 1.1 hour 3 min 2 min 82.31 5500 458.33 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. "Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M. " Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. 10.3390/ijms23042060 "Anti-SARS-CoV-2,Anti-HSV, Anti-MeV,Anti-H1N1" DRAVPe00397 TLLKKVLKAAAKAALNAVLVGANA 24 Dermaseptin S4 (5-28) Synthetic construct(derived from Dermaseptin S4) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=27.07 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=25.27 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.23161023]Vero cells:CC50=34 μM. DRAVPe00397 DRAVPe00397.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2348.9 C107H194N30O28 CDEFHIMPQRSWY A 10.48 4 0 4 4 16 92.92 1409 7.2 hour >20 hour >10 hour 150.83 0 0 23161023 J Med Virol. 2013 Feb;85(2):272-81. "Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. "  In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. 10.1002/jmv.23450 Anti-HSV DRAVPe00398 ALWKTLLKKVLKAAAKAALNAVLVGANA 28 Dermaseptin K4S4 Synthetic construct(derived from Dermaseptin S4) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=2.7 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=5.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.23161023]Vero cells:CC50=12 μM. DRAVPe00398 DRAVPe00398.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2847.53 C133H232N36O32 CDEFHIMPQRSY A 10.6 5 0 5 4 19 82.5 1760 4.4 hour >20 hour >10 hour 146.79 5500 203.7 23161023 J Med Virol. 2013 Feb;85(2):272-81. "Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. "  In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. 10.1002/jmv.23450 Anti-HSV DRAVPe00399 ALWKTLLKKVLKAAAKAALKAVLVGANA 28 Dermaseptin K4K20S4 Synthetic construct(derived from Dermaseptin S4) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=2.1 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=5.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.23161023]Vero cells:CC50=25 μM. DRAVPe00399 DRAVPe00399.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2861.6 C135H238N36O31 CDEFHIMPQRSY A 10.7 6 0 6 3 19 81.07 1869 4.4 hour >20 hour >10 hour 146.79 5500 203.7 23161023 J Med Virol. 2013 Feb;85(2):272-81. "Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. "  In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. 10.1002/jmv.23450 Anti-HSV DRAVPe00400 ALWDTLLKKVLKAAAKAALDAVLVGANA 28 Dermaseptin D4D20S4 Synthetic construct(derived from Dermaseptin S4) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=5.41 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=9.63 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.23161023]Vero cells:CC50=17.75 μM. DRAVPe00400 DRAVPe00400.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2835.43 C131H224N34O35 CEFHIMPQRSY A 9.53 4 2 2 3 19 83.93 1235 4.4 hour >20 hour >10 hour 146.79 5500 203.7 23161023 J Med Virol. 2013 Feb;85(2):272-81. "Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. "  In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. 10.1002/jmv.23450 Anti-HSV DRAVPe00401 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1 Synthetic construct(derived from OC43-HR2P) Q8BB25 Experimentally Validated 2697049  S2 (918758) "MN908947.3,AY585229.1" "EK1 peptide was individually fused to the 3′ end of the HR1 domain from SARS-CoV, MERS-CoV, and HCoV-229E (residues 892 to 970, 984 to 1062, and 785 to 873, respectively) " cd22380##pfam01601 "MN908947, AY585229" Genomic RNA Long arm (q) of chromosome 3 at position 13.33. None "SARS-CoV-2,MERS-CoV,HCoV-229E,HCoV-NL63,CoV-WIV1" Coronaviridae Cell fusion assay "[Ref.35087243]SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=119.68 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=74.99 nM);inhibition of infection(Pseudovirus)(IC50=309.4 nM);inhibition of infection(Authentic)(IC50=1138 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=131.8 nM);inhibition of infection(Pseudovirus)(IC50=427.55 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=314.6 nM);inhibition of infection(Pseudovirus)(IC50=414.85 nM).##[Ref.32231345]SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=409.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=3237 nM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=239.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=631.8 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=802.1 nM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50=787.6 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=1398 nM),inhibit the replication of HCoV-OC43 in RD cells(IC50=1554 nM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50=207.4 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=3963 nM),inhibit the replication of HCoV-229E in Huh-7 cells(IC50=4375 nM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50=751.0 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=7666 nM),inhibit the replication of HCoV-NL63 in LLC-MK2 cells(IC50=3693 nM);##CoV-WIV1:ihibition of cell-cell fusion in Huh-7 cells(IC50=265.7 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=5425 nM);##CoV-Rs3367:ihibition of cell-cell fusion in Huh-7 cells(IC50=237.0 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=6014 nM);##CoV-SHC014:ihibition of cell-cell fusion in Huh-7 cells(IC50=279.6 nM);##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=286.7-315.0 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=2375.0 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=2468 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00401 DRAVPe00401.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 1.9 hour >20 hour >10 hour 119.17 2980 85.14 35087243##32231345 Cell Res. 2022 Apr;32(4):404-406.##Cell Res. 2020 Apr;30(4):343-355. "Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-022-00617-x##10.1038/s41422-020-0305-x "Anti-SARS-CoV-2,Anti-MERS-CoV,Anti-HCoV-229E,Anti-Anti-HCoV-NL63,Anti-CoV-WIV1" DRAVPe00402 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1P Synthetic construct(derived from EK1) Q8BB25 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae [Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=69.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00402.cif Linear Free PEG4-C(Palm) None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 1.9 hour >20 hour >10 hour 119.17 2980 85.14 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00403 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1C Synthetic construct(derived from EK1) Q8BB25 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=37.3-48.1 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=139.4 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00403.cif Linear Free PEG4-C(Chol) None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 1.9 hour >20 hour >10 hour 119.17 2980 85.14 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00404 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1C1 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=56.8 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=480.3 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00404.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 1.9 hour >20 hour >10 hour 119.17 2980 85.14 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00405 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSG 39 EK1C2 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=48.2 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=418.6 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00405 DRAVPe00405.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4533.16 C203H328N46O68S CHPRW EL 4.36 5 10 -5 9 13 -44.1 -6455 1.9 hour >20 hour >10 hour 110 2980 78.42 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00406 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSG 39 EK1C3 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=10.6 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=86.4 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00406.cif Linear Free PEG4-Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4533.16 C203H328N46O68S CHPRW EL 4.36 5 10 -5 9 13 -44.1 -6455 1.9 hour >20 hour >10 hour 110 2980 78.42 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00407 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C4 Synthetic construct(derived from EK1) No entry found Experimentally Validated 31631  31631  31631  Not available cd22380##pfam01601 AY585229 Genomic RNA Long arm (q) of chromosome 3 at position 13.33. 6NZK "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-OC43,HCoV-229E" Coronaviridae pseudovirus inhibition assay "[Ref.35087243]SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=3.32 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=0.88 nM);inhibition of infection(Pseudovirus)(IC50=8.63 nM);inhibition of infection(Authentic)(IC50=85.38 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=4.04 nM);inhibition of infection(Pseudovirus)(IC50=9.83 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=2.57 nM);inhibition of infection(Pseudovirus)(IC50=5.58 nM).##[Ref.32231345]SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=11.7 nM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=2.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=11.1 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=4.2 nM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50=7.7 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=37.7 nM),inhibit the replication of HCoV-OC43 in RD cells(IC50=24.8 nM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50=5.2 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=12.4 nM),inhibit the replication of HCoV-229E in Huh-7 cells(IC50=101.5 nM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50=21.4 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=76.6 nM),inhibit the replication of HCoV-NL63 in LLC-MK2 cells(IC50=187.6 nM);##CoV-WIV1:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=30.8 nM);##CoV-Rs3367:ihibition of cell-cell fusion in Huh-7 cells(IC50=8.1 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=66.9 nM);##CoV-SHC014:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.3 nM);##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=1.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=15.8 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=2468 nM)." No hemolysis information or data found in the reference(s) presented in this entry "[Ref.32231345]<10% cytotoxicity against VERO-E6 cells, RD cells, LLC-MK2 cells, Huh-7 cells up to 10000 nM." DRAVPe00407 DRAVPe00407.cif Linear Free PEG4-Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 35087243##32231345 Cell Res. 2022 Apr;32(4):404-406.##Cell Res. 2020 Apr;30(4):343-355. "Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-022-00617-x##10.1038/s41422-020-0305-x "Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-MERS-CoV,Anti-HCoV-OC43,Anti-HCoV-229E" DRAVPe00408 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C5 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.1 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=31.3 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00408.cif Linear Free PEG8-Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00409 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C6 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.9 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=77.4 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00409.cif Linear Free PEG12-Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00410 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C7 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay "[Ref.32231345]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.9 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=84.4 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00410.cif Linear Free PEG24-Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00411 LKVLLYEEFKLLESLIMEILEYQKDSDIKENAEDTK 36 EK1-scrambled Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.32231345]SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-OC43,HCoV-229E,HCoV-NL63,CoV-WIV1,CoV-Rs3367,CoV-SHC014(No inhibition on the concentration up to 10 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00411 DRAVPe00411.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 5.5 hour 3 min 2 min 119.17 2980 85.14 32231345 Cell Res. 2020 Apr;30(4):343-355. "Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L." Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. 10.1038/s41422-020-0305-x Anti-SARS-CoV-2 DRAVPe00412 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 IBP02V1 Synthetic construct(derived from HR2 region of SARS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=1.1±0.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=17.8 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=14.3 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.6±0.1 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=50 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=21.5 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=33.6±3.5 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=66.9±7.6 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=62.5±17.2 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=203.9±8.8 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. DRAVPe00412 DRAVPe00412.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 3893.41 C168H287N47O58 CFHMPTWY ILN 4.36 3 6 -3 9 15 -8.29 -5930 20 hour 30 min >10 hour 142 0 0 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-Anti-HCoV-NL63" DRAVPe00413 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 HR2(1151-1185) Synthetic construct(derived from SARS-CoV spike protein) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18442051]HIV‐luc/SARS Pseudotyped Virus:inhibition of viral-entry in Vero E3 cells(EC50=0.34 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00413.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3893.41 C168H287N47O58 CFHMPTWY ILN 4.36 3 6 -3 9 15 -8.29 -5930 20 hour 30 min >10 hour 142 0 0 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. "Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM." Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.  10.1002/jcb.21790 Anti-HIV DRAVPe00414 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V2 Synthetic construct(derived from HR2 region of SARS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.6±0.03 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=20.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=18.1 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.4±0.04 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=19.3 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=20.8 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=56.5±9.4nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=55.3±2.8 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=67.5±8 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=535.7±44.6 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. DRAVPe00414 DRAVPe00414.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4008.5 C172H292N48O61 CFHMPTWY ILN 4.2 3 7 -4 9 15 -17.78 -6802 1.1 hour 3 min >10 hour 138.06 0 0 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00415 EISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V3 Synthetic construct(derived from HR2 region of SARS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.4±0.02 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=14.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=17.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.2±0.02 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=40.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=14.4 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=48±5.8 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=38.5±6.2 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=75.8±9.9 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=545.7±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. DRAVPe00415 DRAVPe00415.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4022.52 C173H294N48O61 CFHMPTWY EILN 4.25 3 7 -4 9 15 -17.78 -6611 1 hour 30 min >10 hour 138.06 0 0 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00416 ELSGINASVVNLQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V4 Synthetic construct(derived from HR2 region of SARS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.3±0.02 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=18.6 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=15.2 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.1±0.02 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=29.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=26.3 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=63±1.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=22.4±2.2 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=66.3±3.1 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=502±24.2 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. DRAVPe00416 DRAVPe00416.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4022.52 C173H294N48O61 CFHMPTWY L 4.25 3 7 -4 9 15 -21.67 -6611 1 hour 30 min >10 hour 138.06 0 0 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00417 SLTQINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V5 Synthetic construct(derived from HR2 region of SARS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae Cell fusion assay [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=2.1±0.5 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=21 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=23.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=1.3±0.1 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=98.8 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=27.5 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=65.9±13.2 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=68.4±9.7 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=70.8±8.7 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=1128.4±148.6 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. DRAVPe00417 DRAVPe00417.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4065.59 C175H299N49O61 CFGHMPWY L 4.36 3 6 -3 9 15 -20.56 -6835 1.9 hour >20 hour >10 hour 138.06 0 0 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00418 SLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 36 MERS-LP Synthetic construct(derived from HR2 region of MERS-CoV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=102.9±7.2 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=5046±905.2 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=79.1±9.8 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=82.9±8.6 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00418 DRAVPe00418.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4141.78 C185H307N43O61S CFGHPRW L 4.18 2 5 -3 11 14 13.06 -3327 1.9 hour >20 hour >10 hour 138.06 2980 85.14 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00419 SLDYINVTFLDLQDEMNRLQEAIKVLNQSYINLKDI 36 OC43-LP Synthetic construct(derived from HR2 region of OC43-LP) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=4.1±1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=82.8±22.1 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=2.4±0.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=97.5±5.9 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=250.4±39.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=5.2±0.5 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=416.5±227.5 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=2008.8±697.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00419 DRAVPe00419.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4270.86 C190H306N48O61S CGHPW L 4.23 3 6 -3 9 14 -19.44 -6293 1.9 hour >20 hour >10 hour 127.22 2980 85.14 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00420 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELK 37 EK1V1 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=273.5±4.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=2672.1±384.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=214.5±20.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=1790.8±363.2 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=4370.3±719.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=499.8±163.3 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=487.2±41.3 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=1255.6±453.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00420 DRAVPe00420.cif Linear Free Chol None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4460.16 C202H329N45O65S CGHPRW EL 4.53 6 10 -4 6 13 -52.7 -6858 1.9 hour >20 hour >10 hour 115.95 2980 82.78 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00421 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1V2 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34344868]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.9±0.2 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=87.2±8.3 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.5±0.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=106.5±5.4 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=252±5.6 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=1.1±0.3 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=59.4±13.1 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=503.3±20.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00421.cif Linear Free PEG8-K(Chol) None L membrane "A six-helical bundle structure is formed by two heptad repeat domains (HR1 and HR2) in S2, juxtaposing the viral and cellular membranes for fusion.The peptide derived from the HR2 sequence can competitively bind to the viral HR1 domain thus exerting antiviral activity." 4331.98 C196H317N43O64S CGHPRW EL 4.36 5 10 -5 6 13 -43.33 -6303 1.9 hour >20 hour >10 hour 119.17 2980 85.14 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. "Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y." SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. 10.1038/s41392-021-00698-x "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00422 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP20 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=1.36 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=50.52 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=33.85 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=103.17 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=128.87 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=111.41 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=79.09 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=88.49 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=92.16 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=73.86 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=228.4 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=817.21 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=471.54 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00422 DRAVPe00422.cif Linear Free Chol(cholesterol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00423 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP21 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=7.5 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=191.4 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=126.65 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00423.cif Linear Free C16(palmitic acid) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 Anti-SARS-CoV-2 DRAVPe00424 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP22 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=6.23 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=179.95 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=86.33 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00424.cif Linear Free C18(stearic acid) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 Anti-SARS-CoV-2 DRAVPe00425 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP23 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=39.07 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=1236.38 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=507.32 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00425.cif Linear Free Toc(tocophenol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 Anti-SARS-CoV-2 DRAVPe00426 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP24 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.33 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=3.77 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=2.89 nM);inhibition of live SARS-CoV-2 infection in Vero cells(IC50=8.97 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.29 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.5 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.42 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.97 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.22 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.06 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=21.64 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=69.9 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=375.56 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=421.48 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34057039]Huh-7 cells:CC50=6.6 μM;Vero-E6 cells:CC50=13.67 μM. No predicted structure available DRAVPe00426.cif Linear Free PEG4-K(Chol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00427 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP25 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae "[Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.29 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=2.13 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.43 nM),inhibition of live SARS-CoV-2 infection in Vero cells(IC50=25.71 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.8 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.52 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.56 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.71 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=5.87 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.76 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=17.69 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=48.5 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=353.22 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=336.14 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.34057039]Huh-7 cells:CC50=3.54 μM;Vero-E6 cells:CC50=6.95 μM. No predicted structure available DRAVPe00427.cif Linear Free PEG5-K(Chol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00428 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP26 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae [Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.26 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=3.05 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.82 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00428.cif Linear Free PEG6-K(Chol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 Anti-SARS-CoV-2 DRAVPe00429 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP27 Synthetic construct(derived from HR2 region of SARS-CoV-2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae "[Ref.34057039]SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.32 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=2.77 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.54 nM),inhibition of live SARS-CoV-2 infection in Vero cells(IC50=29.85 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.75 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.87 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.56 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.55 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.18 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=8.25 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=24.95 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=60.08 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=179.53 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=231.18 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.34057039]Huh-7 cells:CC50=4.04 μM;Vero-E6 cells:CC50=5.05 μM. No predicted structure available DRAVPe00429.cif Linear Free PEG8-K(Chol) None L membrane "Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived." 4347.93 C192H317N51O63 CFHMPTW EL 4.77 5 7 -2 9 13 -60.27 -7972 1.9 hour >20 hour >10 hour 121.08 2980 82.78 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. "Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y." Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. 10.1080/22221751.2021.1937329 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00430 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKW 45 EKL0 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.583±0.073 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.442±0.037 μmol/L),inhibition of cell-cell fusion(IC50=0.277±0.029 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00430 DRAVPe00430.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 5522.3 C256H392N54O79S CHPR E 4.44 6 11 -5 11 15 -54.89 -7107 1.9 hour >20 hour >10 hour 101.78 12950 294.32 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00431 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEY 36 EKL1 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63" Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.622±0.089 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.746±0.152 μmol/L),inhibition of cell-cell fusion(IC50=0.220±0.034 μmol/L);inhibited authentic SARS-CoV-2 infection in Vero E6 cells(IC50=1.407±0.189 μmol/L);##inhibition of multiple HCoV Pseudovirus:SARS-CoV (IC50=6.716±5.937 μmol/L), MERS-CoV(IC50=4.086±0.345 μmol/L), HCoV-OC43(IC50=10.530±3.778 μmol/L), HCoV-NL63(IC50=3.700±0.222 μmol/L), SARSr-CoV-WIV1(IC50=30.270±4.713 μmol/L), and HCoV-Rs3367 (IC50=88.300±24.600 μmol/L),inhibition of authentic HCoV-OC43 infection in RD cells (IC50=20.290±1.092 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00431 DRAVPe00431.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4388.99 C201H312N42O65S CHPQRW E 4.39 5 10 -5 9 11 -64.72 -6393 1.4 hour 3 min >10 hour 97.5 5960 170.29 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63" DRAVPe00432 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYV 36 EKL2 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.526±0.049 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=4.714±1.173 μmol/L),inhibition of cell-cell fusion(IC50=1.240±0.246 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00432 DRAVPe00432.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4438.06 C206H315N41O65S CHNPQRW E 4.39 5 10 -5 9 11 -58.61 -5743 7.2 hour >20 hour >10 hour 97.5 7450 212.86 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00433 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKW 36 EKL3 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50>10 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50>5 μmol/L),inhibition of cell-cell fusion(IC50=2.167±0.270 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00433 DRAVPe00433.cif Linear Free Free None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4504.17 C210H321N43O64S CFHNPQR E 4.57 6 10 -4 8 11 -77.78 -6106 5.5 hour 3 min 2 min 97.5 12950 370 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00434 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGC 49 EKL0C Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.122±0.012 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.147±0.055 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.162±0.022 μmol/L),inhibition of cell-cell fusion(IC50=0.021±0.003 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00434 DRAVPe00434.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 5826.62 C266H408N58O84S2 HPR E 4.44 6 11 -5 15 15 -48.57 -7131 1.9 hour >20 hour >10 hour 93.47 12950 269.79 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00435 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVGSGC 40 EKL2C Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.115±0.019 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.054±0.014 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.200±0.020 μmol/L),inhibition of cell-cell fusion(IC50=0.022±0.001 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00435 DRAVPe00435.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4742.38 C216H331N45O70S2 HNPQRW E 4.39 5 10 -5 13 11 -50.5 -5767 7.2 hour >20 hour >10 hour 87.75 7450 191.03 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00436 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGC 40 EKL3C Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.127±0.293 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=1.176±1.230 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.892±0.069 μmol/L),inhibition of cell-cell fusion(IC50=0.045±0.004 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00436 DRAVPe00436.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4808.49 C220H337N47O69S2 FHNPQR E 4.57 6 10 -4 12 11 -67.75 -6130 5.5 hour 3 min 2 min 87.75 12950 332.05 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00437 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGK 49 EKL0P Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.093±0.012 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.619±0.341 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.176±0.019 μmol/L),inhibition of cell-cell fusion(IC50=0.083±0.009 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00437 DRAVPe00437.cif Linear Free Palm None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 5851.66 C269H415N59O84S CHPR E 4.61 7 11 -4 14 15 -61.63 -7814 1.9 hour >20 hour >10 hour 93.47 12950 269.79 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00438 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYGSGK 40 EKL1P Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.182±0.034 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.812±0.182 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.231±0.022 μmol/L),inhibition of cell-cell fusion(IC50=0.064±0.004 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00438 DRAVPe00438.cif Linear Free Palm None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4718.35 C214H335N47O70S CHPQRW E 4.57 6 10 -4 12 11 -72 -7100 1.4 hour 3 min >10 hour 87.75 5960 152.82 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00439 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVGSGK 40 EKL2P Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=1.129±0.166 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.973±0.254 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.304±0.051 μmol/L),inhibition of cell-cell fusion(IC50=0.183±0.028 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00439 DRAVPe00439.cif Linear Free Palm None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4767.42 C219H338N46O70S CHNPQRW E 4.57 6 10 -4 12 11 -66.5 -6450 7.2 hour >20 hour >10 hour 87.75 7450 191.03 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00440 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGK 40 EKL3P Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae "[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=3.987±0.682 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=2.214±0.371 μmol/L),inhibition of cell-cell fusion(IC50=0.193±0.021 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00440 DRAVPe00440.cif Linear Free Palm None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4833.52 C223H344N48O69S CFHNPQR E 4.76 7 10 -3 11 11 -83.75 -6813 5.5 hour 3 min 2 min 87.75 12950 332.05 34367893 Acta Pharm Sin B. 2021 Aug 2. "Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1016/j.apsb.2021.07.026 Anti-SARS-CoV-2 DRAVPe00441 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYGSGC 40 EKL1C Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-NL63,HCoV-OC43" Coronaviridae Cell fusion assay "[Ref.35087243]SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=12.18 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=5.52 nM);inhibition of infection(Pseudovirus)(IC50=26.14 nM);inhibition of infection(Authentic)(IC50=182.2 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=14.42 nM);inhibition of infection(Pseudovirus)(IC50=31.99 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=11.77 nM);inhibition of infection(Pseudovirus)(IC50=23.6 nM).##[Ref.34367893]SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.045±0.006 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.037±0.009 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.040±0.005 μmol/L),inhibition of cell-cell fusion(IC50=0.008±0.001 μmol/L);inhibited authentic SARS-CoV-2 infection in Vero E6 cells(IC50=0.003±0.001 μmol/L);##SARS-CoV-2 variants(inhibition of Pseudovirus(PsV) infection):V341L(IC50=0.047±0.013 μmol/L);F342L(IC50=0.026±0.007 μmol/L);V367F(IC50=0.066±0.012 μmol/L);R408I(IC50=0.148±0.012 μmol/L);N435D(IC50=0.135±0.013 μmol/L);G476S(IC50=0.065±0.008 μmol/L);V483A(IC50=0.078±0.011 μmol/L);N501Y(IC50=0.069±0.006 μmol/L);D614G(IC50=0.104±0.010 μmol/L);12 mutations(P.1)(IC50=0.046±0.006 μmol/L);K417N-E484K-N501Y(IC50=0.113±0.013 μmol/L);8 mutations(B.1.1.7)(IC50=0.120±0.009 μmol/L);wide type(IC50=0.049±0.007 μmol/L);##inhibition of multiple HCoV Pseudovirus:SARS-CoV (IC50=0.076±0.014 μmol/L), MERS-CoV(IC50=0.048±0.006 μmol/L), HCoV-OC43(IC50=0.668±0.081 μmol/L), HCoV-NL63(IC50=0.035±0.003 μmol/L), SARSr-CoV-WIV1(IC50=0.218±0.013 μmol/L), and HCoV-Rs3367 (IC50=0.046±0.003 μmol/L),inhibition of authentic HCoV-OC43 infection in RD cells (IC50=0.281±0.018 μmol/L)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.34367893]Huh-7 cells:CC50=10 μmol/L;Caco-2 cells:CC50=13.81 μmol/L;293T/ACE2 cells:CC50=8.49 μmol/L. DRAVPe00441 DRAVPe00441.cif Linear Free Chol None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4693.31 C211H328N46O70S2 HPQRW E 4.39 5 10 -5 13 11 -56 -6417 1.4 hour 3 min >10 hour 87.75 5960 152.82 35087243##34367893 Cell Res. 2022 Apr;32(4):404-406.##Acta Pharm Sin B. 2021 Aug 2. "Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q." Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. 10.1038/s41422-022-00617-x##10.1016/j.apsb.2021.07.026 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-NL63,HCoV-OC43" DRAVPe00442 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1-C16 Synthetic construct(derived from EK1) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-OC43" Coronaviridae pseudovirus inhibition assay [Ref.35336956]SARS-CoV-2 WT:inhibition of pseudovirus (PsV) infection in Caco2 cells(IC50=0.48 μM);##SARS-CoV-2 Alpha:inhibition of pseudovirus (PsV) infection(IC50=0.19 μM);##SARS-CoV-2 Beta:inhibition of pseudovirus (PsV) infection(IC50=0.43 μM);##SARS-CoV-2 Gamma:inhibition of pseudovirus (PsV) infection(IC50=0.26 μM);##SARS-CoV-2 Delta:inhibition of pseudovirus (PsV) infection(IC50=0.11 μM);##SARS-CoV-2 Omicron:inhibition of pseudovirus (PsV) infection(IC50=0.23 μM);inhibition of authentic infection in Vero-E6-TMPRSS-2 cells(IC50=0.75 μM);##SARS-CoV:inhibition of pseudovirus (PsV) infection(IC50=0.17 μM);##SARSr-CoV WIV1:inhibition of pseudovirus (PsV) infection(IC50=0.15 μM);##SARSr-CoV Rs3367:inhibition of pseudovirus (PsV) infection(IC50=0.3 μM);##MERS-CoV:inhibition of pseudovirus (PsV) infection in Caco2 cells(IC50=0.10 μM);inhibition of cell-cell fusion(IC50=0.012 μM);##HCoV-OC43:inhibition of authentic infection in RD cells(IC50=0.07 μM);inhibition of cell-cell fusion(IC50=0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.35336956]showed no significant cytotoxicity against RD cells at the concentration of 5 μM. No predicted structure available DRAVPe00442.cif Linear Free PEG4-C16(palmitic acid) None L membrane "The 6-HB structure formed by HR1 and HR2 regions in the S2 subunit of HCoVs plays a key role during the viral membrane fusion process,peptides derived from the HR2 regions can competitively inhibit viral 6-HB formation, thereby preventing viral fusion and entry into host cells." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 35336956 Viruses. 2022 Mar 6;14(3):549. "Lan Q, Chan JF, Xu W, Wang L, Jiao F, Zhang G, Pu J, Zhou J, Xia S, Lu L, Yuen KY, Jiang S, Wang Q. " "A Palmitic Acid-Conjugated, Peptide-Based pan-CoV Fusion Inhibitor Potently Inhibits Infection of SARS-CoV-2 Omicron and Other Variants of Concern." 10.3390/v14030549 "Anti-SARS-CoV-2,SARS-CoV,Anti-MERS-CoV,Anti-HCoV-OC43" DRAVPe00443 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 "IPB01(SARS-CoV-S (1151-1185),SR9, SARS-CoV-2-S (1169-1203))" Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.022±0.005 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=33.74±11.827 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM).##[Ref.17942557]SARS-CoV:Inhibition of virus entry in VERO-E6 cells(EC50=0.005 µM).##[Ref.18442051]SARS-CoV: inhibition of PsV entry in Vero-E6 cells(EC50=0.34 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00443.cif Linear Free Free None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3893.41 C168H287N47O58 CFHMPTWY ILN 4.36 3 6 -3 9 15 -8.29 -5930 20 hour 30 min >10 hour 142 0 0 17942557##18442051##32376627 J Virol. 2008 Jan;82(1):588-92.##J Cell Biochem. 2008 Aug 15;104(6):2335-47.##J Virol. 2020 Jul 1;94(14):e00635-20. "Ujike M, Nishikawa H, Otaka A, Yamamoto N, Yamamoto N, Matsuoka M, Kodama E, Fujii N, Taguchi F. ##Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. ##Zhu Y, Yu D, Yan H, Chong H, He Y." "Heptad repeat-derived peptides block protease-mediated direct entry from the cell surface of severe acute respiratory syndrome coronavirus but not entry via the endosomal pathway.##Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.##Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.01697-07##10.1002/jcb.21790##10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00444 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELK 36 IPB02(SARS-CoV-2-S (1169-1203)-K) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.025 ± 0.002 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.08±0.017 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=0.251 ± 0.118 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00444 DRAVPe00444.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 4021.58 C174H299N49O59 CFHMPTWY ILN 4.66 4 6 -2 9 15 -18.89 -6485 20 hour 30 min >10 hour 138.06 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00445 INASVVNIQKEIDRLNEVAKNLNESLIDLQELGK 34 IPB03(SARS-CoV-2-S (1172-1205)) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.015 ± 0.002 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.947 ± 0.179 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.315 ± 0.463 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00445 DRAVPe00445.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3821.34 C165H283N47O56 CFHMPTWY LN 4.66 4 6 -2 8 14 -30.88 -6637 20 hour 30 min >10 hour 134.71 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00446 SVVNIQKEIDRLNEVAKNLNESLIDLQELGK 31 IPB04(SARS-CoV-2-S (1175-1205)) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.033 ± 0.013 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.218 ± 0.063 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.053 ± 0.444 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00446 DRAVPe00446.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3523 C152H261N43O52 CFHMPTWY L 4.66 4 6 -2 7 12 -42.9 -6646 1.9 hour >20 hour >10 hour 131.94 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00447 IQKEIDRLNEVAKNLNESLIDLQELGK 27 IPB05(SARS-CoV-2-S (1179-1205)) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay." "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00447 DRAVPe00447.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3123.55 C135H232N38O46 CFHMPTWY L 4.66 4 6 -2 5 10 -64.44 -6450 20 hour 30 min >10 hour 130 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00448 IDRLNEVAKNLNESLIDLQELGK 23 IPB06(SARS-CoV-2-S (1183-1205)) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00448 DRAVPe00448.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 2624.97 C113H194N32O39 CFHMPTWY L 4.51 3 5 -2 5 9 -47.83 -5152 20 hour 30 min >10 hour 135.65 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00449 IQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 33 IPB07(SARS-CoV-2-S (1179-1211)) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.017 ± 0.001 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.993 ± 0.08 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.037 ± 0.836 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00449 DRAVPe00449.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3948.49 C175H288N46O57 CFHMPTW EL 4.77 5 7 -2 7 11 -80 -7776 20 hour 30 min >10 hour 118.18 2980 93.13 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00450 ISGINASVVNIQKEIDRLNEVAKNLNESLIK 31 IPB08(SARS-CoV-2-S (1169-1198)-K) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=4.66 ± 1.565 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=1.738 ± 0.898 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.13 ± 0.472 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00450 DRAVPe00450.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 3422.93 C148H257N43O49 CFHMPTWY IN 6.26 4 4 0 9 13 -12.58 -5362 20 hour 30 min >10 hour 135.16 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00451 SVVNIQKEIDRLNEVAKNLNESLIK 25 IPB09(SARS-CoV-2-S (1175-1198)-K) Synthetic construct(derived from SARS-CoV-2 S protein) P59594##P0DTC2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" "cell fusion assay, single-cycle infection assay" "[Ref.32376627]SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00451 DRAVPe00451.cif Linear Free Chol None L membrane "The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently." 2867.3 C124H216N36O41 CFGHMPTWY N 5.98 4 4 0 6 10 -40 -5617 1.9 hour >20 hour >10 hour 132.4 0 0 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. "Zhu Y, Yu D, Yan H, Chong H, He Y." "Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity." 10.1128/JVI.00635-20 "Anti-Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-VSV" DRAVPe00452 RLFFKCIYRFFEHGLKRG 18 M2 AH Synthetic construct(derived from influenza virus M2 protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None H1N1 Orthomyxoviridae [Ref.31375212]H1N1(A/Puerto Rico/8/34):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=870 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.31375212]Madin-Darby canine kidney epithelial(MDCK) cells:CC50=70.3 μM DRAVPe00452 DRAVPe00452.cif Linear Free Free None L membrane "M2 AH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 AH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission." 2317.79 C111H165N31O22S ADMNPQSTVW F 10.3 6 1 5 4 7 -23.89 -3763 1 hour 2 min 2 min 65 1490 87.65 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. "Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH. " Envelope-deforming antiviral peptide derived from influenza virus M2 protein. 10.1016/j.bbrc.2019.07.088 Anti-H1N1 DRAVPe00453 RKFFKKIYRFFRKLLKRL 18 M2 MH Synthetic construct(derived from influenza virus M2 protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae [Ref.31375212]H1N1(A/Puerto Rico/8/34):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=53 nM);##H3N2(A/Sydney/5/97):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.058 μM);##H3N2(A/X31):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.016 μM);##H5N2(A/aquatic bird/Korea/w81/2005 ):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.066 μM);##H1N1(A/Swine/Iowa/15/30):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.053 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.31375212]Madin-Darby canine kidney epithelial(MDCK) cells:CC50=19.2 μM DRAVPe00453 DRAVPe00453.cif Linear Free Free None L membrane "M2 MH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 MH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission." 2488.16 C123H199N35O20 ACDEGHMNPQSTVW K 12.02 9 0 9 1 8 -65 -5597 1 hour 2 min 2 min 86.67 1490 87.65 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. "Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH. " Envelope-deforming antiviral peptide derived from influenza virus M2 protein. 10.1016/j.bbrc.2019.07.088 Anti-Influenza virus DRAVPe00454 RLAAKCAARFAEHGLKRG 18 M2 NH Synthetic construct(derived from influenza virus M2 protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None H1N1 Orthomyxoviridae [Ref.31375212]H1N1:did not exhibit any inhibitory effect. No hemolysis information or data found in the reference(s) presented in this entry [Ref.31375212]did not show apparent cytotoxicity against Madin-Darby canine kidney epithelial(MDCK) cells up to a concentration of 100 μM. DRAVPe00454 DRAVPe00454.cif Linear Free Free None L membrane "M2 NH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 NH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission." 1955.31 C84H143N31O21S DIMNPQSTVWY A 10.92 6 1 5 3 8 -38.33 -4230 1 hour 2 min 2 min 71.11 0 0 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. "Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH. " Envelope-deforming antiviral peptide derived from influenza virus M2 protein. 10.1016/j.bbrc.2019.07.088 Anti-H1N1 DRAVPe00455 GFSSLFKAGAKYLLKQVGKAGAQQLACKAANNC 33 Brevinin-2GHk(BR2GK) Fejervarya limnocharis A0A6G6CZ26 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None ZIKV Flaviviridae [Ref.34960651]Zika Virus: inhibition of infection of Zika virus in Vero cells(IC50=3.408 ± 0.738 μM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.34960651]exhibited no significant toxicity to Vero, Hela, and Huh7 cells in the concentration range 0-20 µM." DRAVPe00455 DRAVPe00455.cif Linear Free Free None L membrane BR2GK directly inactivated ZIKV by disrupting the integrity of the envelope and may also penetrate the host cell membrane to inhibit the middle stage of ZIKV infection. 3386.98 C150H245N43O42S2 DEHIMPRTW A 9.79 5 0 5 11 14 3.33 -1592 30 hour >20 hour >10 hour 77.27 1615 50.47 34960651 Viruses. 2021 Nov 28;13(12):2382.  "Xiong W, Li J, Feng Y, Chai J, Wu J, Hu Y, Tian M, Lu W, Xu X, Zou M." "Brevinin-2GHk, a Peptide Derived from the Skin of Fejervarya limnocharis, Inhibits Zika Virus Infection by Disrupting Viral Integrity." 10.3390/v13122382 Anti-ZIKV DRAVPe00456 FLPLILPSIVTALSSFLKQG 20 Hs-1 Hypsiboas semilineatus No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae [Ref.29153860]DENV2:reduced the number of lysis plaques by 100% at 125 µg/mL; by 60% at 7.81 μg/mL;##DENV3:reduced the number of lysis plaques by 100% at 125 µg/mL; by 50% at 7.81 μg/mL No hemolysis information or data found in the reference(s) presented in this entry [Ref.29153860]No significant cytotoxicity agaisnt Vero cells up to 125μg/ mL. DRAVPe00456 DRAVPe00456.cif Linear Free Free None L envelope It was possible to observe that the viral particle lost its ability to infect because of the breakdown on the envelope as the peptide acted directly on the virus. 2144.63 C104H170N22O26 CDEHMNRWY L 8.75 1 0 1 5 11 127.5 2333 1.1 hour 3 min 2 min 156 0 0 29153860 Virology. 2018 Jan 15;514:79-87. "Monteiro JMC, Oliveira MD, Dias RS, Nacif-Marçal L, Feio RN, Ferreira SO, Oliveira LL, Silva CC, Paula SO." The antimicrobial peptide HS-1 inhibits dengue virus infection. 10.1016/j.virol.2017.11.009 Anti-DENV DRAVPe00457 GGARDAGKAEWW 12 gg-ww Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae [Ref.26248692]dengue virus serotype 2(DENV-2):inhibition the cytopathic effect(CPE) and plaque formation in Vero cells(IC50=77-91 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry [Ref.26248692]It was not toxic to Vero cells up to 400 μmol/L. DRAVPe00457 DRAVPe00457.cif Linear Free Free None L membrane The peptide gg-ww could exert its inhibition during the viral entry step of DENV-2 infection by interfering with viral attachment or internalization. 1303.4 C58H82N18O17 CFHILMNPQSTVY AG 6.07 2 2 0 3 5 -108.33 -2309 30 hour >20 hour >10 hour 25 11000 1000 26248692 J Appl Microbiol. 2015 Oct;119(4):1170-80.  "Chew MF, Tham HW, Rajik M, Sharifah SH. " Anti-dengue virus serotype 2 activity and mode of action of a novel peptide. 10.1111/jam.12921 Anti-DENV DRAVPe00458 CNDFRSKTC 9 P1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza viruse Orthomyxoviridae [Ref.19680476]Avian influenza viruses (AIV) H9N2: inhibition of viral attachment on MDCK cells(>50% inhibition at the concentration of 50 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00458 DRAVPe00458.cif Linear Free Free None L membrane "Avian influenza viruses possess two important surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA) against which neutralizing antibodies are produced. This peptide inhibits the replication of the virus in ovo and in vitro by its binding to the HA glycoprotein. " 1073.21 C42H68N14O15S2 AEGHILMPQVWY C 8.06 2 1 1 5 1 -101.11 -3626 1.2 hour >20 hour >10 hour 0 125 15.63 19680476 Int J Biol Sci. 2009 Aug 8;5(6):543-8. "Rajik M, Omar AR, Ideris A, Hassan SS, Yusoff K." A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells.  10.7150/ijbs.5.543 Anti-Influenza viruse DRAVPe00459 QEGISRFKICPYHWYKQHMSLLFRRYYHKLDSII 34 CPXV012 Synthetic construct(derived from the cowpox virus protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV,HBV,HIV,RVFV" "Herpesviridae, Hepadnaviridae, Retroviridae, Phenuiviridae" [Ref.32872420]Herpes simplex virus-1(HSV-1):inhibition of HSV-1 infection in MelJuSo(MJS) cells(75.9 ± 5.7% inhibition at 150 µg/mL);##Hepatitis B virus(HBV): decrease of HBeAg and viral DNA infected with HBV-1 in HepRG cells(84.0 ± 3.0% of HBeAg and 73.6 ± 2.3% of viral DNA at 100 µg/mL);##HIV-1:inhibition of virus infection in LC5-RIC reporter cells(82.7 ± 4.9% inhibition at 100 µg/mL);inhibition of virus replication in LC5-RIC reporter cells(62.2 ± 2.4% inhibition at 100 µg/mL);##Rift Valley fever virus(RVFV): inhibition of virus infection in MJS cells(65.5 ± 2.3% inhibition at 160 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.32872420]Did not observe any decrease in live cells against Vero and Huh7.5 cells up to 200 µg/mL. DRAVPe00459 DRAVPe00459.cif Linear Free Free None L envelope(phosphatidylserine) "Within virus-infected cells, this protein helps to evade the immune system by inhibiting the transporter associated with antigen processing (TAP), thereby interfering with MHC I-dependent antigen presentation. And the peptide is the segment of the CPXV012 protein responsible for blocking TAP." 4358.11 C204H303N55O48S2 ANTV IY 9.65 9 2 7 9 10 -58.53 -6546 0.8 hour 10 min >10 hour 80.29 11460 347.27 32872420 Cells. 2020 Aug 29;9(9):1989. "Luteijn RD, Praest P, Thiele F, Sadasivam SM, Singethan K, Drijfhout JW, Bach C, de Boer SM, Lebbink RJ, Tao S, Helfer M, Bach NC, Protzer U, Costa AI, Killian JA, Drexler I, Wiertz EJHJ." A Broad-Spectrum Antiviral Peptide Blocks Infection of Viruses by Binding to Phosphatidylserine in the Viral Envelope.  10.3390/cells9091989 "Anti-HSV,Anti-HBV,Anti-HIV,RVFV" DRAVPe00460 TEPSTRGSWKFW 12 P1 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None JEV Flaviviridae [Ref.24468276]Japanese encephalitis virus (JEV): inhibition of JEV infection in BHK-21 cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00460 DRAVPe00460.cif Linear Free Free None L envelope protein "E glycoprotein has been identified as the major antigenic determinant on flavivirus particles and mediates binding and fusion during viral entry,DIII has been proposed to act as the binding region for the cellular receptor. And the peptide could bingding with DIII domain and inhibit the initial step of JEV infection." 1481.63 C69H96N18O19 ACDHILMNQVY STW 8.41 2 1 1 5 3 -132.5 -3064 7.2 hour >20 hour >10 hour 0 11000 1000 24468276 Antiviral Res. 2014 Apr;104:7-14. "Zu X, Liu Y, Wang S, Jin R, Zhou Z, Liu H, Gong R, Xiao G, Wang W." Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. 10.1016/j.antiviral.2014.01.011 Anti-JEV DRAVPe00461 SENRKVPFYSHS 12 P3 Synthetic construct(phage display) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None JEV Flaviviridae "[Ref.24468276]Japanese encephalitis virus (JEV): inhibition of JEV infection in BHK-21 cells(IC50=1.42 ± 0.41 μM determined by plaque assay,IC50=1.12 ± 0.38 μM determined by qRT-PCR,IC90~100 μM determined by plaque assay and qRT-PCR)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00461 DRAVPe00461.cif Linear Free Free None L envelope protein "E glycoprotein has been identified as the major antigenic determinant on flavivirus particles and mediates binding and fusion during viral entry,DIII has been proposed to act as the binding region for the cellular receptor. And the peptide could bingding with DIII domain and inhibit the initial step of JEV infection." 1450.57 C64H95N19O20 ACDGILMQTW S 8.33 3 1 2 5 2 -140.83 -4190 1.9 hour >20 hour >10 hour 24.17 1490 135.45 24468276 Antiviral Res. 2014 Apr;104:7-14. "Zu X, Liu Y, Wang S, Jin R, Zhou Z, Liu H, Gong R, Xiao G, Wang W." Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. 10.1016/j.antiviral.2014.01.011 Anti-JEV DRAVPe00462 MVDRGWGNHAGLFGKGSIV 19 DN80 Synthetic construct(derived from the E polyprotein of DENV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(17±10% inhibition at 49.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00462 DRAVPe00462.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 2001.29 C89H137N27O24S CEPQTY G 8.52 3 1 2 7 7 4.74 -1180 30 hour >20 hour >10 hour 76.84 5500 305.56 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-DENV DRAVPe00463 AWLVHTQWFLDLPLPWLPGADTQGSNWI 28 DN57 Synthetic construct(derived from the E polyprotein of DENV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(7±4% inhibition at 30.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00463 DRAVPe00463.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 3262.72 C158H221N37O39 CEKMRY L 4.2 1 2 -1 6 14 7.14 300 4.4 hour >20 hour >10 hour 101.07 22000 814.81 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-DENV DRAVPe00464 AWLVHRQWFLDLPLPWLPG 19 DN81 Synthetic construct(derived from the E polyprotein of DENV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(25±8% inhibition at 42.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00464 DRAVPe00464.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 2344.79 C118H166N28O23 CEIKMNSTY L 6.79 2 1 1 1 11 27.37 752 4.4 hour >20 hour >10 hour 123.16 16500 916.67 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-DENV DRAVPe00465 MAILGDTAWDFGSLGGVFTSIGKALHQVFGAIY 33 DN59 Synthetic construct(derived from the E polyprotein of DENV) No entry found Experimentally Validated 11065  envelope (E) glycoprotein M29095.1 residues 412 to 444 residues 412 to 444 M29095 M29095 Not available None "DENV,WNV" Flaviviridae "[Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM,100.0±0.5% inhibition at 20 μM);##West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(>99% inhibition at <25μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. DRAVPe00465 DRAVPe00465.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 3443.96 C161H240N38O44S CENPR G 5.19 2 2 0 11 16 77.58 1883 30 hour >20 hour >10 hour 100.61 6990 218.44 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 "Anti-DENV,MNV" DRAVPe00466 VVDRGWGNGAGLFGKGSID 19 WN82 Synthetic construct(derived from the E polyprotein of WNV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae [Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(4±13% inhibition at 52.5μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00466 DRAVPe00466.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 1905.1 C84H129N25O26 CEHMPQTY G 5.93 2 2 0 8 7 -8.95 -1727 100 hour >20 hour >10 hour 76.84 5500 305.56 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-WNV DRAVPe00467 TFLVHREWFMDLNLPWSSAGSTVWR 25 WN53 Synthetic construct(derived from the E polyprotein of WNV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae "[Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM,56.0±3.0% inhibition at 99μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. DRAVPe00467 DRAVPe00467.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 3036.46 C142H203N37O36S CIKQY LSW 6.42 3 2 1 7 11 -8.4 -3112 7.2 hour >20 hour >10 hour 74 16500 687.5 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-WNV DRAVPe00468 TFLVHREWFMDLNLPWSSA 19 WN83 Synthetic construct(derived from the E polyprotein of WNV) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae "[Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM, 70.0±3.0% inhibition at 128 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. DRAVPe00468 DRAVPe00468.cif Linear Free Free None L envelope The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. 2349.69 C111H157N27O28S CGIKQY L 5.29 2 2 0 4 9 5.26 -1754 7.2 hour >20 hour >10 hour 82.11 11000 611.11 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  "da Silva-Júnior EF, de Araújo-Júnior JX. " "Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses." 10.1016/j.bmc.2019.07.038 Anti-WNV DRAVPe00469 AIGSILGALAKGLPTLISWIKNR 23 AR-23 Rana tagoi (Tago frog) A7BJK6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 6dst "HSV,MeV,HPIV,HCoV-229E" "Herpesviridae, Paramyxoviridae, Coronaviridae" [Ref.35055066]HSV-1: Co-treatment:simultaneous addition of AR-23 and virus to the cells(IC50=0.78 μM);Virus pre-treatment: virus incubated with the peptide(IC50=0.39 μM);Cell pre-treatment: AR-23 incubated with the cells before the viral infection and Post-treatment: AR-23 added to the infected cells(AR-23 had a slight inhibitory effect);inhibition the entry of virus(IC50=3.125μM);inhibition of viral attachment on the host cell membrane(IC50=6.25 μM);##Measles virus (MeV):Co-treatment: simultaneous addition of AR-23 and virus to the cells(IC50=6.25 μM);Virus pre-treatment: virus incubated with the peptide(IC50=3.125 μM);##Human parainfluenza virus type-2 (HPIV2):Co-treatment: simultaneous addition of AR-23 and virus to the cells(IC50=6.25 μM);Virus pre-treatment: virus incubated with the peptide(IC50=3.125 μM);##HCoV-229E:Virus pre-treatment: virus incubated with the peptide(IC50=3.125 μM);##SARS-CoV-2:Co-treatment:simultaneous addition of AR-23 and virus to the cells(60% of inhibition at 25 μM);Virus pre-treatment: virus incubated with the peptide(IC50=12.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.35055066]Vero cells:CC50=25 μM; >80% cytotoxic against Vero cells at 100 and 50 µM. DRAVPe00469 DRAVPe00469.cif Linear Free Amidation None L envelope glycoprotein No machanism information found in the reference(s) presented in this entry 2392.91 C111H190N30O28 CDEFHMQVY IL 11.17 3 0 3 7 12 73.04 791 4.4 hour >20 hour >10 hour 148.7 5500 250 35055066 Int J Mol Sci. 2022 Jan 14;23(2):883. "Chianese A, Zannella C, Monti A, De Filippis A, Doti N, Franci G, Galdiero M." The Broad-Spectrum Antiviral Potential of the Amphibian Peptide AR-23. 10.3390/ijms23020883 "Anti-HSV,Anti-MeV,Anti-HPIV,Anti-HCoV-229E" DRAVPe00470 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P4HC Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,HCoV-229E,HCoV-OC43,MERS-CoV" Coronaviridae pseudovirus inhibition assay [Ref.34769299]SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.8 μM);##SARS-CoV-2 B.1.1.7 (Alpha):inhibition of Pseudoviruse infection in Caco2 cells(IC50=2.28 μM);##SARS-CoV-2 B.1.351 (Beta):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.62 μM);##SARS-CoV-2 P.1 (Gamma):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.48 μM);##SARS-CoV-2 B.1.617.2 (Delta):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.11 μM);##HCoV-229E(Authentic):inhibition of infection in Caco2 cells(IC50=0.48 μM);##HCoV-OC43(Authentic):inhibition of infection in Caco2 cells(IC50=0.41 μM);##SARS-CoV:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.35 μM);##MERS-CoV:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.10 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. No predicted structure available DRAVPe00470.cif Linear Free PEG4-25-HC None L mambrane "The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. "Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. " "25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses." 10.3390/ijms222111869 "Anti-SARS-CoV-2,SARS-CoV,Anti-HCoV-229E,Anti-HCoV-OC43,Anti-MERS-CoV" DRAVPe00471 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P8HC Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.34769299]SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=3.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. No predicted structure available DRAVPe00471.cif Linear Free PEG8-25-HC None L membrane "The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. "Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. " "25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses." 10.3390/ijms222111869 Anti-SARS-CoV-2 DRAVPe00472 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P12HC Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.34769299]SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=5.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. No predicted structure available DRAVPe00472.cif Linear Free PEG12-25-HC None L membrane` "The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. "Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. " "25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses." 10.3390/ijms222111869 Anti-SARS-CoV-2 DRAVPe00473 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P24HC Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.34769299]SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=10.3 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. No predicted structure available DRAVPe00473.cif Linear Free PEG24-25-HC None L membrane "The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level." 4677.29 C208H336N48O71S CHPRW EL 4.36 5 10 -5 11 13 -44.88 -6701 1.9 hour >20 hour >10 hour 104.63 2980 74.5 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. "Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. " "25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses." 10.3390/ijms222111869 Anti-SARS-CoV-2 DRAVPe00474 TFLDKFNHEAEDLFYQ 16 ACE2 (27-42)(SAP1) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,HCoV-OC43,VSV" "Coronaviridae, Rhabdoviridae" pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=2.39±0.20 mM);Inhibition of infection in 293T/ACE2/GFP cells(IC50=3 mM);##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(80% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM;##HCoV-NL63:Inhibition of cytopathic effect in LLC-MK2 cells(30% Inhibition at 3 mM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00474 DRAVPe00474.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 2017.18 C94H129N21O29 CGIMPRSVW F 4.31 2 4 -2 3 6 -76.88 -3557 7.2 hour >20 hour >10 hour 55 1490 99.33 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 "Anti-SARS-CoV-2,Anti-SARS-CoV,Anti-HCoV-OC43,Anti-VSV" DRAVPe00475 EDLFYQSSL 9 ACE2 (37-45)(SAP2) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=3.72±0.37 mM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00475 DRAVPe00475.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 1101.18 C50H72N10O18 ACGHIKMNPRTVW LS 3.67 0 2 -2 3 3 -33.33 -1519 1 hour 30 min >10 hour 86.67 1490 186.25 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 Anti-SARS-CoV-2 DRAVPe00476 LAQMYPL 7 ACE2 (79-85)(SAP3) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00476 DRAVPe00476.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 835.03 C39H62N8O10S CDEFGHIKNRSTVW L 5.52 0 0 0 1 3 70 832 5.5 hour 3 min 2 min 125.71 1490 248.33 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 Anti-SARS-CoV-2 DRAVPe00477 GKGDFRIL 8 ACE2 (352-359)(SAP4) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00477 DRAVPe00477.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 905.06 C41H68N12O11 ACEHMNPQSTVWY G 8.75 2 1 1 2 3 -20 -1449 30 hour >20 hour >10 hour 97.5 0 0 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 Anti-SARS-CoV-2 DRAVPe00478 QAKTFLDKFNHEA 13 ACE2 (24-36)(SAP5) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM);No nhibition of infection in 293T/ACE2/GFP cells up to 3 mM;##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(30% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00478 DRAVPe00478.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 1548.72 C70H105N19O21 CGIMPRSVWY AFK 6.75 3 2 1 2 5 -97.69 -3154 0.8 hour 10 min >10 hour 45.38 0 0 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 "Anti-SARS-CoV-2,SARS-CoV,Anti-VSV" DRAVPe00479 EDLFYQ 6 ACE2 (37-42)(SAP6) Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV-2,SARS-CoV,VSV" "Coronaviridae, Rhabdoviridae" pseudovirus inhibition assay [Ref.33356169]SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=1.9±0.14 mM);Inhibition of infection in 293T/ACE2/GFP cells(IC50=3 mM);##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(85% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM;##HCoV-NL63:Inhibition of cytopathic effect in LLC-MK2 cells(30% Inhibition at 3 mM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00479 DRAVPe00479.cif Linear Free Free None L Not found Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. 813.86 C38H51N7O13 ACGHIKMNPRSTVW DEFLQY 3.67 0 2 -2 1 2 -86.67 -1331 1 hour 30 min >10 hour 65 1490 298 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. "Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A." Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. 10.1021/acs.bioconjchem.0c00664 "Anti-SARS-CoV-2,SARS-CoV,Anti-VSV" DRAVPe00480 DEDLEELERLYRKAEEVAKEAKDASRRGDDERAKEQMERAMRLFDQVFELAQELQEKQTDGNRQKATHLDKAVKEAADELYQRVR 85 AHB1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV-2 Coronaviridae neutralization assay [Ref.32907861]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=35 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00480 DRAVPe00480.cif Linear Free Free None L spike protein The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. 10096.13 C426H695N133O147S2 CIPW E 4.9 19 24 -5 8 25 -141.88 -34516 1.1 hour 3 min >10 hour 63.29 2980 35.48 32907861 Science. 2020 Oct 23;370(6515):426-431. "Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. " De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. 10.1126/science.abd9909 Anti-SARS-CoV-2 DRAVPe00481 ELEEQVMHVLDQVSELAHELLHKLTGEELERAAYFNWWATEMMLELIKSDDEREIREIEEEARRILEHLEELARK 75 AHB2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae neutralization assay [Ref.32907861]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=15.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00481 DRAVPe00481.cif Linear Free Free None L spike protein The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. 9101.25 C399H633N109O128S3 CP E 4.56 13 22 -9 7 28 -66.67 -19283 1 hour 30 min >10 hour 102.8 12490 168.78 32907861 Science. 2020 Oct 23;370(6515):426-431. "Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. " De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. 10.1126/science.abd9909 Anti-SARS-CoV-2 DRAVPe00482 DKEWILQKIYEIMRLLDELGHAEASMRVSDLIYEFMKKGDERLLEEAERLLEEVER 56 LCB1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae neutralization assay [Ref.32907861]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=23.54 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00482 DRAVPe00482.cif Linear Free Free None L spike protein The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. 6810.81 C301H485N79O94S3 CNPT E 4.59 10 16 -6 6 20 -57.5 -13897 1.1 hour 3 min >10 hour 106.25 8480 154.18 32907861 Science. 2020 Oct 23;370(6515):426-431. "Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. " De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. 10.1126/science.abd9909 Anti-SARS-CoV-2 DRAVPe00483 NDDELHMLMTDLVYEALHFAKDEEIKKRVFQLFELADKAYKNNDRQKLEKVVEELKELLERLLS 64 LCB3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae neutralization assay [Ref.32907861]SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=48.1 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00483 DRAVPe00483.cif Linear Free Free None L spike protein The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. 7736.88 C346H556N90O106S2 CGPW L 4.94 13 16 -3 7 24 -66.25 -15515 1.4 hour 3 min >10 hour 103.59 2980 47.3 32907861 Science. 2020 Oct 23;370(6515):426-431. "Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. " De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. 10.1126/science.abd9909 Anti-SARS-CoV-2 DRAVPe00484 GYIEAEVI 8 HIV-1 integrase(82-89) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1 mM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00484 DRAVPe00484.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 893 C41H64N8O14 CDFHKLMNPQRSTW EI 3.79 0 2 -2 2 4 78.75 287 30 hour >20 hour >10 hour 146.25 1490 212.86 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00485 QETAYFLLKLAGRWP 15 HIV-1 integrase(95-109) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00485 DRAVPe00485.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 1793.1 C86H129N21O21 CDHIMNSV L 8.59 2 1 1 3 7 -16.67 -1090 0.8 hour 10 min >10 hour 91.33 6990 499.29 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00486 STTVKAASWWA 11 HIV-1 integrase(123-133) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1 mM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00486 DRAVPe00486.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 1207.35 C56H82N14O16 CDEFGHILMNPQRY A 8.47 1 0 1 4 6 8.18 -336 1.9 hour >20 hour >10 hour 53.64 11000 1100 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00487 HLKTAVQMAVFIHNFKR 17 HIV-1 integrase(171-187) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00487 DRAVPe00487.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 2040.46 C94H150N28O21S CDEGPSWY AFHKV 11.17 5 0 5 2 8 8.24 -2024 3.5 hour 10 min >10 hour 91.76 0 0 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00488 AGERIVDIIATDIQ 14 HIV-1 integrase(196-210) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=2.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00488 DRAVPe00488.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 1513.71 C65H112N18O23 CFHKLMNPSWY I 4.03 1 3 -2 2 7 44.29 -1900 4.4 hour >20 hour >10 hour 146.43 0 0 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00489 QETAYFLLKLAGR 13 HIV-1 integrase(95-107) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=150 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00489 DRAVPe00489.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 1509.77 C70H112N18O19 CDHIMNPSVW L 8.59 2 1 1 3 6 0 -1323 0.8 hour 10 min >10 hour 105.38 1490 124.17 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00490 AGERIVDIIA 10 HIV-1 integrase(196-206) Synthetic construct(derived from HIV-1 integrase) P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae HIV-1 Integrase 30 -DNA Processing Assay [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=30 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00490 DRAVPe00490.cif Linear Free Amidation None L Integrase The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. 1056.23 C46H81N13O15 CFHKLMNPQSTWY I 4.37 1 2 -1 1 6 94 -709 4.4 hour >20 hour >10 hour 166 0 0 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. "Zhao L, O'Reilly MK, Shultz MD, Chmielewski J." Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  10.1016/s0960-894x(03)00040-4 Anti-HIV DRAVPe00491 WNSLKIDNLDV 11 LEDGF 361–370 Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(81% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00491 DRAVPe00491.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1316.48 C59H93N15O19 ACEFGHMPQRTY DLN 4.21 1 2 -1 3 5 -30 -1854 2.8 hour 3 min 2 min 132.73 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00492 WASLKIDNLDV 11 LEDGF 361–370[N361A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(76% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00492 DRAVPe00492.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1273.45 C58H92N14O18 CEFGHMPQRTY DL 4.21 1 2 -1 2 6 18.18 -1009 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00493 WNALKIDNLDV 11 LEDGF 361–370[S362A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(79% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00493 DRAVPe00493.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1300.48 C59H93N15O18 CEFGHMPQRSTY DLN 4.21 1 2 -1 2 6 -6.36 -1333 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00494 WNSAKIDNLDV 11 LEDGF 361–370[L363A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(71% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00494 DRAVPe00494.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1274.4 C56H87N15O19 CEFGHMPQRTY DN 4.21 1 2 -1 3 5 -48.18 -2165 2.8 hour 3 min 2 min 106.36 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00495 WNSLAIDNLDV 11 LEDGF 361–370[K364A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(68% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00495 DRAVPe00495.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1259.38 C56H86N14O19 CEFGHKMPQRTY DLN 3.56 0 2 -2 3 6 21.82 -1118 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00496 WNSLKADNLDV 11 LEDGF 361–370[I365A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(65% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00496 DRAVPe00496.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1274.4 C56H87N15O19 CEFGHIMPQRTY DLN 4.21 1 2 -1 3 5 -54.55 -2165 2.8 hour 3 min 2 min 106.36 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00497 WNSLKIANLDV 11 LEDGF 361–370[D366A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(58% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00497 DRAVPe00497.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1272.47 C58H93N15O17 CEFGHMPQRTY LN 5.84 1 1 0 3 6 18.18 -801 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00498 WNSLKIDALDV 11 LEDGF 361–370[N367A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(75% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00498 DRAVPe00498.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1273.45 C58H92N14O18 CEFGHMPQRTY DL 4.21 1 2 -1 2 6 18.18 -1009 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00499 WNSLKIDNADV 11 LEDGF 361–370[L368A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(75% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00499 DRAVPe00499.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1274.4 C56H87N15O19 CEFGHMPQRTY DN 4.21 1 2 -1 3 5 -48.18 -2165 2.8 hour 3 min 2 min 106.36 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00500 WNSLKIDNLAV 11 LEDGF 361–370[D369A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(73% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00500 DRAVPe00500.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1272.47 C58H93N15O17 CEFGHMPQRTY LN 5.84 1 1 0 3 6 18.18 -801 2.8 hour 3 min 2 min 141.82 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00501 WNSLKIDNLDA 11 LEDGF 361–370[V370A] Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(68% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00501 DRAVPe00501.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1288.42 C57H89N15O19 CEFGHMPQRTVY DLN 4.21 1 2 -1 3 5 -51.82 -2077 2.8 hour 3 min 2 min 115.45 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00502 WNSLKIANLAV 11 "LEDGF 361–370[D366A,D369A]" Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(43% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00502 DRAVPe00502.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1228.46 C57H93N15O15 CDEFGHMPQRTY ALN 8.75 1 0 1 3 7 66.36 252 2.8 hour 3 min 2 min 150.91 5500 550 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00503 WIDNLD 6 LEDGF 365–369 Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(30% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00503 DRAVPe00503.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 774.83 C35H50N8O12 ACEFGHKMPQRSTVY D 3.56 0 2 -2 1 3 -51.67 -1191 2.8 hour 3 min 2 min 130 5500 1100 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00504 WKFALKVDSPDV 12 HRP2 483–493 Synthetic construct Q7Z4V5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae quantitative assay(IN enzymatic activity) [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(25% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00504 DRAVPe00504.cif Linear Free Free None L Integrase The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. 1404.63 C67H101N15O18 CEGHIMNQRTY DKV 5.96 2 2 0 1 6 -10.83 -1182 2.8 hour 3 min 2 min 89.17 5500 500 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  "Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A." Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. 10.1016/j.bbrc.2010.02.100 Anti-HIV DRAVPe00505 WEEWDKKIEEYTKKIEELIKKSQNQQ 26 WQ(628-653) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=123.4 ±6.5 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=159.5 ± 9.5 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=126.2 ± 9.2 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=81.2-383.3 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=13.5-686.2 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=34.8-433.1 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=195.1-1128.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00505 DRAVPe00505.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3351.76 C151H236N38O48 ACFGHMPRV EK 5.19 6 7 -1 4 6 -189.23 -8791 2.8 hour 3 min 2 min 60 12490 499.6 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00506 MTWEEWDKKIEEYTKKIEELIKKSQNQQ 28 MT-WQ(626-653) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=8.8 ±0.4 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=14.8 ± 2.8 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=6.7 ± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00506 DRAVPe00506.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3584.06 C160H252N40O51S ACFGHPRV EK 5.19 6 7 -1 5 6 -171.43 -8813 30 hour >20 hour >10 hour 55.71 12490 462.59 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00507 WEEWDKKIEEYTKKIEELIKKSQNQQSM 28 WQ-SM(628-655) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=60.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00507 DRAVPe00507.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3570.03 C159H250N40O51S ACFGHPRV EK 5.19 6 7 -1 5 6 -171.79 -8896 2.8 hour 3 min 2 min 55.71 12490 462.59 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00508 WEEWDKKIEEYTKKIEELIKKSQNQQSW 28 WQ-SW(628-655) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=47.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00508 DRAVPe00508.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3625.05 C165H251N41O51 ACFGHMPRV EK 5.19 6 7 -1 5 7 -181.79 -8898 2.8 hour 3 min 2 min 55.71 17990 666.3 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00509 WEEWDKKIEEYTKKIEELIKKSQNQQSY 28 WQ-SY(628-655) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=54.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00509 DRAVPe00509.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3602.01 C163H250N40O52 ACFGHMPRV EK 5.19 6 7 -1 6 6 -183.21 -9145 2.8 hour 3 min 2 min 55.71 13980 517.78 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00510 WEEWDKKIEEYTKKIEELIKKSQNQQSDLD 30 WQ-SDLD(628-657) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=44.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00510 DRAVPe00510.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3782.18 C168H262N42O57 ACFGHMPRV EK 4.65 6 9 -3 5 7 -177.33 -10383 2.8 hour 3 min 2 min 65 12490 430.69 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00511 WEEWDKKIEEYTKKIEELIKKSQNQQLDL 29 WQ-LDL(628-656) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.7 ±1.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=6.4 ±2.7 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.6± 0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00511 DRAVPe00511.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3693.17 C167H263N41O53 ACFGHMPRV EK 4.86 6 8 -2 4 8 -155.52 -8679 2.8 hour 3 min 2 min 80.69 12490 446.07 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00512 WEEWDKKIEEYTKKIEELIKKSQNQQIDI 29 WQ-IDI(628-656) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.7 ±0.3 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=6.4 ± 1.8 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.2 ± 0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00512 DRAVPe00512.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3693.17 C167H263N41O53 ACFGHMPRV EK 4.86 6 8 -2 4 8 -150.69 -8679 2.8 hour 3 min 2 min 80.69 12490 446.07 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00513 WEEWDKKIEEYTKKIEELIKKSQNQQLDI 29 WQ-LDI(628-656) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.6±0.2nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=7.2 ± 1.0 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.1 ± 0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00513 DRAVPe00513.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3693.17 C167H263N41O53 ACFGHMPRV EK 4.86 6 8 -2 4 8 -153.1 -8679 2.8 hour 3 min 2 min 80.69 12490 446.07 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00514 WEEWDKKIEEYTKKIEELIKKSQNQQIDL 29 WQ-IDL(628-656) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=1.6 ±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=5.6± 1.2 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=2.5 ± 0.1 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=2.0-90.7 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.8-37.4 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=1.6-22.0 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=8.5-61.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00514 DRAVPe00514.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3693.17 C167H263N41O53 ACFGHMPRV EK 4.86 6 8 -2 4 8 -153.1 -8679 2.8 hour 3 min 2 min 80.69 12490 446.07 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00515 MTWEEWDKKIEEYTKKIEELIKKSQNQQIDL 31 MT-WQ-IDL(626-656) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=0.6±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=1.2± 0.2 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=0.6 ±0.1 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=0.5-15.1 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.1-9.0 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=0.1-4.4 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=1.1-11.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00515 DRAVPe00515.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3925.47 C176H279N43O56S ACFGHPRV EK 4.86 6 8 -2 5 8 -139.35 -8701 30 hour >20 hour >10 hour 75.48 12490 416.33 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00516 EEQKTQLKNKIEIDWTKMELEQDWSKIYKEI 31 MT-WQ-IDL-scrambled Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.27795416]HIV-1 IIIB:inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50>500 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50>500 nM);## No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00516 DRAVPe00516.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3925.47 C176H279N43O56S ACFGHPRV EK 4.86 6 8 -2 5 8 -139.35 -8701 1 hour 30 min >10 hour 75.48 12490 416.33 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-HIV DRAVPe00517 TTLLDLTYEMLSLQQVVKALNESYIDLKEL 30 M0 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae ELISA [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=4.5 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=17.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00517 DRAVPe00517.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3485.05 C157H259N35O51S CFGHPRW L 4.18 2 5 -3 8 12 16.33 -2496 7.2 hour >20 hour >10 hour 139.67 2980 102.76 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-MERS-CoV DRAVPe00518 EANTTLLDLTYEMLSLQQVVKALNESYIDLKEL 33 M1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MERS-CoV Coronaviridae ELISA [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=0.9 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=2.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00518 DRAVPe00518.cif Linear Free Free None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3799.35 C169H277N39O57S CFGHPRW L 4.08 2 6 -4 9 13 -0.91 -3660 1 hour 30 min >10 hour 130 2980 93.13 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. "Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1128/JVI.01445-16 Anti-MERS-CoV DRAVPe00519 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELL 34 C34 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=7.3± 2.5 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=15± 2.3 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=23 ± 5.0 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=19 ±4.7 nM).##[Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=7.2±0.2 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=18.8± 1.6 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=7.6±0.2 nM);## No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00519 DRAVPe00519.cif Linear Free Free None L membrane "The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion." 4248.6 C184H280N50O64S ACFGPV E 4.21 3 8 -5 9 9 -127.06 -10170 2.8 hour 3 min 2 min 80.29 12490 378.48 19073606##27795416 J Biol Chem. 2009 Feb 20;284(8):4914-20.##J Virol. 2016 Dec 16;91(1):e01445-16. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M.##Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20.##Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1074/jbc.M807169200##10.1128/JVI.01445-16 DRAVPa0875 Anti-HIV DRAVPe00520 YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF 36 T-20(Enfuvirtide) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "MAGI/cMAGI infectivity assay,neutralization assay" [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=2.4 ± 0.6 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=23± 8.2 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=49 ± 10 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=84 ± 16 nM).##[Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=71.8±2.2 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=91.0± 1.2 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=70.5 ±0.9 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=20.4-157.3 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=7.1-91.0 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00520 DRAVPe00520.cif Linear Free Free None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4450.88 C202H298N50O64 CGMPRV EL 4.3 3 7 -4 9 13 -87.5 -7259 2.8 hour 10 min 2 min 89.44 17990 514 19073606##27795416 J Biol Chem. 2009 Feb 20;284(8):4914-20.##J Virol. 2016 Dec 16;91(1):e01445-16. "Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M.##Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. " Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20.##Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. 10.1074/jbc.M807169200##10.1128/JVI.01445-16 DRAVPa0326 Anti-HIV DRAVPe00521 LQQLLFIHFRIGRRRRRRRR 20 peptide 4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00521.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2734.31 C120H209N51O23 ACDEKMNPSTVWY R 12.9 10 0 10 1 7 -125.5 -11852 5.5 hour 3 min 2 min 97.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00522 EAIIRILQQLLFIHFRIGRRRRRRRR 26 peptide 5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.09 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.04 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00522.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3430.17 C152H266N60O31 CDKMNPSTVWY R 12.6 11 1 10 1 11 -68.46 -12368 1 hour 30 min >10 hour 123.85 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00523 ILQQLLFIHFRIGRRRRRRRR 21 peptide 6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.10 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00523 DRAVPe00523.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2847.47 C126H220N52O24 ACDEKMNPSTVWY R 12.9 10 0 10 1 8 -98.1 -11360 20 hour 30 min >10 hour 111.43 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00524 RILQQLLFIHFRIGRRRRRRRR 22 peptide 7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.11 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00524 DRAVPe00524.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3003.65 C132H232N56O25 ACDEKMNPSTVWY R 12.95 11 0 11 1 8 -114.09 -12852 1 hour 2 min 2 min 106.36 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00525 IRILQQLLFIHFRIGRRRRRRRR 23 peptide 8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.26 ±0.04 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.11 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00525 DRAVPe00525.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3116.81 C138H243N57O26 ACDEKMNPSTVWY R 12.95 11 0 11 1 9 -89.57 -12360 20 hour 30 min >10 hour 118.7 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00526 IIRILQQLLFIHFRIGRRRRRRRR 24 peptide 9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.11 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00526 DRAVPe00526.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3229.97 C144H254N58O27 ACDEKMNPSTVWY R 12.95 11 0 11 1 10 -67.08 -11868 20 hour 30 min >10 hour 130 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00527 AIIRILQQLLFIHFRIGRRRRRRRR 25 peptide 10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.08 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.05 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00527 DRAVPe00527.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3301.05 C147H259N59O28 CDEKMNPSTVWY R 12.95 11 0 11 1 11 -57.2 -11687 4.4 hour >20 hour >10 hour 128.8 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00528 EAIIRILQQLLFIEFRIKRRRRRRRR 26 peptide 11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.05± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.01 ± 0.001 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00528 DRAVPe00528.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3493.26 C155H275N59O33 CDGHMNPSTVWY R 12.37 11 2 9 0 11 -83.08 -13232 1 hour 30 min >10 hour 123.85 0 0 3422.14 C151H266N58O33 CDHKMNPSTVWY R 12.369999999999999 Anti-HIV DRAVPe00529 EEIIRKLQQLLFIHFRIGRRRRRRRR 26 peptide 12 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.047 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00529 DRAVPe00529.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3503.22 C154H269N61O33 ACDMNPSTVWY R 12.37 12 2 10 1 9 -121.15 -14277 1 hour 30 min >10 hour 105 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00530 EAIIRILQELLFKHFRIGRRRRRRRR 26 peptide 13 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.14 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.065 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00530 DRAVPe00530.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3446.17 C152H266N60O32 CDMNPSTVWY R 12.37 12 2 10 1 10 -100.77 -13542 1 hour 30 min >10 hour 108.85 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00531 EAIERILKQLLFIHFRIGRRRRRRRR 26 peptide 14 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.23± 0.03 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.15 ± 0.002 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00531 DRAVPe00531.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3446.17 C152H266N60O32 CDMNPSTVWY R 12.37 12 2 10 1 10 -100.77 -13542 1 hour 30 min >10 hour 108.85 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00532 EAEIRIKQQLLFIHFRIGRRRRRRRR 26 peptide 15 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.04 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.031± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00532 DRAVPe00532.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3461.14 C151H263N61O33 CDMNPSTVWY R 12.37 12 2 10 1 9 -128.85 -14588 1 hour 30 min >10 hour 93.85 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00533 EAIIRILQQLEFIHKRIGRRRRRRRR 26 peptide 16 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.71 ± 0.21 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.004µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00533 DRAVPe00533.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3427.12 C148H265N61O33 CDMNPSTVWY R 12.37 12 2 10 1 9 -122.31 -14394 1 hour 30 min >10 hour 108.85 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00534 EEIIRKLQQLLFIEFRIKRRRRRRRR 26 peptide 17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.18 ± 0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.08 ± 0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00534 DRAVPe00534.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 3566.32 C157H278N60O35 ACDGHMNPSTVWY R 12.18 12 3 9 0 9 -135.77 -15141 1 hour 30 min >10 hour 105 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00535 AQQLLFIHFRIGRRRRRRRR 20 peptide 18 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.004 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.08 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00535 DRAVPe00535.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2692.23 C117H203N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -135.5 -12163 4.4 hour >20 hour >10 hour 83 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00536 LAQLLFIHFRIGRRRRRRRR 20 peptide 19 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00536 DRAVPe00536.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2677.26 C118H206N50O22 CDEKMNPSTVWY R 12.9 10 0 10 1 8 -99 -11117 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00537 LQALLFIHFRIGRRRRRRRR 20 peptide 20 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.10 ± 0.004 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00537 DRAVPe00537.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2677.26 C118H206N50O22 CDEKMNPSTVWY R 12.9 10 0 10 1 8 -99 -11117 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00538 LQQALFIHFRIGRRRRRRRR 20 peptide 21 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00538 DRAVPe00538.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2692.23 C117H203N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -135.5 -12163 5.5 hour 3 min 2 min 83 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00539 LQQLAFIHFRIGRRRRRRRR 20 peptide 22 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.003 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00539 DRAVPe00539.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2692.23 C117H203N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -135.5 -12163 5.5 hour 3 min 2 min 83 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00540 LQQLLAIHFRIGRRRRRRRR 20 peptide 23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.34 ± 0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.18 ± 0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00540 DRAVPe00540.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2658.21 C114H205N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -130.5 -11969 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00541 LQQLLFAHFRIGRRRRRRRR 20 peptide 24 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.33 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.22± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00541 DRAVPe00541.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2692.23 C117H203N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -139 -12163 5.5 hour 3 min 2 min 83 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00542 LQQLLFIAFRIGRRRRRRRR 20 peptide 25 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00542 DRAVPe00542.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2668.25 C117H207N49O23 CDEHKMNPSTVWY R 12.9 9 0 9 1 8 -100.5 -11205 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00543 LQQLLFIHARIGRRRRRRRR 20 peptide 26 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.25 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.12± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00543 DRAVPe00543.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2658.21 C114H205N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -130.5 -11969 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00544 LQQLLFIHFAIGRRRRRRRR 20 peptide 27 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.11 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.05 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00544 DRAVPe00544.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2649.2 C117H202N48O23 CDEKMNPSTVWY R 12.85 9 0 9 1 8 -94 -10179 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00545 LQQLLFIHFRAGRRRRRRRR 20 peptide 28 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.20 ± 0.03 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.16 ± 0.02µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00545 DRAVPe00545.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2692.23 C117H203N51O23 CDEKMNPSTVWY R 12.9 10 0 10 1 7 -139 -12163 5.5 hour 3 min 2 min 83 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00546 LQQLLFIHFRIARRRRRRRR 20 peptide 29 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Integrase assay [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.09 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.09 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00546 DRAVPe00546.cif Linear Acetylation Amidation None L Integrase The peptide acts antiviral activity by inhibiting the activity of integrase. 2748.33 C121H211N51O23 CDEGKMNPSTVWY R 12.9 10 0 10 0 8 -114.5 -11765 5.5 hour 3 min 2 min 102.5 0 0 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. "Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H." Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. 10.1016/j.bmc.2010.07.050 Anti-HIV DRAVPe00547 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C8- N27 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=1075±90 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=293±27 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00547 DRAVPe00547.cif Linear C8(octanoic acid) Free None L membrane "N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry." 3140.64 C136H235N45O40 CDFMPTWY Q 10.84 4 1 3 4 11 -47.04 -5436 1 hour 2 min 2 min 133.7 0 0 20605950 FASEB J. 2010 Nov;24(11):4196-202.  "Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y." Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  10.1096/fj.09-151704 Anti-HIV DRAVPe00548 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C12- N27 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=473±74 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=182±15 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00548.cif Linear C12(dodecanoic acid) Free None L membrane "N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry." 3140.64 C136H235N45O40 CDFMPTWY Q 10.84 4 1 3 4 11 -47.04 -5436 1 hour 2 min 2 min 133.7 0 0 20605950 FASEB J. 2010 Nov;24(11):4196-202.  "Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y." Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  10.1096/fj.09-151704 Anti-HIV DRAVPe00549 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C16-N27 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=148±4 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=10±1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00549.cif Linear C16(hexadecanoic acid) Free None L membrane "N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry." 3140.64 C136H235N45O40 CDFMPTWY Q 10.84 4 1 3 4 11 -47.04 -5436 1 hour 2 min 2 min 133.7 0 0 20605950 FASEB J. 2010 Nov;24(11):4196-202.  "Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y." Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  10.1096/fj.09-151704 Anti-HIV DRAVPe00550 RQLLSGIVQQQNNLLRAIEAQQHLL 25 C16- N25 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=484±60 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00550 DRAVPe00550.cif Linear C16(hexadecanoic acid) Free None L membrane "N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry." 2884.33 C125H215N41O37 CDFKMPTWY LQ 9.61 3 1 2 4 11 -21.2 -4327 1 hour 2 min 2 min 144.4 0 0 20605950 FASEB J. 2010 Nov;24(11):4196-202.  "Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y." Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  10.1096/fj.09-151704 Anti-HIV DRAVPe00551 RQLLSGIVQQQNNLLRAIEAQQH 23 C16- N23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=1931±187 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00551 DRAVPe00551.cif Linear C16(hexadecanoic acid) Free None L membrane "N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry." 2658.02 C113H193N39O35 CDFKMPTWY Q 9.61 3 1 2 4 9 -56.09 -5311 1 hour 2 min 2 min 123.04 0 0 20605950 FASEB J. 2010 Nov;24(11):4196-202.  "Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y." Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  10.1096/fj.09-151704 Anti-HIV DRAVPe00552 XDLTXEMLSLQQVVKALNESY 21 P21S1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00552.cif Cyclic Acetylation Amidation ①The 'X' (position: 1 and 5) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (1) and X (5) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2404.15 C95H153N23O31S CFGHIPRW L 4.14 1 3 -2 5 7 -5.71 -2320 106.67 1490 74.5 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00553 LXLTYXMLSLQQVVKALNESY 21 P21S2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.90 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00553.cif Cyclic Acetylation Amidation ①The 'X' (position: 2 and 6) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (2) and X (6) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2436.28 C101H161N23O28S CDFGHIPRW L 6 1 1 0 6 8 39.52 -289 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00554 LDLXYEMXSLQQVVKALNESY 21 P21S3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00554.cif Cyclic Acetylation Amidation ①The 'X' (position: 4 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (4) and X (8) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2466.22 C100H155N23O31S CFGHIPRTW L 4.14 1 3 -2 5 7 -8.57 -2077 5.5 hour 3 min 2 min 106.67 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00555 LDLTXEMLXLQQVVKALNESY 21 P21S4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=7.14 ± 0.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00555.cif Cyclic Acetylation Amidation ①The 'X' (position: 5 and 9) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (5) and X (9) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2430.23 C98H159N23O30S CFGHIPRW L 4.14 1 3 -2 4 8 16.19 -1488 5.5 hour 3 min 2 min 125.24 1490 74.5 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00556 LDLTYEMXSLQXVVKALNESY 21 P21S5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.7±2.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00556.cif Cyclic Acetylation Amidation ①The 'X' (position: 8 and 12) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (8) and X (12) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2439.19 C99H154N22O31S CFGHIPRW L 4.14 1 3 -2 6 7 4.76 -1780 5.5 hour 3 min 2 min 106.67 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00557 LDLTYEMLXLQQXVKALNESY 21 P21S6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00557.cif Cyclic Acetylation Amidation ①The 'X' (position: 9 and 13) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (9) and X (13) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2494.27 C102H159N23O31S CFGHIPRW L 4.14 1 3 -2 5 7 -10 -1906 5.5 hour 3 min 2 min 111.43 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00558 LDLTYEMLSLXQVVXALNESY 21 P21S7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00558.cif Cyclic Acetylation Amidation ①The 'X' (position: 11 and 15) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (11) and X (15) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2424.18 C99H153N21O31S CFGHIKPRW L 3.57 0 3 -3 6 8 41.43 -733 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00559 LDLTYEMLSLQXVVKXLNESY 21 P21S8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.26±0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=3.03 ± 0.29 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.06± 0.34 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.98± 0.28 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29442512]Calu-3 cell:CC50>100 μM No predicted structure available DRAVPe00559.cif Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2481.27 C102H160N22O31S ACFGHIPRW L 4.14 1 3 -2 6 7 14.29 -1469 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00560 LDLTYEMLSLQQVVXALNXSY 21 P21S9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=14.1 ± 2.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00560.cif Cyclic Acetylation Amidation ①The 'X' (position: 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (15) and X (19) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2423.19 C99H154N22O30S CFGHIKPRW L 3.67 0 2 -2 6 8 41.43 -606 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00561 LDLTYEMLSLQQVVKXLNEXY 21 P21S10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.33 ± 0.04 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.97± 0.08 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.82± 0.28 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.89± 0.07 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29442512]Calu-3 cell:CC50>100 μM No predicted structure available DRAVPe00561.cif Cyclic Acetylation Amidation ①The 'X' (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (16) and X (20) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2522.33 C104H163N23O31S ACFGHIPRW L 4.14 1 3 -2 5 7 1.43 -1683 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00562 LXLTYXMLSLQQVVKALNESY 21 P21L2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.9 ±1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00562.cif Linear Acetylation Amidation The 'X' at position 2 and 6 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2436.28 C101H161N23O28S CDFGHIPRW L 6 1 1 0 6 8 39.52 -289 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00563 LDLTXEMLXLQQVVKALNESY 21 P21L4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=8.21 ±0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00563.cif Linear Acetylation Amidation The 'X' at position 5 and 9 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2430.23 C98H159N23O30S CFGHIPRW L 4.14 1 3 -2 4 8 16.19 -1488 5.5 hour 3 min 2 min 125.24 1490 74.5 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00564 LDLTYEMXSLQXVVKALNESY 21 P21L5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=4.49 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00564.cif Linear Acetylation Amidation The 'X' at position 8 and 12 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2439.19 C99H154N22O31S CFGHIPRW L 4.14 1 3 -2 6 7 4.76 -1780 5.5 hour 3 min 2 min 106.67 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00565 LDLTYEMLSLQXVVKXLNESY 21 P21L8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=20.6± 3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00565.cif Linear Acetylation Amidation The 'X' at position 12 and 16 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2481.27 C102H160N22O31S ACFGHIPRW L 4.14 1 3 -2 6 7 14.29 -1469 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00566 LDLTYEMLSLQQVVXALNXSY 21 P21L9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.9 ± 1.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00566.cif Linear Acetylation Amidation The 'X' at position 15 and 19 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2423.19 C99H154N22O30S CFGHIKPRW L 3.67 0 2 -2 6 8 41.43 -606 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00567 LDLTYEMLSLQQVVKXLNEXY 21 P21L10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.55 ± 0.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00567.cif Linear Acetylation Amidation The 'X' at position 16 and 20 are S5((S)-pentenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2522.33 C104H163N23O31S ACFGHIPRW L 4.14 1 3 -2 5 7 1.43 -1683 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00568 LDLTYEMLSLQXVVKXLNESY 21 P21R8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=16.3 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00568.cif Cyclic Acetylation Amidation ①The 'X' at position 12 and 16 are R5 amino acids. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2481.27 C102H160N22O31S ACFGHIPRW L 4.14 1 3 -2 6 7 14.29 -1469 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00569 LDLTYEZLSLQXVVKXLNESY 21 P21S8Z Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.63 ± 0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.80 ± 0.74 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.15± 0.25 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.49±0.18 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29442512]Calu-3 cell:CC50>100 μM No predicted structure available DRAVPe00569.cif Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. The 'Z' at position 7 indicates R8 ((R)-octenyl alanine) L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2478.83 C97H149N21O29 ACFGHIMPRW L 4.14 1 3 -2 6 7 5.24 -1704 5.5 hour 3 min 2 min 120.48 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00570 LDLTYEMLSLQXVVKXLNESF 21 P21S8F Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=2.16± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00570.cif Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2465.27 C102H160N22O30S ACGHIPRW L 4.14 1 3 -2 5 8 33.81 -1157 5.5 hour 3 min 2 min 120.48 1490 74.5 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00571 LDLTYEZLSLQXVVKXLNESF 21 P21S8ZF Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.89 ± 0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00571.cif Cyclic Acetylation Amidation "①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling.,The 'Z' at position 7 indicates R8 ((R)-octenyl alanine)" L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2462.83 C97H149N21O28 ACGHIMPRW L 4.14 1 3 -2 5 8 24.76 -1392 5.5 hour 3 min 2 min 120.48 1490 74.5 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00572 LDLTYEMLSLQQVVKALNESY 21 P21 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00572 DRAVPe00572.cif Linear Acetylation Amidation None L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 2457.82 C110H177N25O36S CFGHIPRW L 4.14 1 3 -2 6 8 6.19 -1842 5.5 hour 3 min 2 min 125.24 2980 149 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00573 SLTQINTTLLDLEYEMKKLEEVVKKLEESYIDLKEL 36 HR2P-M2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Inhibition of MERS-CoV S-Protein-Mediated Cell–Cell Fusion Assay [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.75 ± 0.09 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.07±0.21 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.25± 0.18 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.64± 0.16 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29442512]Calu-3 cell:CC50>100 μM DRAVPe00573 DRAVPe00573.cif Linear Acetylation Amidation None L membrane The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. 4299.98 C193H321N43O64S ACFGHPRW L 4.48 5 9 -4 8 12 -40.56 -6020 1.9 hour >20 hour >10 hour 124.44 2980 85.14 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. "Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K." Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  10.1021/acs.jmedchem.7b01732 Anti-MERS-CoV DRAVPe00574 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNI 36 FP3(FCoV Sgp (1338-1373)) Synthetic construct(derived from S protein of FCoV) P10033 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FCoV Coronaviridae plaque reduction assay [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=14.21 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24312629]Fcwf-4 cell:CC50>200 μM. DRAVPe00574 DRAVPe00574.cif Linear Free Free None L membrane The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. 4136.62 C185H292N46O61 CMPQW L 4.19 3 7 -4 11 15 -3.33 -5515 1.1 hour 3 min 2 min 121.94 1490 42.57 24312629  PLoS One. 2013 Dec 3;8(12):e82081. "Liu IJ, Tsai WT, Hsieh LE, Chueh LL." Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. 10.1371/journal.pone.0082081 Anti-FCoV DRAVPe00575 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNINNTLVNL 43 FP4(FCoV Sgp (1338-1380)) Synthetic construct(derived from S protein of FCoV) P10033 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FCoV Coronaviridae plaque reduction assay [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=1.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24312629]Fcwf-4 cell:CC50>200 μM. DRAVPe00575 DRAVPe00575.cif Linear Free Free None L membrane The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. 4905.49 C218H348N56O72 CMPQW L 4.19 3 7 -4 15 18 -1.4 -6376 1.1 hour 3 min 2 min 126.98 1490 35.48 24312629  PLoS One. 2013 Dec 3;8(12):e82081. "Liu IJ, Tsai WT, Hsieh LE, Chueh LL." Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. 10.1371/journal.pone.0082081 Anti-FCoV DRAVPe00576 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNINNTLVNLEWLNRIE 50 FP5(FCoV Sgp (1338-1387)) Synthetic construct(derived from S protein of FCoV) P10033 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FCoV Coronaviridae plaque reduction assay [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=1.33 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24312629]Fcwf-4 cell:CC50>200 μM. DRAVPe00576 DRAVPe00576.cif Linear Free Free None L membrane The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. 5846.55 C261H412N68O84 CMPQ LN 4.25 4 9 -5 16 21 -16.4 -8677 1.1 hour 3 min 2 min 124.8 6990 142.65 24312629  PLoS One. 2013 Dec 3;8(12):e82081. "Liu IJ, Tsai WT, Hsieh LE, Chueh LL." Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. 10.1371/journal.pone.0082081 Anti-FCoV DRAVPe00577 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKELK 34 SC34EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.9±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00577 DRAVPe00577.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4365.95 C196H315N49O63 ACFGHMPRV EK 5.43 10 11 -1 4 7 -210.29 -12689 2.8 hour 3 min 2 min 57.35 12490 378.48 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00578 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKEL 33 SC33EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00578 DRAVPe00578.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4237.77 C190H303N47O62 ACFGHMPRV E 5.08 9 11 -2 4 7 -204.85 -12134 2.8 hour 3 min 2 min 59.09 12490 390.31 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00579 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKE 32 SC32EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00579 DRAVPe00579.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4124.61 C184H292N46O61 ACFGHMPRV E 5.08 9 11 -2 4 6 -223.13 -12626 2.8 hour 3 min 2 min 48.75 12490 402.9 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00580 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEK 31 SC31EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00580 DRAVPe00580.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3995.5 C179H285N45O58 ACFGHMPRV EK 5.38 9 10 -1 4 6 -219.03 -11945 2.8 hour 3 min 2 min 50.32 12490 416.33 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00581 WEEWDKKIEEYTKKIEELIKKSEEQQKKNE 30 SC30EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1±0 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00581 DRAVPe00581.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3867.32 C173H273N43O57 ACFGHMPRV E 5.03 8 10 -2 4 6 -213.33 -11390 2.8 hour 3 min 2 min 52 12490 430.69 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00582 WEEWDKKIEEYTKKIEELIKKSEEQQKKN 29 SC29EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.2±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00582 DRAVPe00582.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3738.21 C168H266N42O54 ACFGHMPRV EK 5.33 8 9 -1 4 6 -208.62 -10709 2.8 hour 3 min 2 min 53.79 12490 446.07 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00583 WEEWDKKIEEYTKKIEELIKKSEEQQKK 28 SC28EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=18±3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=13±1.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00583 DRAVPe00583.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3624.11 C164H260N40O52 ACFGHMNPRV EK 5.33 8 9 -1 3 6 -203.57 -10045 2.8 hour 3 min 2 min 55.71 12490 462.59 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00584 WEEWDKKIEEYTKKIEELIKKSEEQQK 27 SC27EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=29±2.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21.4±2.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00584 DRAVPe00584.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3495.93 C158H248N38O51 ACFGHMNPRV E 4.97 7 9 -2 3 6 -196.67 -9490 2.8 hour 3 min 2 min 57.78 12490 480.38 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00585 WEEWDKKIEEYTKKIEELIKKSEEQQ 26 SC26EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=44.9±5.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=36.2±4.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00585 DRAVPe00585.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3367.76 C152H236N36O50 ACFGHMNPRV E 4.73 6 9 -3 3 6 -189.23 -8935 2.8 hour 3 min 2 min 60 12490 499.6 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00586 WEEWDKKIEEYTKKIEELIKKSEEQ 25 SC25EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=79.8±9.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=41.5±3.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00586 DRAVPe00586.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3239.63 C147H228N34O48 ACFGHMNPRV E 4.73 6 9 -3 3 6 -182.8 -8381 2.8 hour 3 min 2 min 62.4 12490 520.42 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00587 WEEWDKKIEEYTKKIEELIKKSEE 24 SC24EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=107.6±8 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=75.7±11.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00587 DRAVPe00587.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3111.5 C142H220N32O46 ACFGHMNPQRV E 4.73 6 9 -3 3 6 -175.83 -7827 2.8 hour 3 min 2 min 65 12490 543.04 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00588 WEEWDKKIEEYTKKIEELIKKSE 23 SC23EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=105.1±15.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=94.2±12.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00588 DRAVPe00588.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2982.38 C137H213N31O43 ACFGHMNPQRV E 4.9 6 8 -2 3 6 -168.26 -7146 2.8 hour 3 min 2 min 67.83 12490 567.73 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00589 WEEWDKKIEEYTKKIEELIKKS 22 SC22EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=66.9±15.9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=98.6±7.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00589 DRAVPe00589.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2853.26 C132H206N30O40 ACFGHMNPQRV EK 5.19 6 7 -1 3 6 -160 -6465 2.8 hour 3 min 2 min 70.91 12490 594.76 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00590 WEEWDKKIEEYTKKIEELIKK 21 SC21EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=113.2±8 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=105.4±12.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00590 DRAVPe00590.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2766.19 C129H201N29O38 ACFGHMNPQRSV EK 5.19 6 7 -1 2 6 -163.81 -6125 2.8 hour 3 min 2 min 74.29 12490 624.5 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00591 WEEWDKKIEEYTKKIEELIK 20 SC20EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=126.6±10.7 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=202.4±5.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00591 DRAVPe00591.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2638.01 C123H189N27O37 ACFGHMNPQRSV E 4.82 5 7 -2 2 6 -152.5 -5570 2.8 hour 3 min 2 min 78 12490 657.37 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00592 WEEWDKKIEEYTKKIEELI 19 SC19EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=70.7±9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=217.2±16.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00592 DRAVPe00592.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2509.84 C117H177N25O36 ACFGHMNPQRSV E 4.55 4 7 -3 2 6 -140 -5015 2.8 hour 3 min 2 min 82.11 12490 693.89 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00593 WEEWDKKIEEYTKKIEEL 18 SC18EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50>2000 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>2000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00593 DRAVPe00593.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2396.68 C111H166N24O35 ACFGHMNPQRSV E 4.55 4 7 -3 2 5 -172.78 -5507 2.8 hour 3 min 2 min 65 12490 734.71 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00594 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKELK 36 MT-SC34EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00594 DRAVPe00594.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4598.25 C205H331N51O66S ACFGHPRV EK 5.42 10 11 -1 5 7 -195.28 -12711 30 hour >20 hour >10 hour 54.17 12490 356.86 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00595 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKEL 35 MT-SC33EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.2±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00595 DRAVPe00595.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4470.07 C199H319N49O65S ACFGHPRV E 5.08 9 11 -2 5 7 -189.71 -12156 30 hour >20 hour >10 hour 55.71 12490 367.35 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00596 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKE 34 MT-SC32EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00596 DRAVPe00596.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4356.91 C193H308N48O64S ACFGHPRV E 5.08 9 11 -2 5 6 -206.47 -12648 30 hour >20 hour >10 hour 45.88 12490 378.48 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00597 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEK 33 MT-SC31EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00597 DRAVPe00597.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4227.8 C188H301N47O61S ACFGHPRV EK 5.37 9 10 -1 5 6 -202.12 -11967 30 hour >20 hour >10 hour 47.27 12490 390.31 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00598 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNE 32 MT-SC30EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.8±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00598 DRAVPe00598.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 4099.62 C182H289N45O60S ACFGHPRV E 5.03 8 10 -2 5 6 -196.25 -11412 30 hour >20 hour >10 hour 48.75 12490 402.9 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00599 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKN 31 MT-SC29EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.9±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00599 DRAVPe00599.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3970.51 C177H282N44O57S ACFGHPRV EK 5.32 8 9 -1 5 6 -191.29 -10731 30 hour >20 hour >10 hour 50.32 12490 416.33 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00600 MTWEEWDKKIEEYTKKIEELIKKSEEQQKK 30 MT-SC28EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.2±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00600 DRAVPe00600.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3856.4 C173H276N42O55S ACFGHNPRV EK 5.32 8 9 -1 4 6 -186 -10067 30 hour >20 hour >10 hour 52 12490 430.69 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00601 MTWEEWDKKIEEYTKKIEELIKKSEEQQK 29 MT-SC27EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.4±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00601 DRAVPe00601.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3728.23 C167H264N40O54S ACFGHNPRV E 4.97 7 9 -2 4 6 -178.97 -9512 30 hour >20 hour >10 hour 53.79 12490 446.07 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00602 MTWEEWDKKIEEYTKKIEELIKKSEEQQ 28 MT-SC26EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.6±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00602 DRAVPe00602.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3600.05 C161H252N38O53S ACFGHNPRV E 4.73 6 9 -3 4 6 -171.43 -8957 30 hour >20 hour >10 hour 55.71 12490 462.59 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00603 MTWEEWDKKIEEYTKKIEELIKKSEEQ 27 MT-SC25EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.9±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00603 DRAVPe00603.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3471.92 C156H244N36O51S ACFGHNPRV E 4.73 6 9 -3 4 6 -164.81 -8403 30 hour >20 hour >10 hour 57.78 12490 480.38 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00604 MTWEEWDKKIEEYTKKIEELIKKSEE 26 MT-SC24EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.8±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.3±0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00604 DRAVPe00604.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3343.79 C151H236N34O49S ACFGHNPQRV E 4.73 6 9 -3 4 6 -157.69 -7849 30 hour >20 hour >10 hour 60 12490 499.6 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00605 MTWEEWDKKIEEYTKKIEELIKKSE 25 MT-SC23EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.9±0.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00605 DRAVPe00605.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3214.68 C146H229N33O46S ACFGHNPQRV E 4.9 6 8 -2 4 6 -150 -7168 30 hour >20 hour >10 hour 62.4 12490 520.42 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00606 MTWEEWDKKIEEYTKKIEELIKKS 24 MT-SC22EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.4±0.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.2±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00606 DRAVPe00606.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3085.56 C141H222N32O43S ACFGHNPQRV EK 5.19 6 7 -1 4 6 -141.67 -6487 30 hour >20 hour >10 hour 65 12490 543.04 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00607 MTWEEWDKKIEEYTKKIEELIKK 23 MT-SC21EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=3.8±0.4 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3.1±1.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00607 DRAVPe00607.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2998.48 C138H217N31O41S ACFGHNPQRSV EK 5.19 6 7 -1 3 6 -144.35 -6147 30 hour >20 hour >10 hour 67.83 12490 567.73 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00608 MTWEEWDKKIEEYTKKIEELIK 22 MT-SC20EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=3.7±0.5 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3.3±1.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00608 DRAVPe00608.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2870.31 C132H205N29O40S ACFGHNPQRSV E 4.82 5 7 -2 3 6 -133.18 -5592 30 hour >20 hour >10 hour 70.91 12490 594.76 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00609 MTWEEWDKKIEEYTKKIEELI 21 MT-SC19EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=5±0.9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=4.9±1.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00609 DRAVPe00609.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2742.14 C126H193N27O39S ACFGHNPQRSV E 4.55 4 7 -3 3 6 -120.95 -5037 30 hour >20 hour >10 hour 74.29 12490 624.5 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00610 MTWEEWDKKIEEYTKKIEEL 20 MT-SC18EK Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50>2000 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>2000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00610 DRAVPe00610.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 2628.98 C120H182N26O38S ACFGHNPQRSV E 4.55 4 7 -3 3 5 -149.5 -5529 30 hour >20 hour >10 hour 58.5 12490 657.37 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00611 MTWEEWDKKIEEYTKKIEELIKKSQNQQEKN 31 MT-WQ-EKN Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00611 DRAVPe00611.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3955.45 C175H277N45O57S ACFGHPRV EK 5.26 7 8 -1 6 6 -190 -10713 30 hour >20 hour >10 hour 50.32 12490 416.33 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00612 WEEWDKKIEEYTKKIEELIKKSQNQQEKN 29 WQ-EKN Synthetic construct Q5DP94 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "dual split-protein (DSP)-based cell-cell fusion assay,luciferase assay" [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.4±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00612 DRAVPe00612.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. 3723.15 C166H261N43O54 ACFGHMPRV EK 5.26 7 8 -1 5 6 -207.24 -10691 2.8 hour 3 min 2 min 53.79 12490 446.07 31277353 Viruses. 2019 Jul 3;11(7):609.  "Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y." Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. 10.3390/v11070609 Anti-HIV DRAVPe00613 YTSLIREILVESRIQQEKNERELRDIDKWASLWNWF 36 "T20v1(T20 [H6R; S7E; L8,26I; I9L; E10V; Q13,21R; N14I; L24R; E25D])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.10 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.12 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=0.29 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00613 DRAVPe00613.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4566.16 C207H319N57O60 CGHMP E 5.15 6 7 -1 7 14 -81.67 -10436 2.8 hour 10 min 2 min 97.5 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00614 YTSLIHSIIEESRNRQEKNEQALLELDKWASLWNWF 36 "T20v2(T20 [L8I; Q13,15R; E22A])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.09 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.05 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00614 DRAVPe00614.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4448.96 C202H304N54O60 CGMPV EL 5.06 5 6 -1 9 14 -76.39 -8273 2.8 hour 10 min 2 min 92.22 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00615 YTSLLRSIIEEGRNQQEKNEQALLELDKWASLWNWF 36 "T20v3(T20 [I5L, H6R, L8I; S12G; Q13R; E22A])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.13 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.08 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.19 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.08 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.34 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00615 DRAVPe00615.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4409.92 C200H303N53O60 CHMPV L 4.72 4 6 -2 9 14 -78.06 -7927 2.8 hour 10 min 2 min 92.22 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00616 YTSLIRSIIEESRNQQEKNEQKLLEVDKWASLWNWF 36 "T20v4(T20 [H6R, L8I, Q13R, E22K, L26V])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.15 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.12 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.04 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.22 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00616 DRAVPe00616.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4483.02 C203H310N54O61 CGHMP E 5.11 5 6 -1 9 13 -91.94 -9185 2.8 hour 10 min 2 min 86.67 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00617 YTSLLRSLIEESRNLQEKNEQALLEVDKWASLWNWF 36 "T20v5(T20 [I5L, H6R, Q13R, Q15L, E22A, L26V])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.15 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.14 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.29 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.13 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.69 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00617 DRAVPe00617.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4410.95 C201H306N52O60 CGHMP L 4.72 4 6 -2 9 15 -59.72 -7403 2.8 hour 10 min 2 min 100.28 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00618 YTSLLWSIIEEGRNLQEKNEQKLLELDKWASLWNWF 36 "T20v6(T20 [I5L, H6W, L8I, S12G, Q13R, Q15L, E22K])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.16 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.14 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.21 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.62 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.59 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.10 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.68 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00618 DRAVPe00618.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4482.07 C209H311N51O59 CHMPV L 4.72 4 6 -2 9 15 -63.61 -5892 2.8 hour 10 min 2 min 100.28 23490 671.14 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00619 YTSLIWKVLNDAREQQENNQETLVEIDKWASLWNWF 36 "T20v7(T20 [H6W; S7K; L8,24V; I9L; E10N; E11D; S12A; Q13R; N14E; K18N; E20Q; Q21E; L26I])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.37 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.16 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.45 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=1.12 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.23 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.07 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00619 DRAVPe00619.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4468.95 C205H300N52O61 CGHMP ELNW 4.36 3 6 -3 9 15 -74.17 -7244 2.8 hour 10 min 2 min 86.67 23490 671.14 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00620 YTSLIREIMNKSWGQQRRNEGTLAEIDKWASLWNWF 36 "T20v8(T20 [H6R; S7E; L8,26I; I9M; E10N; E11K; Q13W; N14G; E17R; K18R; Q21G; E22T; L24A])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.40 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.24 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.31 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.53 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=1.11 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.24 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=10.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00620 DRAVPe00620.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4428.99 C201H300N56O56S CHPV W 8.5 5 4 1 11 13 -80.83 -8182 2.8 hour 10 min 2 min 70.56 23490 671.14 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00621 YTSLIRELISNARTQQTDNEESLRNVDKWASLWNWF 36 "T20v9(T20 [H6R; S7E; E10,22S; E11,25N; S12A; Q13R; N14T; E17T; K18D; Q21E; L24R; L26V])" Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=1.20 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.34 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.41 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.82 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=1.09 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.35 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=16.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00621 DRAVPe00621.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4385.82 C195H295N55O61 CGHMP LNS 4.94 4 5 -1 12 13 -84.44 -10012 2.8 hour 10 min 2 min 78.61 17990 514 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00622 YTSLIWSIIIDGREQQRDNEGVLADLDKWASLWNWF 36 T20v10(T20 [H6W; L8I; E10I;E11D;S12G;Q13R;N14E;E17R;K18D;Q21G;E22V;L24D;E25D]) Synthetic construct(derived from T20) P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae neutralization assay [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=23.3 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=3.35 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=12.0 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.45 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.11 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=24.4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00622 DRAVPe00622.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4339.83 C200H293N51O58 CHMP DILW 4.23 3 6 -3 9 16 -35.83 -5996 2.8 hour 10 min 2 min 100.28 23490 671.14 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. "Chen G, Cook JD, Ye W, Lee JE, Sidhu SS." Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. 10.1002/pro.3669 Anti-HIV DRAVPe00623 EKINQSLAFIRKSDELLHNV 20 peptide 4(RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) P03420 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00623 DRAVPe00623.cif Linear Acetylation Free None L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2354.69 C104H172N30O32 CGMPTWY L 6.86 4 3 1 4 8 -44.5 -4521 1 hour 30 min >10 hour 117 0 0 Anti-RSV DRAVPe00624 EKINQSLXFIRXSDXLLHXV 20 peptide 4a(derived from RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.82±0.42 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00624.cif Cyclic Acetylation Free "The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2357.54 C86H134N24O21 ACGMPTWY X 6.85 3 2 1 3 7 1 -2802 1 hour 30 min >10 hour 112 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00625 EKIXQSLXFIXKSDXLLHNV 20 peptide 4bb(derived from RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.74±0.27 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00625.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2329.53 C86H134N22O21 ACGMPRTWY X 6.85 3 2 1 3 7 4 -1865 1 hour 30 min >10 hour 112 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00626 EXINXSLXFIRXSDELLHNV 20 peptide 4ca(derived from RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.59±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00626.cif Cyclic Acetylation Free "The 'X' at position 2 indicates R-pentenylalanine; The 'X' at position 5,8,12 indicates S-pentenylalanine, X(2) and X(5), X(8) and X(12) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2344.46 C84H127N23O23 ACGKMPQTWY X 4.65 2 3 -1 4 7 3 -3038 1 hour 30 min >10 hour 112 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00627 XKINQSLXFIRXSDELLHXV 20 peptide 4ef(derived from RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=3.07±1.45 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00627.cif Cyclic Acetylation Free "The 'X' at position 1,8 indicates R-octenyl-alanine; The 'X' at position 12,19 indicates S-pentenylalanine, X(1) and X(8), X(12) and X(19) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2357.54 C86H134N24O21 ACGMPTWY X 6.75 3 2 1 3 7 1 -2802 112 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00628 EKIXQSLXFIRXSDELLHXV 20 peptide 4bf(derived from RSV fusion protein(497-515)) Synthetic construct(derived from RSV fusion protein) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=2.49±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00628.cif Cyclic Acetylation Free "The 'X' at position 12 indicates R-octenyl-alanine; The 'X' at position 4,8,19 indicates S-pentenylalanine, X(4) and X(8), X(12) and X(19) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2372.55 C87H135N23O22 ACGMNPTWY X 5.45 3 3 0 2 7 1 -2819 1 hour 30 min >10 hour 112 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00629 EKIAQSLXFIRXSDXLLHXV 20 peptide 4a[N500A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=20.41±2.4 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00629.cif Cyclic Acetylation Free "The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2314.52 C85H133N23O20 CGMNPTWY X 6.85 3 2 1 2 8 27.5 -1957 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00630 EKINQSLXFIAXSDXLLHXV 20 peptide 4a[R507A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=175±0.00 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00630.cif Cyclic Acetylation Free "The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2272.43 C83H127N21O21 CGMPRTWY X 5.32 2 2 0 3 8 32.5 -1129 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00631 AKIXQSLXFIXKSDXLLHNV 20 peptide 4bb[E497A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.16±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00631.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2271.49 C84H132N22O19 CEGMPRTWY X 8.64 3 1 2 3 8 30.5 -1003 4.4 hour >20 hour >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00632 EAIXQSLXFIXKSDXLLHNV 20 peptide 4bb[K498A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.60±0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00632.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2272.43 C83H127N21O21 CGMPRTWY X 5.32 2 2 0 3 8 32.5 -1129 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00633 EKAXQSLXFIXKSDXLLHNV 20 peptide 4bb[I499A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.30±0.89 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00633.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2287.45 C83H128N22O21 CGMPRTWY X 6.85 3 2 1 3 7 -9.5 -2176 1 hour 30 min >10 hour 97.5 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00634 EKIXASLXFIXKSDXLLHNV 20 peptide 4bb[Q501A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.28±0.43 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00634.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2272.48 C84H131N21O20 CGMPQRTWY X 6.85 3 2 1 3 8 30.5 -1130 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00635 EKIXQALXFIXKSDXLLHNV 20 peptide 4bb[S502A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.66±0.26 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00635.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2313.53 C86H134N22O20 CGMPRTWY X 6.85 3 2 1 2 8 17 -1344 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00636 EKIXQSAXFIXKSDXLLHNV 20 peptide 4bb[L503A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.95±0.53 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00636.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2287.45 C83H128N22O21 CGMPRTWY X 6.85 3 2 1 3 7 -6 -2176 1 hour 30 min >10 hour 97.5 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00637 EKIXQSLXAIXKSDXLLHNV 20 peptide 4bb[F505A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.39±0.10 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00637.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2253.43 C80H130N22O21 CFGMPRTWY X 6.85 3 2 1 3 7 -1 -1982 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00638 EKIXQSLXFAXKSDXLLHNV 20 peptide 4bb[I506A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=10.44±2.97 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00638.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2287.45 C83H128N22O21 CGMPRTWY X 6.85 3 2 1 3 7 -9.5 -2176 1 hour 30 min >10 hour 97.5 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00639 EKIXQSLXFIXASDXLLHNV 20 peptide 4bb[K508A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=10.93±13.90 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00639.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2272.43 C83H127N21O21 CGMPRTWY X 5.32 2 2 0 3 8 32.5 -1129 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00640 EKIXQSLXFIXKADXLLHNV 20 peptide 4bb[S509A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=82.04±1.56 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00640.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2313.53 C86H134N22O20 CGMPRTWY X 6.85 3 2 1 2 8 17 -1344 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00641 EKIXQSLXFIXKSAXLLHNV 20 peptide 4bb[D510A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.10±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00641.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2285.52 C85H134N22O19 CDGMPRTWY X 8.69 3 1 2 3 8 30.5 -812 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00642 EKIXQSLXFIXKSDXALHNV 20 peptide 4bb[L512A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.88±0.06 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00642.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2287.45 C83H128N22O21 CGMPRTWY X 6.85 3 2 1 3 7 -6 -2176 1 hour 30 min >10 hour 97.5 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00643 EKIXQSLXFIXKSDXLLANV 20 peptide 4bb[H514A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.52±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00643.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2263.47 C83H132N20O21 CGHMPRTWY X 6.17 2 2 0 3 8 29 -1218 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00644 EKIXQSLXFIXKSDXLLHAV 20 peptide 4bb[N515A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=2.71±2.93 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00644.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2286.5 C85H133N21O20 CGMNPRTWY X 6.85 3 2 1 2 8 30.5 -1020 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00645 EKIXQSLXFIXKSDXLLHNA 20 peptide 4bb[V516A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.60±0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00645.cif Cyclic Acetylation Free "The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2301.47 C84H130N22O21 CGMPRTVWY X 6.85 3 2 1 3 7 -8 -2088 1 hour 30 min >10 hour 102.5 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00646 EXINXSLXFIRXSDALLHNV 20 peptide 4ca[E511A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae rHRSV-mCherry inhibition assay [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.00±0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00646.cif Cyclic Acetylation Free "The 'X' at position 2 indicates R-pentenylalanine; The 'X' at position 5,8,12 indicates S-pentenylalanine, X(2) and X(5), X(8) and X(12) are cross-linked by hydrocarbon stapling." L membrane The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. 2286.42 C82H125N23O21 CGKMPQTWY X 5.32 2 2 0 4 8 29.5 -2176 1 hour 30 min >10 hour 117 0 0 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. "Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O." A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. 10.1128/AAC.02241-16 Anti-RSV DRAVPe00647 YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF 36 ENF (T-20) Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "MAGI/cMAGI infectivity assay,neutralization assay" "[Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.006 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.050 μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.526 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=54.958 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=47.822 μg/ml).##[Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.37 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.09 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.30 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.02 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=3.58 µg/ml).##[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=24633±2467 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=10825±1354 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=4503±384 pM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=34858 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=9.12 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=90.18-2250 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=263.68-829.01 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=490.8-648.49 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=157.87 ± 8.79 μM;##MT-4 cell:CC50=171.73± 23.13 μM;##HEK293T cell:CC50=216.23± 33.08 μM;##PBMC:CC50=81.23± 4.59 μM. No predicted structure available DRAVPe00647.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4450.88 C202H298N50O64 CGMPRV EL 4.3 3 7 -4 9 13 -87.5 -7259 2.8 hour 10 min 2 min 89.44 17990 514 17640899##31228294##30089693 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7. ##Protein Sci. 2019 Aug;28(8):1501-1512.##J Virol. 2018 Sep 26;92(20):e01088-18. "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK.##Chen G, Cook JD, Ye W, Lee JE, Sidhu SS.##Chong H, Zhu Y, Yu D, He Y." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus.##Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display.##Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1073/pnas.0701478104##10.1002/pro.3669##10.1128/JVI.01088-18 "Anti-HIV,Anti-SIV" DRAVPe00648 YTSLIHSLIEESQNQQEKNEQELLEX 26 LP-53 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2949±400 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9968±2224 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=21352±1876 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00648.cif Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3114.56 C128H202N34O48 ACDFGMPRVW E 4.2 2 6 -4 7 6 -112.69 -6990 2.8 hour 10 min 2 min 90 1490 59.6 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00649 YTSLIEELIKKSEEQQKKNEEELKX 25 LP-54 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=149±48 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=301±26 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1796±340 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00649.cif Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3048.62 C128H212N32O45 ACDFGHMPRVW E 4.86 5 7 -2 5 5 -150.8 -7805 2.8 hour 10 min 2 min 78 1490 62.08 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00650 WEQKIEELLKKAEEQQKKNEEELKKX 26 LP-55 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=8±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=12±1 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.11-189.34 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=10.67-137.77 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.19-10.61 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=34 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00650.cif Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3267.91 C139H229N37O45 CDFGHMPRSTVY E 5.3 7 8 -1 1 6 -201.92 -9277 2.8 hour 3 min 2 min 63.85 5500 220 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00651 WEQKIEELLKKAEEQQKKNEEELKXX 26 LP-56 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=12±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=11±2 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00651.cif Linear Acetylation Amidation "The 'X' at position 26 is Lys-C16(palmitic acid),The 'X' at position 25 is Lys-AEEA(8-amino-3,6-dioxaoctanoic acid)" L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3251.07 C133H215N35O43 CDFGHMPRSTVY E 4.94 6 8 -2 1 6 -186.92 -8722 2.8 hour 3 min 2 min 63.85 5500 220 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00652 WEQKIEELLKKAEEQQKKNEEEX 23 LP-57 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=213±21 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=178±38 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1917±440 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00652.cif Linear Acetylation Amidation The 'X' at position 23 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2898.41 C121H194N32O42 CDFGHMPRSTVY E 4.69 5 8 -3 1 5 -210.87 -8659 2.8 hour 3 min 2 min 55.22 5500 250 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00653 WEQKIEELLKKAEEQQKKNEX 21 LP-58 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=143000±19911 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=110900±3715 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=107033±9473 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00653.cif Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2640.18 C111H180N30O36 CDFGHMPRSTVY E 5.16 5 6 -1 1 5 -197.62 -7297 2.8 hour 3 min 2 min 60.48 5500 275 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00654 WEQKIEELLKKAEEQQKX 18 LP-59 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>900000 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=240800±23649 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=210477±25537 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00654.cif Linear Acetylation Amidation The 'X' at position 18 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2268.78 C96H155N25O30 CDFGHMNPRSTVY E 5.07 4 5 -1 0 5 -170 -5397 2.8 hour 3 min 2 min 70.56 5500 323.53 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00655 SLIEELIKKSEEQQKKNEEELKKLEX 26 LP-60 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=55±6 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=48±6 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=62±27 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00655.cif Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3154.79 C132H226N34O46 ACDFGHMPRTVWY E 4.94 6 8 -2 3 6 -151.15 -8278 1.9 hour >20 hour >10 hour 90 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00656 IEELIKKSEEQQKKNEEELKKLEX 24 LP-61 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=85±9 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=43±9 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=126±63 pM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=144 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=193.63±13.92 μM;##MT-4 cell:CC50=164.47±37.69 μM;##HEK293T cell:CC50=140.43± 10.7μM;##PBMC:CC50=46.43± 2.6 μM. No predicted structure available DRAVPe00656.cif Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2954.55 C123H210N32O43 ACDFGHMPRTVWY E 4.94 6 8 -2 2 5 -176.25 -8430 20 hour 30 min >10 hour 81.25 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00657 EQKIEELLKKAEEQQKKNEEELKKLEX 27 LP-62 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=15±1 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=5±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=12±1 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00657.cif Linear Acetylation Amidation The 'X' at position 27 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3323.98 C139H237N37O48 CDFGHMPRSTVWY E 5 7 9 -2 1 6 -190 -9699 1 hour 30 min >10 hour 75.93 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00658 QKIEELLKKAEEQQKKNEEELKKLEX 26 LP-63 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=17±5 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=6±2 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=13±2 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00658.cif Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3194.86 C134H230N36O45 CDFGHMPRSTVWY E 5.3 7 8 -1 1 6 -183.85 -9018 0.8 hour 10 min >10 hour 78.85 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00659 KIEELLKKAEEQQKKNEEELKKLEX 25 LP-64 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=128±27 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=36±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=25±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.04 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.08-140.75 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.23-0.75 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.10-0.11 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=58 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00659.cif Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3066.73 C129H222N34O43 CDFGHMPRSTVWY E 5.3 7 8 -1 1 6 -177.2 -8464 1.3 hour 3 min 2 min 82 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00660 IEELLKKAEEQQKKNEEELKKLEX 24 LP-65 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=8±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=7±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.15-88.63 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.23-0.75 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.07-0.04 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=35 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=256.23 ±14.58 μM;##MT-4 cell:CC50=213.4±59.59 μM;##HEK293T cell:CC50=208.43± 22.9μM;##PBMC:CC50=49.95± 2.97 μM. No predicted structure available DRAVPe00660.cif Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2938.56 C123H210N32O42 CDFGHMPRSTVWY E 4.94 6 8 -2 1 6 -168.33 -7909 20 hour 30 min >10 hour 85.42 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00661 EELLKKAEEQQKKNEEELKKLEX 23 LP-66 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1008±248 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=434±71 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1109±193 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00661.cif Linear Acetylation Amidation The 'X' at position 23 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2825.4 C117H199N31O41 CDFGHIMPRSTVWY E 4.94 6 8 -2 1 5 -195.22 -8401 1 hour 30 min >10 hour 72.17 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00662 LLEQAEEQQKKNEEELKKLEX 21 LP-67 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3417±419 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=627±154 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1527±565 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00662.cif Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2568.06 C105H176N28O38 CDFGHIMPRSTVWY E 4.6 4 7 -3 1 5 -176.67 -7164 5.5 hour 3 min 2 min 79.05 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00663 AEEQQKKNEEELKKLEX 17 LP-68 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>250000 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>250000 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>250000 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00663.cif Linear Acetylation Amidation The 'X' at position 17 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2084.5 C83H139N23O31 CDFGHIMPRSTVWY E 4.77 4 6 -2 1 3 -221.76 -6913 4.4 hour >20 hour >10 hour 51.76 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00664 IEELLKKAEEQQKKNEEELKX 21 LP-69 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=239±16 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=125±27 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=157±29 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.31 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=2.01-1815.67 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=9.83-152.28 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.56-11.91 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=1391 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00664.cif Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2568.11 C106H180N28O37 CDFGHMPRSTVWY E 4.86 5 7 -2 1 5 -175.24 -7165 20 hour 30 min >10 hour 79.05 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00665 INNYTSLIEELIKKSEEQQKKNEEELKKLEX 31 LP-70 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=25±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=21±4 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=30±10 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00665.cif Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3760.44 C159H265N41O55 ACDFGHMPRVW E 4.94 6 8 -2 7 7 -141.29 -9385 20 hour 30 min >10 hour 88.06 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00666 IEEYTKKIEEILKKSEEQQKKNEEELKKLEX 31 LP-71 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=27±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=25±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=55±5 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00666.cif Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3846.57 C164H275N41O56 ACDFGHMPRVW E 5.06 8 10 -2 4 6 -176.13 -10681 20 hour 30 min >10 hour 75.48 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00667 VRYLEANIEELLKKAEEQQKKNEEELKKLEX 31 LP-72 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=23±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=28±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=24±9 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00667.cif Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3784.51 C161H269N43O53 CDFGHMPSTW E 5 7 9 -2 3 9 -140 -9683 100 hour >20 hour >10 hour 91.29 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00668 VEELEKKIEELLKKAEEQQKKNEEELKKLEX 31 LP-73 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=33±6 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=19±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=42±2 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00668.cif Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3794.54 C161H275N41O55 CDFGHMPRSTWY E 4.88 8 11 -3 1 8 -163.55 -10166 100 hour >20 hour >10 hour 88.06 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00669 WEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEX 38 LP-74 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=110±10 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=59±11 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=59±32 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00669.cif Linear Acetylation Amidation The 'X' at position 38 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4862.7 C213H340N52O69 ACDFGHMPRV E 4.98 10 13 -3 4 8 -196.58 -13368 2.8 hour 3 min 2 min 61.58 12490 337.57 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00670 EMTWEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEX 41 LP-75 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=100±22 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=65±8 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=86±26 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00670.cif Linear Acetylation Amidation The 'X' at position 41 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 5224.11 C227H363N55O75S ACDFGHPRV E 4.85 10 14 -4 5 8 -187.8 -14071 1 hour 30 min >10 hour 57.07 12490 312.25 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00671 WQEWEQKITALLEQAQIQQEKNEYELQKLDKX 32 LP-46 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=88±4 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=50±8 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=44±7 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00671.cif Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid). L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4000.66 C174H269N45O55 CFGHMPRSV Q 4.55 4 7 -3 3 10 -137.81 -8211 2.8 hour 3 min 2 min 79.38 12490 402.9 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00672 WEQKITALLEQAQIQQEKNEYELQKLDKX 29 LP-48 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=83±9 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=47±6 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=37±4 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00672.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid). L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3557.2 C153H244N40O49 CFGHMPRSV Q 4.72 4 6 -2 3 9 -124.83 -7209 2.8 hour 3 min 2 min 87.59 6990 249.64 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00673 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELLX 35 C34-C16 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=247±28 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=65±25 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=109±13 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00673.cif Linear Acetylation Amidation The 'X' at position 35 is Lys-C16(palmitic acid). L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4359.93 C184H278N50O63S ACFGPV E 4.21 3 8 -5 9 9 -123.43 -10170 2.8 hour 3 min 2 min 78 12490 367.35 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00674 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELLGSGX 38 C34-Chol Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=316±62 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24±2 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=37±5 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00674.cif Linear Acetylation Amidation The 'X' at position 38 is Cys-Chol(cholesterol) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4561.12 C191H289N53O67S ACFPV E 4.21 3 8 -5 12 9 -117.89 -10322 2.8 hour 3 min 2 min 71.84 12490 337.57 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00675 YTSLIHSLIEESQNQQEKNEQELLELDK 28 P-40 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>2000 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>2000 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>2000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00675 DRAVPe00675.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3359.65 C144H232N38O54 ACFGMPRVW E 4.3 3 7 -4 7 7 -117.5 -7925 2.8 hour 10 min 2 min 97.5 1490 55.19 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 DRAVPa0419 Anti-HIV DRAVPe00676 YTSLIEELIKKSEEQQKKNEEELKKLEK 28 P-50 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=35.6±1.3 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=191.1±57.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=21.8±3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00676 DRAVPe00676.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3435.92 C151H256N38O52 ACDFGHMPRVW E 5.3 7 8 -1 5 6 -161.43 -9104 2.8 hour 10 min 2 min 83.57 1490 55.19 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00677 LEANIEELLKKAEEQQKKNEEELKKLEK 28 P-51 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=10.2±0.7 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24.9±2.9 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=45.4±10.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00677 DRAVPe00677.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3382.86 C147H253N39O51 CDFGHMPRSTVWY E 5 7 9 -2 2 8 -163.21 -9136 5.5 hour 3 min 2 min 90.71 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00678 WEQKIEELLKKAEEQQKKNEEELKKLEK 28 P-52 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=1.9±0.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1.9±0.4 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=20541 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=916.6 ±42.46 μM;##MT-4 cell:CC50=770.63±131.46 μM;##HEK293T cell:CC50=649.07± 37.03μM;##PBMC:CC50=91.19± 20.46 μM. DRAVPe00678 DRAVPe00678.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3527.03 C156H261N41O51 CDFGHMPRSTVY E 5.36 8 9 -1 1 7 -200.36 -10021 2.8 hour 3 min 2 min 73.21 5500 203.7 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00679 YTSLIEELIKKSEEQQKKNEEELKK 25 P-54 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00679 DRAVPe00679.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3065.47 C134H226N34O47 ACDFGHMPRVW E 5.24 6 7 -1 5 5 -166.4 -8360 2.8 hour 10 min 2 min 78 1490 62.08 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00680 WEQKIEELLKKAEEQQKKNEEELKK 25 P-55 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14.2±1.8 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=16.9±2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=32.3±9.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00680 DRAVPe00680.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3156.58 C139H231N37O46 CDFGHMPRSTVY E 5.3 7 8 -1 1 6 -210 -9277 2.8 hour 3 min 2 min 66.4 5500 229.17 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00681 WEQKIEELLKKAEEQQKKNEEEK 23 P-57 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00681 DRAVPe00681.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2915.25 C127H208N34O44 CDFGHMPRSTVY E 4.94 6 8 -2 1 5 -227.83 -9214 2.8 hour 3 min 2 min 55.22 5500 250 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00682 WEQKIEELLKKAEEQQKKNEK 21 P-58 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00682 DRAVPe00682.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2657.02 C117H194N32O38 CDFGHMPRSTVY EK 6.38 6 6 0 1 5 -216.19 -7852 2.8 hour 3 min 2 min 60.48 5500 275 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00683 WEQKIEELLKKAEEQQKK 18 P-59 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00683 DRAVPe00683.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2285.63 C102H169N27O32 CDFGHMNPRSTVY EK 6.34 5 5 0 0 5 -191.67 -5952 2.8 hour 3 min 2 min 70.56 5500 323.53 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00684 SLIEELIKKSEEQQKKNEEELKKLEK 26 P-60 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=591.4±65.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00684 DRAVPe00684.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3171.64 C138H240N36O48 ACDFGHMPRTVWY E 5.29 7 8 -1 3 6 -166.15 -8833 1.9 hour >20 hour >10 hour 90 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00685 EQKIEELLKKAEEQQKKNEEELKKLEK 27 P-62 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=25.3±2.6 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=44.2±2.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=22.1±3.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00685 DRAVPe00685.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3340.82 C145H251N39O50 CDFGHMPRSTVWY E 5.36 8 9 -1 1 6 -204.44 -10254 1 hour 30 min >10 hour 75.93 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00686 QKIEELLKKAEEQQKKNEEELKKLEK 26 P-63 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=16.1±2.5 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24±2.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=24.4±2.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00686 DRAVPe00686.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3211.7 C140H244N38O47 CDFGHMPRSTVWY EK 6.44 8 8 0 1 6 -198.85 -9573 0.8 hour 10 min >10 hour 78.85 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00687 KIEELLKKAEEQQKKNEEELKKLEK 25 P-64 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=7.6±1.3 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.3±0.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=10.4±2.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00687 DRAVPe00687.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3083.57 C135H236N36O45 CDFGHMPRSTVWY EK 6.44 8 8 0 1 6 -192.8 -9019 1.3 hour 3 min 2 min 82 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00688 IEELLKKAEEQQKKNEEELKKLEK 24 P-65 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=17.9±2.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=25.7±1.3 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=25.8±1.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00688 DRAVPe00688.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2955.4 C129H224N34O44 CDFGHMPRSTVWY E 5.3 7 8 -1 1 6 -184.58 -8464 20 hour 30 min >10 hour 85.42 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00689 IEELLKKAEEQQKKNEEELKK 21 P-69 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>7508 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00689 DRAVPe00689.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 2584.95 C112H194N30O39 CDFGHMPRSTVWY E 5.24 6 7 -1 1 5 -193.81 -7720 20 hour 30 min >10 hour 79.05 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00690 INNYTSLIEELIKKSEEQQKKNEEELKKLEK 31 P-70 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=8.5±0.5 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=36.5±6.4 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=49.7±5.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00690 DRAVPe00690.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3777.28 C165H279N43O57 ACDFGHMPRVW E 5.3 7 8 -1 7 7 -153.87 -9940 20 hour 30 min >10 hour 88.06 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00691 IEEYTKKIEEILKKSEEQQKKNEEELKKLEK 31 P-71 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.1±0.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.1±3.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=38.7±7.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00691 DRAVPe00691.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3863.42 C170H289N43O58 ACDFGHMPRVW E 5.41 9 10 -1 4 6 -188.71 -11236 20 hour 30 min >10 hour 75.48 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00692 VRYLEANIEELLKKAEEQQKKNEEELKKLEK 31 P-72 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=4.1±0.9 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=16.2±3.4 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=15.9±1.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00692 DRAVPe00692.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3801.35 C167H283N45O55 CDFGHMPSTW E 5.36 8 9 -1 3 9 -152.58 -10238 100 hour >20 hour >10 hour 91.29 1490 49.67 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00693 VEELEKKIEELLKKAEEQQKKNEEELKKLEK 31 P-73 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2±0.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=5.6±0.7 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=8.2±1.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00693 DRAVPe00693.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3811.39 C167H289N43O57 CDFGHMPRSTWY E 5.11 9 11 -2 1 8 -176.13 -10721 100 hour >20 hour >10 hour 88.06 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00694 WEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEK 38 P-74 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.4±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=0.8±0.1 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1.4±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00694 DRAVPe00694.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 4879.54 C219H354N54O71 ACDFGHMPRV E 5.19 11 13 -2 4 8 -206.84 -13923 2.8 hour 3 min 2 min 61.58 12490 337.57 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00695 EMTWEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEK 41 P-75 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.4±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=0.9±0.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=0.6±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00695 DRAVPe00695.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 5240.95 C233H377N57O77S ACDFGHPRV E 5.02 11 14 -3 5 8 -197.32 -14626 1 hour 30 min >10 hour 57.07 12490 312.25 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00696 ILPWKWPWWPWRR 13 Indolicidin (Cathelicidin-4) Bos taurus (Bovine) P33046##A3KN14 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 1G8C##1G89 "HSV,HIV" "Herpesviridae, Retroviridae" HIV-1 integrase inhibition assay [Ref.15081088]Herpes simplex virus type 1 (HSV-1):inhibition of HSV-1 infection in Vero cells(EC50=28.68 μM);##Herpes simplex virus type 2 (HSV-2):inhibition of HSV-2 infection in Vero cells(EC50=5.00 μM).##[Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=60 µM);inhibition of strand transfer catalyzed by integrase(IC50=57 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15081088]Vero cells:CC50>100 μM. DRAVPe00696 DRAVPe00696.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1907.3 C100H131N25O14 ACDEFGHMNQSTVY W 12.01 3 0 3 0 7 -106.92 -1390 20 hour 30 min >10 hour 60 27500 2291.67 15081088##15482931  Int J Antimicrob Agents. 2004 Apr;23(4):382-9.##Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Albiol Matanic VC, Castilla V.##Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus.##Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.ijantimicag.2003.07.022##10.1016/j.bmcl.2004.08.061 "Anti-HSV,Anti-HIV" DRAVPe00697 ILPWKWPWWPWPP 13 Indolicidin [R12P][R13P] Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=16 µM);inhibition of strand transfer catalyzed by integrase(IC50=13 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00697 DRAVPe00697.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1789.16 C98H121N19O14 ACDEFGHMNQRSTVY PW 8.75 1 0 1 0 7 -62.31 1594 20 hour 30 min >10 hour 60 27500 2291.67 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00698 LPWKWPWWPWPP 12 Indolicidin (2-13)[R12P][R13P] Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=185 µM);inhibition of strand transfer catalyzed by integrase(IC50=215 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00698 DRAVPe00698.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1676 C92H110N18O13 ACDEFGHIMNQRSTVY PW 8.75 1 0 1 0 6 -105 1102 5.5 hour 3 min 2 min 32.5 27500 2500 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00699 ILPWKWPWWPWP 12 Indolicidin (1-12)[R12P] Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=180 µM);inhibition of strand transfer catalyzed by integrase(IC50=80 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00699 DRAVPe00699.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1692.04 C93H114N18O13 ACDEFGHMNQRSTVY W 8.75 1 0 1 0 7 -54.17 1594 20 hour 30 min >10 hour 65 27500 2500 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00700 ILPWGWPWWPWPP 13 Indolicidin [K5G;R12P;R13P] Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00700 DRAVPe00700.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1718.04 C94H112N18O14 ACDEFHKMNQRSTVY PW 5.52 0 0 0 1 7 -35.38 2243 20 hour 30 min >10 hour 60 27500 2291.67 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00701 ILPWGWPWWPWRR 13 Indolicidin [K5G] Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=49 µM);inhibition of strand transfer catalyzed by integrase(IC50=19 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00701 DRAVPe00701.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1836.18 C96H122N24O14 ACDEFHKMNQSTVY W 12 2 0 2 1 7 -80 -741 20 hour 30 min >10 hour 60 27500 2291.67 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00702 ILAWKWAWWAWPP 13 "Indolicidin [P3,7,10A,R12,13P]" Synthetic construct(derived from Indolicidin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 integrase inhibition assay [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=54 µM);inhibition of strand transfer catalyzed by integrase(IC50=41 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00702 DRAVPe00702.cif Linear Free Amidtion None L HIV Integrase The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. 1711.04 C92H115N19O14 CDEFGHMNQRSTVY W 8.75 1 0 1 0 10 16.15 2137 20 hour 30 min >10 hour 83.08 27500 2291.67 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. "Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP. " Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. 10.1016/j.bmcl.2004.08.061 Anti-HIV DRAVPe00703 LLEYSI 6 peptide 1 from hydrolysate of oyster Crassostrea gigas(hydrolysate of oyster) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=20 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00703 DRAVPe00703.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 736.86 C35H56N6O11 ACDFGHKMNPQRTVW L 4 0 1 -1 2 3 108.33 441 5.5 hour 3 min 2 min 195 1490 298 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00704 LLEYSL 6 peptide 2 from hydrolysate of oyster Crassostrea gigas(hydrolysate of oyster) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=15 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00704 DRAVPe00704.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 736.86 C35H56N6O11 ACDFGHIKMNPQRTVW L 4 0 1 -1 2 3 96.67 441 5.5 hour 3 min 2 min 195 1490 298 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00705 LLEYS 5 peptide derived from hydrolysate of oyster Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=120 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00705 DRAVPe00705.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 623.7 C29H45N5O10 ACDFGHIKMNPQRTVW L 4 0 1 -1 2 2 40 -51 5.5 hour 3 min 2 min 156 1490 372.5 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00706 LEYSI 5 peptide derived from hydrolysate of oyster Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=550 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00706 DRAVPe00706.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 623.7 C29H45N5O10 ACDFGHKMNPQRTVW EILSY 4 0 1 -1 2 2 54 -51 5.5 hour 3 min 2 min 156 1490 372.5 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00707 LLEY 4 peptide derived from hydrolysate of oyster Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=5100 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00707 DRAVPe00707.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 536.63 C26H40N4O8 ACDFGHIKMNPQRSTVW L 4 0 1 -1 1 2 70 289 5.5 hour 3 min 2 min 195 1490 496.67 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00708 LEYS 4 peptide derived from hydrolysate of oyster Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1 protease inhibition assay [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=4800 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00708 DRAVPe00708.cif Linear Free Free None L HIV-1 protease "The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity." 510.54 C23H34N4O9 ACDFGHIKMNPQRTVW ELSY 4 0 1 -1 2 1 -45 -543 5.5 hour 3 min 2 min 97.5 1490 496.67 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. "Lee TG, Maruyama S. " Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. 10.1006/bbrc.1998.9824 Anti-HIV DRAVPe00709 FVFLM 5 FM5 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00709 DRAVPe00709.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 655.85 C34H49N5O6S ACDEGHIKNPQRSTWY F 5.52 0 0 0 0 4 310 1727 1.1 hour 3 min 2 min 136 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00710 PFVFLM 6 PM6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00710 DRAVPe00710.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 752.97 C39H56N6O7S ACDEGHIKNQRSTWY F 5.96 0 0 0 0 4 231.67 1727 >20 hour >20 hour ? 113.33 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00711 KPFVFLM 7 KM7 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00711 DRAVPe00711.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 881.14 C45H68N8O8S ACDEGHINQRSTWY F 8.75 1 0 1 0 4 142.86 1172 1.3 hour 3 min 2 min 97.14 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00712 NKPFVFLM 8 NM8 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00712 DRAVPe00712.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 995.25 C49H74N10O10S ACDEGHIQRSTWY F 8.75 1 0 1 1 4 81.25 508 1.4 hour 3 min >10 hour 85 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00713 PFVYLI 6 PI6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00713 DRAVPe00713.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 750.94 C40H58N6O8 ACDEGHKMNQRSTW FILPVY 5.95 0 0 0 1 4 206.67 1672 >20 hour >20 hour ? 178.33 1490 298 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00714 PFVFLE 6 PE6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00714 DRAVPe00714.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 750.89 C39H54N6O9 ACDGHIKMNQRSTWY F 4 0 1 -1 0 4 141.67 811 >20 hour >20 hour ? 113.33 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00715 EFVFLM 6 EM6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00715 DRAVPe00715.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 784.97 C39H56N6O9S ACDGHIKNPQRSTWY F 4 0 1 -1 0 4 200 1046 1 hour 30 min >10 hour 113.33 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00716 PEVFLM 6 PEM6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00716 DRAVPe00716.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 734.91 C35H54N6O9S ACDGHIKNQRSTWY EFLMPV 4 0 1 -1 0 3 126.67 748 >20 hour >20 hour ? 113.33 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00717 PFVFLR 6 PR6 Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00717 DRAVPe00717.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 777.96 C40H59N9O7 ACDEGHIKMNQSTWY F 10.18 1 0 1 0 4 125 0 >20 hour >20 hour ? 113.33 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00718 CPFVFLM 7 CPM Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=8.96 ± 2.23 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells between H9/HIV-1IIIB cells and MT-2 cells(IC50=67.20 ± 4.05 μM);##HIV-1:inhibition of pseudovirus infection(IC50=5.95 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22406118]MT-2 cells:CC50>200 μM. DRAVPe00718 DRAVPe00718.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) None L Not found The cyclic peptide inhibited HIV-1 infection by blocking virus fusion with and entry into the target cells. 856.11 C42H61N7O8S2 ADEGHIKNQRSTWY F 5.52 0 0 0 1 4 234.29 1855 1.2 hour >20 hour >10 hour 97.14 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00719 CPFVFLE 7 CPE Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=55.84 ± 3.31μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50=115.58 ± 6.28 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22406118]MT-2 cells:CC50>200 μM. DRAVPe00719 DRAVPe00719.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) None L Not found The cyclic peptide inhibited HIV-1 infection by blocking virus fusion with and entry into the target cells. 854.03 C42H59N7O10S ADGHIKMNQRSTWY F 4 0 1 -1 1 4 157.14 939 1.2 hour >20 hour >10 hour 97.14 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00720 CPFVFLR 7 CPR Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=74.07± 22.84 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50=73.98 ± 7.44 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22406118]MT-2 cells:CC50>200 μM. DRAVPe00720 DRAVPe00720.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) None L Not found The cyclic peptide inhibited HIV-1 infection by blocking virus fusion with and entry into the target cells. 881.1 C43H64N10O8S ADEGHIKMNQSTWY F 8.25 1 0 1 1 4 142.86 128 1.2 hour >20 hour >10 hour 97.14 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00721 CPEVFLM 7 CPEM Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22406118]MT-2 cells:CC50>200 μM. DRAVPe00721 DRAVPe00721.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) None L Not found The cyclic peptide inhibited HIV-1 infection by blocking virus fusion with and entry into the target cells. 838.05 C38H59N7O10S2 ADGHIKNQRSTWY CEFLMPV 4 0 1 -1 1 3 144.29 876 1.2 hour >20 hour >10 hour 97.14 0 0 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  "Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K." Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. 10.1016/j.bmcl.2012.02.037 Anti-HIV DRAVPe00722 IWNHGNITLGEWYNQTKDLQQKFYEIIMDIEQNNV 35 T1562(FIV envelope protein (724-758)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.318 μM,EC90=1.236 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00722 DRAVPe00722.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4296.78 C194H288N50O59S ACPRS IN 4.5 3 5 -2 11 11 -78.86 -6406 20 hour 30 min >10 hour 86.29 13980 411.18 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00723 WNHGNITLGEWYNQTKDLQQKFYEIIMDIEQNNVQ 35 T1568(FIV envelope protein (725-759)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.259 μM,EC90=0.971 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00723 DRAVPe00723.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4311.75 C193H285N51O60S ACPRS NQ 4.5 3 5 -2 11 10 -101.71 -7452 2.8 hour 3 min 2 min 75.14 13980 411.18 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00724 GNITLGEWYNQTKDLQQKFYEIIMDIEQNNVQG 33 T1967(FIV envelope protein (728-760)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=2.454 μM,EC90>2.518 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50=2.053 μM,EC90>2.518 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00724 DRAVPe00724.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3931.35 C174H265N45O57S ACHPRS Q 4.18 2 5 -3 11 9 -86.06 -6461 30 hour >20 hour >10 hour 79.7 8480 265 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00725 NITLGEWYNQTKDLQQKFYEIIMDIEQNNVQGK 33 T1968(FIV envelope protein (729-761)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.586 μM,EC90=2.067 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.473 μM,EC90>2.473 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00725 DRAVPe00725.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4002.47 C178H274N46O57S ACHPRS Q 4.51 3 5 -2 10 9 -96.67 -7110 1.4 hour 3 min >10 hour 79.7 8480 265 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00726 ITLGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGI 35 T1569(FIV envelope protein (730-764)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.026 μM,EC90=0.117 μM);inhibition of virus infection in FCD4-E cells(EC50=0.055 μM,EC90=0.106 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.356 μM,EC90>2.356 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00726 DRAVPe00726.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4186.75 C188H294N48O58S ACHPRS IQ 4.94 4 5 -1 10 10 -80.57 -6415 20 hour 30 min >10 hour 86.29 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00727 TLGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKG 33 T1969(FIV envelope protein (731-763)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.435 μM,EC90=1.413 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00727 DRAVPe00727.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3960.43 C176H272N46O56S ACHPRS Q 4.93 4 5 -1 10 8 -112.73 -7399 7.2 hour >20 hour >10 hour 67.88 8480 265 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00728 LGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQ 35 T1577(FIV envelope protein (732-766)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.050 μM,EC90=0.162 μM);inhibition of virus infection in FCD4-E cells(EC50=0.098 μM,EC90=0.177 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50=1.933 μM,EC90>2.342 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00728 DRAVPe00728.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4228.75 C188H292N50O59S ACHPRS Q 4.94 4 5 -1 9 9 -111.43 -7758 5.5 hour 3 min 2 min 75.14 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00729 GEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQL 35 T1971(FIV envelope protein (733-767)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.012 μM,EC90=0.033 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.342 μM,EC90>2.342 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.12186891]No cytotoxic effects against HeLa cells at the concentration of 23 μM. DRAVPe00729 DRAVPe00729.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4228.75 C188H292N50O59S ACHPRS Q 4.94 4 5 -1 9 9 -111.43 -7758 30 hour >20 hour >10 hour 75.14 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00730 EWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQ 35 T1972(FIV envelope protein (734-768)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.012 μM,EC90=0.054 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.304 μM,EC90>2.304 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.12186891]No cytotoxic effects against HeLa cells at the concentration of 23 μM. DRAVPe00730 DRAVPe00730.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4299.82 C191H297N51O60S ACHPRS Q 4.94 4 5 -1 8 9 -120.29 -8406 1 hour 30 min >10 hour 75.14 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00731 WYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQK 35 T1578(FIV envelope protein (735-769)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.020 μM,EC90=0.090 μM);inhibition of virus infection in FCD4-E cells(EC50=0.053 μM,EC90=0.157 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00731 DRAVPe00731.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4298.88 C192H302N52O58S ACHPRS Q 8.3 5 4 1 8 9 -121.43 -8280 2.8 hour 3 min 2 min 75.14 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00732 YNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKW 35 T1588(FIV envelope protein (736-770)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.030 μM,EC90=0.125 μM);inhibition of virus infection in FCD4-E cells(EC50=0.168 μM,EC90=0.4236 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00732 DRAVPe00732.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4298.88 C192H302N52O58S ACHPRS Q 8.3 5 4 1 8 9 -121.43 -8280 2.8 hour 10 min 2 min 75.14 8480 249.41 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00733 NQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWE 35 T1988(FIV envelope protein (737-771)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=1.990 μM,EC90>2.322 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.322 μM,EC90>2.322 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00733 DRAVPe00733.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4264.82 C188H300N52O59S ACHPRS Q 6.28 5 5 0 7 9 -127.71 -8947 1.4 hour 3 min >10 hour 75.14 6990 205.59 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00734 QTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWED 35 T1989(FIV envelope protein (738-772)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50>2.321 μM,EC90>2.321 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00734 DRAVPe00734.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4265.81 C188H299N51O60S ACHPRS Q 5 5 6 -1 6 9 -127.71 -9155 0.8 hour 10 min >10 hour 75.14 6990 205.59 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00735 TKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWEDW 35 T1589(FIV envelope protein (739-773)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "FIV,HIV" Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=1.145 μM,EC90>2.290 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.321 μM,EC90>2.321 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00735 DRAVPe00735.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4323.89 C194H301N51O59S ACHPRS Q 4.99 5 6 -1 6 10 -120.29 -8368 7.2 hour >20 hour >10 hour 75.14 12490 367.35 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 "Anti-FIV,Anti-HIV" DRAVPe00736 FYEIIMDIEQNNVQGKKGIQQLQKWEDWVGWIGNI 35 T1566(FIV envelope protein (746-780)) Synthetic construct(derived from FIV envelope protein) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae "plaque-forming assay,RT infectivity assay" "[Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50>2.346 μM,EC90>2.346 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00736 DRAVPe00736.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4221.8 C194H291N49O55S ACHPRST I 4.51 3 5 -2 8 13 -54 -4368 1.1 hour 3 min 2 min 94.57 17990 529.12 12186891 J Virol. 2002 Sep;76(18):9079-86. "Medinas RJ, Lambert DM, Tompkins WA." C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  10.1128/jvi.76.18.9079-9086.2002 Anti-FIV DRAVPe00737 XTWXEWDREINNYTSLIHSLIEESQNQQEKNEQELLE 37 T649v Synthetic construct P04582 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae luciferase assay [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.9±0.4 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50>3000 nM);##HIV-1 V38A/N42T:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=15.8±1.9 nM);##HIV-1 V38E/N42S:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=44.4±6.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00737.cif Cyclic Free Free The 'X' at position 1 indicates Norleucine. L Not found The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. 4570.29 C188H281N51O66 ACFGMPV E 4.14 3 9 -6 10 9 -133.24 -11343 73.78 12490 346.94 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. "Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. " Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. 10.1073/pnas.1002713107 Anti-HIV DRAVPe00738 XTWXEWDXEINNYTSLIHSLIEESQNQQEKNEQELLE 37 SAH-gp41(626-662)A Synthetic construct P04582 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae luciferase assay [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.1±0.3 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=339±162 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00738.cif Cyclic Free Free "The 'X' at position 1 indicates Norleucine,the 'X' at position 4,8 indicates S-2-(4'-pentenyl) alanine. X(4) and X (5) are cross-linked by hydrocarbon stapling." L Not found The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. 4525.44 C182H267N47O64 ACFGMPRV E 3.93 2 9 -7 10 9 -121.08 -9851 73.78 12490 346.94 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. "Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. " Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. 10.1073/pnas.1002713107 Anti-HIV DRAVPe00739 XTWMEWDREINNYTSLIHSLIEESQNQXEKNXQELLE 37 SAH-gp41(626-662) B Synthetic construct P04582 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae luciferase assay [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=4.5±1.4 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=1958±259 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00739.cif Cyclic Free Free "The 'X' at position 1 indicates Norleucine,the 'X' at position 28,32 indicates S-2-(4'-pentenyl) alanine. X(28) and X (32) are cross-linked by hydrocarbon stapling." L Not found The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. 4555.57 C183H273N49O61S ACFGPV E 4.21 3 8 -5 10 9 -109.19 -9873 73.78 12490 346.94 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. "Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. " Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. 10.1073/pnas.1002713107 Anti-HIV DRAVPe00740 XTWXEWDXEINNYTSLIHSLIEESQNQXEKNXQELLE 37 "SAH-gp41(626-662) A,B" Synthetic construct P04582 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae luciferase assay [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.5±0.2 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=87±30 nM);##HIV-1 V38A/N42T:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=10.7±2.2 nM);##HIV-1 V38E/N42S:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=16.1±3.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00740.cif Cyclic Free Free "The 'X' at position 1 indicates Norleucine,the 'X' at position 4,8.28,32 indicates S-2-(4'-pentenyl) alanine. X(4) and X (5), X(28) and X (32) are cross-linked by hydrocarbon stapling." L Not found The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. 4490.85 C172H248N44O57 ACFGMPRV E 3.99 2 8 -6 10 9 -102.16 -8616 73.78 12490 346.94 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. "Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. " Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. 10.1073/pnas.1002713107 Anti-HIV DRAVPe00741 AEEASKKAEEASKKAEEASKKAEEASKKAEEASKKXX 37 AAS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=4.47±1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=2.38±0.9 μM. No predicted structure available DRAVPe00741.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 3959.75 C155H263N45O59 CDFGHILMNPQRTVWY AEK 6.53 10 10 0 5 10 -162.16 -12250 4.4 hour >20 hour >10 hour 27.03 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00742 VEEVSKKVEEVSKKVEEVSKKVEEVSKKVEEVSKKXX 37 VVS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=74.5±6.8 μM. No predicted structure available DRAVPe00742.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4240.29 C175H303N45O59 ACDFGHILMNPQRTWY EKV 6.46 10 10 0 5 10 -97.3 -10020 100 hour >20 hour >10 hour 78.38 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00743 FEEFSKKFEEFSKKFEEFSKKFEEFSKKFEEFSKKXX 37 FFS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=3.11±0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM. No predicted structure available DRAVPe00743.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4720.73 C215H303N45O59 ACDGHILMNPQRTVWY EFK 6.49 10 10 0 5 10 -135.14 -11080 1.1 hour 3 min 2 min 0 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00744 YEEYSKKYEEYSKKYEEYSKKYEEYSKKYEEYSKKXX 37 YYS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=6.26±2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=19.8±1.6 μM. No predicted structure available DRAVPe00744.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4880.72 C215H303N45O69 ACDFGHILMNPQRTVW EKY 6.48 10 10 0 15 0 -245.95 -14200 2.8 hour 10 min 2 min 0 14900 413.89 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00745 LEELSKKLEELSKKLEELSKKLEELSKKLEELSKKXX 37 LLS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.24±0.08 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=4.04±0.4 μM. No predicted structure available DRAVPe00745.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4380.56 C185H323N45O59 ACDFGHIMNPQRTVWY EKL 6.49 10 10 0 5 10 -108.11 -9140 5.5 hour 3 min 2 min 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00746 IEEISKKIEEISKKIEEISKKIEEISKKIEEISKKXX 37 IIS Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MERS-CoV,H3N2,H1N1" "Coronaviridae, Orthomyxoviridae" MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.10±0.02 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=1.96±0.28 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=6.38±1.06 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=88.8±28 μM;##MDCK cell:CC50>100 μM. No predicted structure available DRAVPe00746.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4380.56 C185H323N45O59 ACDFGHLMNPQRTVWY EIK 6.49 10 10 0 5 10 -89.19 -9140 20 hour 30 min >10 hour 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 "Anti-MERS-CoV,Anti-H3N2,Anti-H1N1" DRAVPe00747 IEEIYKKIEEIYKKIEEIYKKIEEIYKKIEEIYKKXX 37 IIY Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MERS-CoV,H3N2,H1N1" "Coronaviridae, Orthomyxoviridae" MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.52±0.4 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=3.15±1.79 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=12.9±5.55 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM;##MDCK cell:CC50>100 μM. No predicted structure available DRAVPe00747.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4761.05 C215H343N45O59 ACDFGHLMNPQRSTVW EIK 6.48 10 10 0 5 10 -95.95 -7510 20 hour 30 min >10 hour 105.41 7450 206.94 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 "Anti-MERS-CoV,Anti-H3N2,Anti-H1N1" DRAVPe00748 IEEIWKKIEEIWKKIEEIWKKIEEIWKKIEEIWKKXX 37 IIW Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=10.6±2.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM. No predicted structure available DRAVPe00748.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4876.23 C225H348N50O54 ACDFGHLMNPQRSTVY EIK 6.49 10 10 0 0 15 -90.54 -6275 20 hour 30 min >10 hour 105.41 27500 763.89 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00749 IEEIHKKIEEIHKKIEEIHKKIEEIHKKIEEIHKKXX 37 IIH Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=1.68±0.47 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM. No predicted structure available DRAVPe00749.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4630.87 C200H333N55O54 ACDFGLMNPQRSTVWY EIK 7.16 15 10 5 0 10 -121.62 -9770 20 hour 30 min >10 hour 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00750 IEEIQKKIEEIQKKIEEIQKKIEEIQKKIEEIQKKXX 37 IIQ Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MERS-CoV,H3N2,H1N1,HIV,EboV" "Coronaviridae, Orthomyxoviridae, Filoviridae" MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.11±0.02 μM);inhibition of pseudovirus infection in Huh-7 cells(IC50=0.13±0.1 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=1.73±0.81 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=0.70±0.09 μM);##HIV-1 inhibition of cell-cell fusion in TZM-bl cells(EC50=3.63 ±0.54 μM);##Ebola virus (EboV):inhibition of pseudovirus infection in TZM-bl cells(EC50=1.02 ± 0.54 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM;##MDCK cell:CC50>100 μM;##TZM-bl cell:CC50>100 μM. No predicted structure available DRAVPe00750.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4585.82 C195H338N50O59 ACDFGHLMNPRSTVWY EIK 6.49 10 10 0 0 10 -125.68 -10210 20 hour 30 min >10 hour 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 "Anti-MERS-CoV,Anti-H3N2,Anti-H1N1,Anti-HIV,Anti-EBOV" DRAVPe00751 IEEIKKKIEEIKKKIEEIKKKIEEIKKKIEEIKKKXX 37 IIK Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.45±0.13 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50=4.54±0.6 μM. No predicted structure available DRAVPe00751.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4586.04 C200H358N50O54 ACDFGHLMNPQRSTVWY K 9.56 15 10 5 0 10 -131.08 -10215 20 hour 30 min >10 hour 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00752 IEEIEKKIEEIEKKIEEIEKKIEEIEKKIEEIEKKXX 37 IIE Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MERS-CoV Coronaviridae MERS-CoV S Protein-Mediated Cell–Cell Fusion Assay [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=2.93±0.95 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30192544]Huh-7 cell:CC50>100 μM. No predicted structure available DRAVPe00752.cif Linear Acetylation Amidation "The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid)." L membrane The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. 4590.74 C195H333N45O64 ACDFGHLMNPQRSTVWY E 4.76 10 15 -5 0 10 -125.68 -10845 20 hour 30 min >10 hour 105.41 0 0 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. "Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. " De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  10.1021/acs.jmedchem.8b00890 Anti-MERS-CoV DRAVPe00753 LWGEIWNTVKGLI 13 Eval418 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Antiviral assays [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=2.48 μg/ml);inhibition of viral attachment in Vero cells(IC50=3.70 μg/ml);inhibition of viral entry in Vero cells(IC50=31.71 μg/ml). [Ref.29290802]the cell viability of erythrocytes was also more than 95% at concentrations of Eval418 of 10 μg/mL or less. [Ref.29290802]Vero cell:CC50=68.50μg/mL; the cell viability of the peptide-treated Vero cells was greater than 95% after treatment with Eval418 at 10 μg/mL. DRAVPe00753 DRAVPe00753.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1528.81 C74H113N17O18 ACDFHMPQRSY GILW 6 1 1 0 4 7 50.77 869 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV DRAVPe00754 LWGHIWNFVHGLI 13 Eval418-FH2 Synthetic construct(derived from Eval418) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Antiviral assays [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=1.50 μg/ml);inhibition of viral attachment in Vero cells(IC50=1.43 μg/ml);inhibition of viral entry in Vero cells(IC50=8.63 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cell:CC50=27.60 μg/mL. DRAVPe00754 DRAVPe00754.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1591.88 C80H110N20O15 ACDEKMPQRSTY GHILW 6.92 2 0 2 3 8 85.38 1728 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV DRAVPe00755 LWHHIWNFVHGLI 13 Eval418-FH3 Synthetic construct(derived from Eval418) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Antiviral assays [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=1.01 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.86 μg/ml);inhibition of viral entry in Vero cells(IC50=4.23 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cell:CC50=26.83 μg/mL. DRAVPe00755 DRAVPe00755.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1671.97 C84H114N22O15 ACDEKMPQRSTY H 7.02 3 0 3 2 8 63.85 1168 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV DRAVPe00756 LWHHIWNTVHHLI 13 Eval418-FH4 Synthetic construct(derived from Eval418) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Antiviral assays [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=0.87 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.63 μg/ml);inhibition of viral entry in Vero cells(IC50=4.37 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cell:CC50=27.58 μg/mL. DRAVPe00756 DRAVPe00756.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1705.99 C83H116N24O16 ACDEFGKMPQRSY H 7.1 4 0 4 2 7 15.38 53 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV DRAVPe00757 LWHHIWHTVHHLI 13 Eval418-FH5 Synthetic construct(derived from Eval418) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Antiviral assays [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=0.86 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.67 μg/ml);inhibition of viral entry in Vero cells(IC50=2.88 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cell:CC50=106.68 μg/mL. DRAVPe00757 DRAVPe00757.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1729.02 C85H117N25O15 ACDEFGKMNPQRSY H 7.16 5 0 5 1 7 17.69 251 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV DRAVPe00758 WQCLTLTHRGFVLLTITVLR 20 IN-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.18201721]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=38 µM);inhibition of strand transfer catalyzed by integrase(IC50=12 µM).##[Ref.19850483]HIV-1:inhibition of integrase catalytic activity(77% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(70% inhibition at 62.5μM);inhibition of intergration(63% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18201721]No cytotixic against HeLa cells and H9 T-lymphocyte cultured cells up to ~62.5 μM. DRAVPe00758 DRAVPe00758.cif Linear Free Free None L Integrase The peptide can inhibit integrase and thus inhibit virus replication. 2370.88 C110H180N30O26S ADEKMNPSY L 10.35 3 0 3 6 10 87 -519 2.8 hour 3 min 2 min 146 5500 289.47 18201721##19850483 J Mol Biol. 2008 Feb 29;376(4):971-82. ##Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. "Armon-Omer A, Levin A, Hayouka Z, Butz K, Hoppe-Seyler F, Loya S, Hizi A, Friedler A, Loyter A. ##Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A. " Correlation between shiftide activity and HIV-1 integrase inhibition by a peptide selected from a combinatorial library.##Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. 10.1016/j.jmb.2007.11.095##10.1016/j.bmc.2009.09.053 Anti-HIV DRAVPe00759 WQCLTLTHRG 10 IN(1-10) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(73% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(68% inhibition at 62.5μM);inhibition of intergration(64% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00759 DRAVPe00759.cif Linear Free Free None L Integrase The peptide can inhibit integrase and thus inhibit virus replication. 1214.41 C53H83N17O14S ADEFIKMNPSVY LT 8.26 2 0 2 4 3 -38 -1587 2.8 hour 3 min 2 min 78 5500 611.11 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. "Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A. " Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. 10.1016/j.bmc.2009.09.053 Anti-HIV DRAVPe00760 WFVLLTITVLR 11 IN(11-20) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(24% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(29% inhibition at 62.5μM);inhibition of intergration(23% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00760 DRAVPe00760.cif Linear Free Free None L Integrase The peptide can inhibit integrase and thus inhibit virus replication. 1360.71 C68H109N15O14 ACDEGHKMNPQSY L 9.75 1 0 1 2 8 184.55 1301 2.8 hour 3 min 2 min 194.55 5500 550 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. "Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A. " Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. 10.1016/j.bmc.2009.09.053 Anti-HIV DRAVPe00761 WQSLTLTHRG 10 IN(1-10)[C3S] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(62% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(60% inhibition at 62.5μM);inhibition of intergration(51% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00761 DRAVPe00761.cif Linear Free Free None L Integrase The peptide can inhibit integrase and thus inhibit virus replication. 1198.35 C53H83N17O15 ACDEFIKMNPVY LT 9.76 2 0 2 4 3 -71 -2055 2.8 hour 3 min 2 min 78 5500 611.11 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. "Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A. " Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. 10.1016/j.bmc.2009.09.053 Anti-HIV DRAVPe00762 VSGHGQHGVHG 11 Alloferon (3-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay "[Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=500 µM);##HHV-1 clinical strain:inhibition of virus replication in Hep-2 cells(IC50=117 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=38 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=250 µM);inhibition of virus replication in LLC-MK2 cells(IC50=93 µM)." No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 165 µM." DRAVPe00762 DRAVPe00762.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1071.12 C44H66N18O14 ACDEFIKLMNPRTWY G 7 3 0 3 5 2 -64.55 -1108 100 hour >20 hour >10 hour 52.73 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00763 SGHGQHGVHG 10 Alloferon (4-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=186 µM);inhibition of virus replication in Hep-2 cells(IC50=310 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=173 µM);inhibition of virus replication in Hep-2 cells(IC50=450 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=210 µM);inhibition of virus replication in LLC-MK2 cells(IC50=180 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 420 µM." DRAVPe00763 DRAVPe00763.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 971.99 C39H57N17O13 ACDEFIKLMNPRTWY G 6.78 3 0 3 5 1 -113 -1512 1.9 hour >20 hour >10 hour 29 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00764 GHGQHGVHG 9 Alloferon (5-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Hep-2 cells(IC50=360 µM);##HHV-1 clinical strain:inhibition of virus replication in Hep-2 cells(IC50=290 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in LLC-MK2 cells(IC50=230 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 448 µM." DRAVPe00764 DRAVPe00764.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 884.91 C36H52N16O11 ACDEFIKLMNPRSTWY G 7.02 3 0 3 4 1 -116.67 -1172 30 hour >20 hour >10 hour 32.22 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00765 HGQHGVHG 8 Alloferon (6-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=179 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=117 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=78 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=190 µM);inhibition of virus replication in LLC-MK2 cells(IC50=410 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 468 µM." DRAVPe00765 DRAVPe00765.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 827.86 C34H49N15O10 ACDEFIKLMNPRSTWY GH 7.02 3 0 3 3 1 -126.25 -1266 3.5 hour 10 min >10 hour 36.25 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00766 GQHGVHG 7 Alloferon (7-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=215 µM);inhibition of virus replication in HEp-2 cells(IC50=840 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=168 µM);inhibition of virus replication in Vero cells(IC50=280 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);inhibition of virus replication in LLC-MK2 cells(IC50=190 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=870 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 775 µM." DRAVPe00766 DRAVPe00766.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 690.72 C28H42N12O9 ACDEFIKLMNPRSTWY G 6.92 2 0 2 3 1 -98.57 -800 30 hour >20 hour >10 hour 41.43 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00767 QHGVHG 6 Alloferon (8-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=1300 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=950 µM);inhibition of virus replication in Hep-2 cells(IC50=280 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=500 µM);inhibition of virus replication in LLC-MK2 cells(IC50=210 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 380 µM." DRAVPe00767 DRAVPe00767.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 633.66 C26H39N11O8 ACDEFIKLMNPRSTWY GH 6.92 2 0 2 2 1 -108.33 -894 0.8 hour 10 min >10 hour 48.33 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00768 HGVHG 5 Alloferon (9-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=300 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=400 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=350 µM);inhibition of virus replication in LLC-MK2 cells(IC50=290 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=350 µM);inhibition of virus replication in LLC-MK2 cells(IC50=180 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 826 µM." DRAVPe00768 DRAVPe00768.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 505.53 C21H31N9O6 ACDEFIKLMNPQRSTWY GH 6.92 2 0 2 2 1 -60 -340 3.5 hour 10 min >10 hour 58 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00769 GVHG 4 Alloferon (10-13) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Herpesvirus,Coxsackie virus" "Herpesviridae, Picornaviridae" antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=500 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=1500 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=1040 µM);inhibition of virus replication in LLC-MK2 cells(IC50=540 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 1174 µM." DRAVPe00769 DRAVPe00769.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 368.39 C15H24N6O5 ACDEFIKLMNPQRSTWY G 6.74 1 0 1 2 1 5 126 30 hour >20 hour >10 hour 72.5 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 "Anti-Herpesvirus,Anti-Coxsackie virus" DRAVPe00770 HGVSGHGQHGV 11 Alloferon (1-11) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=178 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 260 µM. DRAVPe00770 DRAVPe00770.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1071.12 C44H66N18O14 ACDEFIKLMNPRTWY G 7.02 3 0 3 5 2 -64.55 -1108 3.5 hour 10 min >10 hour 52.73 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00771 HGVSGHGQHG 10 Alloferon (1-10) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=520 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 350 µM. DRAVPe00771 DRAVPe00771.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 971.99 C39H57N17O13 ACDEFIKLMNPRTWY G 7.02 3 0 3 5 1 -113 -1512 3.5 hour 10 min >10 hour 29 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00772 HGVSGHGQ 8 Alloferon (1-8) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=310 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 447 µM. DRAVPe00772 DRAVPe00772.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 777.79 C31H47N13O11 ACDEFIKLMNPRTWY G 6.92 2 0 2 4 1 -96.25 -1140 3.5 hour 10 min >10 hour 36.25 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00773 HGVSGHG 7 Alloferon (1-7) Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=550 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 504 µM. DRAVPe00773 DRAVPe00773.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 649.66 C26H39N11O9 ACDEFIKLMNPQRTWY G 6.92 2 0 2 4 1 -60 -586 3.5 hour 10 min >10 hour 41.43 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00774 FGVSGHGQHGVHG 13 Alloferon [H1F] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=160 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 290 µM. DRAVPe00774 DRAVPe00774.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1275.35 C55H78N20O16 ACDEIKLMNPRTWY G 7.02 3 0 3 6 3 -36.15 -716 1.1 hour 3 min 2 min 44.62 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00775 YGVSGHGQHGVHG 13 Alloferon [H1Y] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 315 µM. DRAVPe00775 DRAVPe00775.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1291.35 C55H78N20O17 ACDEFIKLMNPRTW G 7.02 3 0 3 7 2 -67.69 -1028 2.8 hour 10 min 2 min 44.62 1490 124.17 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00776 WGVSGHGQHGVHG 13 Alloferon [H1W] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 282 µM. DRAVPe00776 DRAVPe00776.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1314.39 C57H79N21O16 ACDEFIKLMNPRTY G 7.02 3 0 3 6 3 -64.62 -781 2.8 hour 3 min 2 min 44.62 5500 458.33 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00777 XGVSGHGQHGVHG 13 Alloferon [H1Phg] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 350 µM. No predicted structure available DRAVPe00777.cif Linear Free Free The 'X' at position 1 indicates Phenylglycine. L Not found No machanism information found in the reference(s) presented in this entry 1239.5 C46H67N19O14 ACDEFIKLMNPRTWY G 7.02 3 0 3 6 2 -57.69 -1014 44.62 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00778 XGVSGHGQHGVHG 13 Alloferon [H1Phe(p-Cl)] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=110 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 255 µM. No predicted structure available DRAVPe00778.cif Linear Free Free The 'X' at position 1 indicates 4-Chloro-phenylalanine. L Not found No machanism information found in the reference(s) presented in this entry 1239.5 C46H67N19O14 ACDEFIKLMNPRTWY G 7.02 3 0 3 6 2 -57.69 -1014 44.62 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00779 XGVSGHGQHGVHG 13 Alloferon [H1Phe(p-OME)] Synthetic construct(derived from Alloferon-1) P83412 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Herpesvirus Herpesviridae antiviral assay [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=220 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22883213]No cytotoxic against Vero cells up to 312 µM. No predicted structure available DRAVPe00779.cif Linear Free Free The 'X' at position 1 indicates 4-Methoxy-phenylalanine. L Not found No machanism information found in the reference(s) presented in this entry 1239.5 C46H67N19O14 ACDEFIKLMNPRTWY G 7.02 3 0 3 6 2 -57.69 -1014 44.62 0 0 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. "Kuczer M, Majewska A, Zahorska R. " New alloferon analogues: synthesis and antiviral properties. 10.1111/cbdd.12020 Anti-Herpesvirus DRAVPe00780 EMTWEEWEKKIEEYTKKIEEILXX 24 LP-11 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=931±68 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=201±41 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=253±40 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00780.cif Linear Acetylation Amidation "The 'X' at position 24 is Lys-C16(palmitic acid),The 'X' at position 23 is Lys-PEG8." L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3107.94 C132H198N28O40S ACDFGHNPQRSV E 4.47 4 8 -4 3 6 -120.42 -5527 1 hour 30 min >10 hour 65 12490 543.04 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00781 EMTWEEWEKKVEELEKKIEELLXX 24 LP-19 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=296±45 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=95±18 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=92±11 pM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00781.cif Linear Acetylation Amidation "The 'X' at position 24 is Lys-C16(palmitic acid),The 'X' at position 23 is Lys-PEG8." L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3071.91 C129H198N28O40S ACDFGHNPQRSY E 4.38 4 9 -5 1 7 -115 -5533 1 hour 30 min >10 hour 77.08 11000 478.26 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00782 YTSLIHSLIEESQNQQEKNEQELLELDX 28 LP-40 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae "cell-fusion assay,single-cycle infection assay" [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=361±60 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=392±73 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=384±33 pM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=800.8 ± 62.29 μM;##MT-4 cell:CC50=366.3± 119.08 μM;##HEK293T cell:CC50=408± 40.1μM;##PBMC:CC50=212.6± 25.71 μM. No predicted structure available DRAVPe00782.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3342.8 C138H218N36O52 ACFGMPRVW E 4.06 2 7 -5 7 7 -103.57 -7370 2.8 hour 10 min 2 min 97.5 1490 55.19 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 Anti-HIV DRAVPe00783 YTSLIEELIKKSEEQQKKNEEELKKLEX 28 LP-50 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=7±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=23±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.06-136.12 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.09-5.81 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.06 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=106.4 ± 2.72 μM;##MT-4 cell:CC50=138.37± 6.55 μM;##HEK293T cell:CC50=166.77± 35.33μM;##PBMC:CC50=40.01± 4.63 μM. No predicted structure available DRAVPe00783.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3419.07 C145H242N36O50 ACDFGHMPRVW E 4.94 6 8 -2 5 6 -147.5 -8549 2.8 hour 10 min 2 min 83.57 1490 55.19 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 "Anti-HIV,Anti-SIV" DRAVPe00784 LEANIEELLKKAEEQQKKNEEELKKLEX 28 LP-51 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21±10 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=6±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=27±5 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.02-12.07 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.09-0.84 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.03-0.06 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=434.03±90.38 μM;##MT-4 cell:CC50=135.07±32.3 μM;##HEK293T cell:CC50=130.07± 15.27μM;##PBMC:CC50=46.83±4.65 μM. No predicted structure available DRAVPe00784.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3366.01 C141H239N37O49 CDFGHMPRSTVWY E 4.76 6 9 -3 2 8 -149.29 -8581 5.5 hour 3 min 2 min 90.71 0 0 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 "Anti-HIV,Anti-SIV" DRAVPe00785 WEQKIEELLKKAEEQQKKNEEELKKLEX 28 LP-52 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=13±1 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=4±0 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=5±1 pM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=17 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.01-1.86 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.06-0.34 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.01-0.04 nM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30089693]TZM-bl cell:CC50=112.9 ± 2.21 μM;##MT-4 cell:CC50=94.06± 4.97 μM;##HEK293T cell:CC50=88.86± 6.68μM;##PBMC:CC50=114.8± 12.68 μM. No predicted structure available DRAVPe00785.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar)" 3510.19 C150H247N39O49 CDFGHMPRSTVY E 5 7 9 -2 1 7 -186.43 -9466 2.8 hour 3 min 2 min 73.21 5500 203.7 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. "Chong H, Zhu Y, Yu D, He Y." "Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus." 10.1128/JVI.01088-18 "Anti-HIV,Anti-SIV" DRAVPe00786 WEQKIEELLKKAEEQQKKNEEELKKLEX 28 LP-80 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=2.66±0.76 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=7.12±0.28 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=13.00±4.55 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=5 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.003±0.001 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.007-4.006 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.288-0.299 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.034-0.155 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=13.4 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00786.cif Linear Acetylation Amidation The 'X' at position 28 is Lys-C18(stearic acid) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 3510.19 C150H247N39O49 CDFGHMPRSTVY E 5 7 9 -2 1 7 -186.43 -9466 2.8 hour 3 min 2 min 73.21 5500 203.7 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00787 WEQKIEELLKKAEEQQKKNEEELKKLEKX 29 LP-83 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=0.49±0.03 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=4.54±1.42 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=4.75±0.83 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=2.91 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.002±0 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.002-0.041 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.02-0.032 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.004-0.006 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=8.55 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30867304]Human PBMC:CC50=40.27 µM;##Human embryonic kidney HEK293T cells:CC50=25.31 µM;##TZM-bl cells:CC50=12.34 μM;##MT-4 cells:CC50=19.65 μM;##C8166 cells:CC50=19.19 μM;##U937 cells:CC50=9.97 μ No predicted structure available DRAVPe00787.cif Linear Acetylation Amidation The 'X' at position 29 is Cys-Chol(cholesterol) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 3638.36 C156H259N41O50 CDFGHMPRSTVY E 5.36 8 9 -1 1 7 -193.45 -10021 2.8 hour 3 min 2 min 70.69 5500 196.43 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00788 LEANIEELLKKAEEQQKKNEEELKKLEKX 29 LP-86 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=0.43±0.03 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=4.78±0.69 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=7.24±1.36 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=4.91 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.003±0 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.003-0.17 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.014-0.026 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.005-0.006 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=12.27 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00788.cif Linear Acetylation Amidation The 'X' at position 29 is Cys-Chol(cholesterol) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 3494.19 C147H251N39O50 CDFGHMPRSTVWY E 5 7 9 -2 2 8 -157.59 -9136 5.5 hour 3 min 2 min 87.59 0 0 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00789 WEQKIEELLKKAEEQQKKNEEELKX 25 LP-93 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=6.27±1.26 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=6.55±1.97 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=7.57±0.62pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.89 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.006±0.001 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.012-2.17 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=1.244-3.514 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.013-0.773 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=14.51pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00789.cif Linear Acetylation Amidation The 'X' at position 25 is Lys-Chol(cholesterol) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 3139.74 C133H217N35O44 CDFGHMPRSTVY E 4.94 6 8 -2 1 6 -194.4 -8722 2.8 hour 3 min 2 min 66.4 5500 229.17 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00790 IEELLKKAEEQQKKNEEELKKLEX 24 LP-94 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available "Chromosome:21,492 - 25,259" None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=1.75±0.23 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=5.90±1.80 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=15.69±1.97 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=6.54 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.004±0.002 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.004-2.295 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.019-0.027 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.011-0.018 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=27.36 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00790.cif Linear Acetylation Amidation The 'X' at position 24 is Lys-Chol(cholesterol) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 2938.56 C123H210N32O42 CDFGHMPRSTVWY E 4.94 6 8 -2 1 6 -168.33 -7909 20 hour 30 min >10 hour 85.42 0 0 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00791 IEELLKKAEEQQKKNEEELKX 21 LP-95 Synthetic construct P03377 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,SIV" Retroviridae "cell-fusion assay,single-cycle infection assay" "[Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=199.92±32.69 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=24.36±0.15 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=4781.17±699.33 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=148.88 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.067±0.026 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.39-408.556 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=2.857-13.512 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.556-0.862 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=29.84 pM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00791.cif Linear Acetylation Amidation The 'X' at position 21 is Lys-Chol(cholesterol) L membrane "The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities." 2568.11 C106H180N28O37 CDFGHMPRSTVWY E 4.86 5 7 -2 1 5 -175.24 -7165 20 hour 30 min >10 hour 79.05 0 0 30867304 J Virol. 2019 May 15;93(11):e02312-18. "Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y." Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. 10.1128/JVI.02312-18 "Anti-HIV,Anti-SIV" DRAVPe00792 TTWEAWDRAIAEYAARIEALIRAAQEQQEKNEAALREL 38 T2635 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI/cMAGI infectivity assay [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.007 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.018μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.025 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.015 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.021 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00792 DRAVPe00792.cif Linear Acetylation Amidation None L membrane "The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion." 4415.89 C193H305N57O62 CFGHMPSV A 4.64 5 8 -3 4 18 -67.11 -9788 7.2 hour >20 hour >10 hour 87.89 12490 337.57 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  "Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK." "Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus." 10.1073/pnas.0701478104 DRAVPa1315 Anti-HIV DRAVPe00793 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=1.5 ± 0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00793 DRAVPe00793.cif Linear Free Free None L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5060.48 C223H337N59O76 CFGMPV E 4.22 4 10 -6 10 13 -117.8 -11455 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00794 XEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 42 X- C41(C41 N teminus-PEG conjugation) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=7.2 ± 0.7 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00794.cif Linear Free Free The 'X' at position 1 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5171.81 C223H335N59O75 CFGMPV E 4.22 4 10 -6 10 13 -115 -11455 85.95 17990 438.78 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00795 XEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 42 X- C41(C41 N teminus-PEG conjugation) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=11.2± 1.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00795.cif Linear Free Free The 'X' at position 1 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5171.81 C223H335N59O75 CFGMPV E 4.22 4 10 -6 10 13 -115 -11455 85.95 17990 438.78 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00796 EWDXEINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [R4X](R4C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.1± 1.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00796.cif Linear Free Free The 'X' at position 4 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5015.62 C217H323N55O74 CFGMPRV E 4.04 3 10 -7 10 13 -106.83 -9963 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00797 EWDXEINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [R4X](R4C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=8.7± 1.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00797.cif Linear Free Free The 'X' at position 4 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5015.62 C217H323N55O74 CFGMPRV E 4.04 3 10 -7 10 13 -106.83 -9963 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00798 EWDREINNYTXLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S11X](S11C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.4± 0.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00798.cif Linear Free Free The 'X' at position 11 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00799 EWDREINNYTXLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S11X](S11C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.9± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00799.cif Linear Free Free The 'X' at position 11 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00800 EWDREINNYTSLIHXLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S15X](S15C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.1± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00800.cif Linear Free Free The 'X' at position 15 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00801 EWDREINNYTSLIHXLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S15X](S15C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.0± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00801.cif Linear Free Free The 'X' at position 15 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00802 EWDREINNYTSLIHSLIXESQNQQEKNEQELLELDKWASLW 41 C41 [E18X](E18C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.5± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00802.cif Linear Free Free The 'X' at position 18 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5042.69 C218H328N58O72 CFGMPV E 4.29 4 9 -5 10 13 -109.27 -10774 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00803 EWDREINNYTSLIHSLIXESQNQQEKNEQELLELDKWASLW 41 C41 [E18X](E18C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.9± 0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00803.cif Linear Free Free The 'X' at position 18 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5042.69 C218H328N58O72 CFGMPV E 4.29 4 9 -5 10 13 -109.27 -10774 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00804 EWDREINNYTSLIHSLIEESQXQQEKNEQELLELDKWASLW 41 C41 [N22X](N22C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.2± 0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00804.cif Linear Free Free The 'X' at position 22 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5057.7 C219H329N57O73 CFGMPV E 4.22 4 10 -6 9 13 -109.27 -10791 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00805 EWDREINNYTSLIHSLIEESQXQQEKNEQELLELDKWASLW 41 C41 [N22X](N22C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.1± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00805.cif Linear Free Free The 'X' at position 22 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5057.7 C219H329N57O73 CFGMPV E 4.22 4 10 -6 9 13 -109.27 -10791 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00806 EWDREINNYTSLIHSLIEESQNQQEKNEXELLELDKWASLW 41 C41 [Q29X](Q29C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.2± 0.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00806.cif Linear Free Free The 'X' at position 29 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5043.68 C218H327N57O73 CFGMPV E 4.22 4 10 -6 10 13 -109.27 -10901 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00807 EWDREINNYTSLIHSLIEESQNQQEKNEXELLELDKWASLW 41 C41 [Q29X](Q29C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.5± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00807.cif Linear Free Free The 'X' at position 29 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5043.68 C218H327N57O73 CFGMPV E 4.22 4 10 -6 10 13 -109.27 -10901 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00808 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWX 42 C41 -X(C41 C teminus-PEG conjugation) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=10.9± 2.2 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00808.cif Linear Free Free The 'X' at position 42 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5171.81 C223H335N59O75 CFGMPV E 4.22 4 10 -6 10 13 -115 -11455 1 hour 30 min >10 hour 85.95 17990 438.78 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00809 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWX 42 C41 -X(C41 C teminus-PEG conjugation) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=43.3± 14.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00809.cif Linear Free Free The 'X' at position 42 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5171.81 C223H335N59O75 CFGMPV E 4.22 4 10 -6 10 13 -115 -11455 1 hour 30 min >10 hour 85.95 17990 438.78 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00810 EWDREINNYTSLIHSLIEEXQNQQEKNEQELLELDKWASLW 41 C41 [S20X](S20C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50>400 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00810.cif Linear Free Free The 'X' at position 20 indicates PEG750-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00811 EWDREINNYTSLIHSLIEEXQNQQEKNEQELLELDKWASLW 41 C41 [S20X](S20C) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae cell-cell fusion inhibition assay [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50>400 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe00811.cif Linear Free Free The 'X' at position 20 indicates PEG2000-Cys. L envelope glycoprotein(gp41) The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. 5084.73 C220H330N58O73 CFGMPV E 4.22 4 10 -6 9 13 -115.85 -11115 1 hour 30 min >10 hour 88.05 17990 449.75 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. "Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA." Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. 10.1021/bc3002248 Anti-HIV DRAVPe00812 RMKQIEDKIEEIESKQKKIENEIARIKKLLQLTVWGIKQLQARIL 45 IQN17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.19±0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00812 DRAVPe00812.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 5431.51 C243H423N69O68S CFHPY IK 9.78 11 7 4 4 17 -62.89 -10181 1 hour 2 min 2 min 123.56 5500 125 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0204 Anti-HIV DRAVPe00813 RMKQIEDKIEEIESKQKKIENEIARIKKLLQLTVWDIKQLQARIL 45 IQN17[G572D] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=15±5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00813 DRAVPe00813.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 5489.55 C245H425N69O70S CFGHPY IK 9.52 11 8 3 3 17 -69.78 -11147 1 hour 2 min 2 min 123.56 5500 125 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00814 RMKQIEDKIEEIESKQKKIENEIARIKKLIEAQQHLLQLTVWGIKQLQARIL 52 IQN23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.015±0.007 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00814 DRAVPe00814.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 6251.43 C279H480N80O79S CFPY IK 9.52 12 8 4 4 20 -61.35 -11271 1 hour 2 min 2 min 123.85 5500 107.84 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0205 Anti-HIV DRAVPe00815 RMKQIEDKIEEIESKQKKIENEIARIKKLISGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARIL 66 IQN36 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.088±0.035 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00815 DRAVPe00815.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 7787.19 C345H594N102O99S CFPY IQ 9.77 13 8 5 8 26 -49.24 -13446 1 hour 2 min 2 min 127.12 5500 84.62 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0206 Anti-HIV DRAVPe00816 IKKEIEAIKKEQEAIKKKIEAIEKLLQLTVWGIKQLQARIL 41 IZN17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.022±0.011 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00816 DRAVPe00816.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 4813.88 C222H388N58O59 CDFHMNPSY K 9.7 10 6 4 2 19 -24.88 -5195 20 hour 30 min >10 hour 140.49 5500 137.5 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0190 Anti-HIV DRAVPe00817 IKKEIEAIKKEQEAIKKKIEAIEKEIEAQQHLLQLTVWGIKQLQARIL 48 IZN23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.030±0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00817 DRAVPe00817.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 5649.75 C257H441N69O72 CDFMNPSY IK 9.11 11 8 3 2 21 -43.96 -7458 20 hour 30 min >10 hour 130.21 5500 117.02 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0191 Anti-HIV DRAVPe00818 IKKEIEAIKKEQEAIKKKIEAIEKEISGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARIL 62 IZN36 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.026±0.007 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00818 DRAVPe00818.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 7185.51 C323H555N91O92 CDFMPY I 9.46 12 8 4 6 27 -35 -9633 20 hour 30 min >10 hour 132.26 5500 90.16 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 DRAVPa0197 Anti-HIV DRAVPe00819 RMKQIEDKIEEIESKIKKIENEIARIKKLLQLTVWGIKQLQARIL 45 IIN17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.14±0.05 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00819 DRAVPe00819.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 5416.54 C244H426N68O67S CFHPY I 9.78 11 7 4 4 18 -45.11 -9135 1 hour 2 min 2 min 132.22 5500 125 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00820 KIEEIESKQKKIENEIARIKKLLQLTVWGIKQLQARIL 38 IQ22N17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=1.4±0.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00820 DRAVPe00820.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 4530.46 C206H359N57O56 CDFHMPY IK 9.87 9 5 4 4 16 -41.58 -6754 1.3 hour 3 min 2 min 136.05 5500 148.65 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00821 KIEEIESKIKKIENEIARIKKLLQLTVWGIKQLQARIL 38 II22N17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.16±0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00821 DRAVPe00821.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 4515.49 C207H362N56O55 CDFHMPY I 9.87 9 5 4 4 17 -20.53 -5708 1.3 hour 3 min 2 min 146.32 5500 148.65 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00822 KQKKIENEIARIKKLLQLTVWGIKQLQARIL 31 IQ15N17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=5.5±1..5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00822 DRAVPe00822.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 3701.55 C170H299N49O42 CDFHMPSY K 10.66 8 2 6 3 14 -30.97 -4800 1.3 hour 3 min 2 min 141.61 5500 183.33 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00823 KIKKIENEIARIKKLLQLTVWGIKQLQARIL 31 II15N17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae HIV luciferase assay [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=2.1±0.8 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe00823 DRAVPe00823.cif Linear Acetylation Amidation None L membrane The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. 3686.58 C171H302N48O41 CDFHMPSY IK 10.66 8 2 6 3 15 -5.16 -3754 1.3 hour 3 min 2 min 154.19 5500 183.33 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. "Eckert DM, Kim PS. " Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. 10.1073/pnas.201392898 Anti-HIV DRAVPe00824 ALWKTMLKKLGTMALHAGKAALGAAADTI 29 Dermaseptin-S1 (1-29) Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=1.7 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50=20 µM;293TT(embryonic human culture cells):CC50=40 µM. DRAVPe00824 DRAVPe00824.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2953.6 C133H226N36O35S2 CEFNPQRSVY A 10 5 1 4 6 15 52.41 1056 4.4 hour >20 hour >10 hour 108.28 5500 196.43 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00825 ALWTTMLKKLGKMALHAGKAALGAAADTI 29 "Dermaseptin-S1 (1-29)[K4T,T12K]" Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=1.3 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50=20 µM;293TT(embryonic human culture cells):CC50=40 µM. DRAVPe00825 DRAVPe00825.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2953.6 C133H226N36O35S2 CEFNPQRSVY A 10 5 1 4 6 15 52.41 1056 4.4 hour >20 hour >10 hour 108.28 5500 196.43 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00826 ALWKTMLKKLGTMALHAGK 19 Dermaseptin-S1 (1-19) Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=9 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50=80 µM;293TT(embryonic human culture cells):CC50=80 µM. DRAVPe00826 DRAVPe00826.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2098.64 C96H164N26O22S2 CDEFINPQRSVY KL 10.48 5 0 5 4 8 13.16 202 4.4 hour >20 hour >10 hour 97.89 5500 305.56 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00827 ALXKTMLKKLGTMAL 15 Dermaseptin-S1 (1-15)[W31NAL] Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=2.7 µM). [Ref.20718719]human red cells:HC50=75 µM. [Ref.20718719]Vero cells:CC50=50 µM;293TT(embryonic human culture cells):CC50>100 µM. DRAVPe00827 DRAVPe00827.cif Linear Free Amidation The 'X' at position 3 indicates Nal (3-[1-naphthyl]alanine). L Not found No machanism information found in the reference(s) presented in this entry 1630.31 C68H125N17O16S2 CDEFHINPQRSVWY L 10.3 3 0 3 3 6 60.67 715 4.4 hour >20 hour >10 hour 117.33 0 0 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00828 ALHKTMLKKLGTMAL 15 Dermaseptin-S1 (1-15)[W3H] Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=5 µM). [Ref.20718719]human red cells:HC50=100 µM. [Ref.20718719]Vero cells:CC50>100 µM;293TT(embryonic human culture cells):CC50>100 µM. DRAVPe00828 DRAVPe00828.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1656.12 C74H134N20O18S2 CDEFINPQRSVWY L 10.3 4 0 4 3 6 39.33 249 4.4 hour >20 hour >10 hour 117.33 0 0 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00829 KALXKTMLKKLGTMAL 16 K-Dermaseptin-S1 (1-15)[W31NAL] Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=5 µM). [Ref.20718719]human red cells:HC50=80 µM. [Ref.20718719]Vero cells:CC50=50 µM;293TT(embryonic human culture cells):CC50>100 µM. No predicted structure available DRAVPe00829.cif Linear Free Amidation The 'X' at position 4 indicates Nal (3-[1-naphthyl]alanine). L Not found No machanism information found in the reference(s) presented in this entry 1758.48 C74H137N19O17S2 CDEFHINPQRSVWY KL 10.48 4 0 4 3 6 32.5 160 1.3 hour 3 min 2 min 110 0 0 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00830 ALWKTMLKKLGTMA 14 Dermaseptin-S1 (1-14) Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=10.5 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50=85 µM;293TT(embryonic human culture cells):CC50>100 µM. DRAVPe00830 DRAVPe00830.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1592.03 C73H126N18O17S2 CDEFHINPQRSVY KL 10.3 3 0 3 3 6 31.43 456 4.4 hour >20 hour >10 hour 97.86 5500 423.08 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00831 ALWKTMLKKLGTM 13 Dermaseptin-S1 (1-13) Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=10 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50=100 µM;293TT(embryonic human culture cells):CC50>100 µM. DRAVPe00831 DRAVPe00831.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1520.96 C70H121N17O16S2 CDEFHINPQRSVY KL 10.3 3 0 3 3 5 20 275 4.4 hour >20 hour >10 hour 97.69 5500 458.33 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00832 ALWKTMLKKLGT 12 Dermaseptin-S1 (1-12) Synthetic construct(derived from Dermaseptin-S1) P24302 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae antiviral assay [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=100 µM). [Ref.20718719]human red cells:HC50>100 µM. [Ref.20718719]Vero cells:CC50>100 µM;293TT(embryonic human culture cells):CC50>100 µM. DRAVPe00832 DRAVPe00832.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1389.76 C65H112N16O15S CDEFHINPQRSVY KL 10.3 3 0 3 3 5 5.83 40 4.4 hour >20 hour >10 hour 105.83 5500 500 20718719 APMIS. 2010 Sep 1;118(9):674-80. "Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R." In vitro activity of dermaseptin S1 derivatives against genital pathogens. 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe00833 EMTWEEWEKKIEEYTKKIEEILKKSQNQQIDL 32 HP23-E6-IDL Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae HIV-1-Mediated Cell-Cell Fusion Assay "[Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=338 pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=1.14 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=813 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=748-1543 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=349-1423 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=699-4937 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. DRAVPe00833 DRAVPe00833.cif Linear Free Free None L membrane It was a fusion inhibitor and inhibits cell-cell fusion 4068.61 C182H288N44O59S ACFGHPRV E 4.73 6 9 -3 5 8 -145.94 -9191 1 hour 30 min >10 hour 73.13 12490 402.9 30901967 Molecules. 2019 Mar 21;24(6):1134. "Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. " A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. 10.3390/molecules24061134 Anti-HIV DRAVPe00834 EMTWEEWEKKIEEYIKKIEEILKKSQNQQIDL 32 YIK(625-656) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1-Mediated Cell-Cell Fusion Assay "[Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=275pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=1.12 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=640 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=627-1423 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=460-1490 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=856-5286 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. DRAVPe00834 DRAVPe00834.cif Linear Free Free None L membrane It was a fusion inhibitor and inhibits cell-cell fusion 4080.66 C184H292N44O58S ACFGHPRV E 4.73 6 9 -3 4 9 -129.69 -8442 1 hour 30 min >10 hour 85.31 12490 402.9 30901967 Molecules. 2019 Mar 21;24(6):1134. "Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. " A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. 10.3390/molecules24061134 Anti-HIV DRAVPe00835 EMTWEEWEKKIEEYIKKIEEILKKSQNQQIDLGSGX 36 YIK-C16(625-656) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV-1-Mediated Cell-Cell Fusion Assay "[Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=76 pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=0.55 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=61 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=40-179 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=65-106 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=65-188 pM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. No predicted structure available DRAVPe00835.cif Linear Free Free The 'X' at position 36 indicates PEG4-Lys-C16(Palmitic Acid). L membrane It was a fusion inhibitor and inhibits cell-cell fusion 4393.18 C191H301N47O61S ACFHPRV E 4.73 6 9 -3 7 9 -119.72 -8594 1 hour 30 min >10 hour 75.83 12490 356.86 30901967 Molecules. 2019 Mar 21;24(6):1134. "Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. " A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. 10.3390/molecules24061134 Anti-HIV DRAVPe00836 GGLKKLGKKLEGAGKRVFNAAEKALPVVAGAKAL 34 Cecropin A Aedes aegypti (Yellowfever mosquito) P01508 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2MMM "Tacaribe virus,JV,PICV" Arenaviridae "[Ref.15081088]Junin virus(JV):inhibtion of JV infection in Vero cells(EC50=3.4 μM,EC90=28.57 μM);##Tacaribe virus:inhibition of tacaribe virus infection in Vero cells(IC50=1.96 μM,EC90=33.39 μM);##Pichinde virus:inhibition of Pichinde virus infection in Vero cells(IC50=6.56 μM,EC90=39 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.15081088]Vero cells:CC50>100 μM. DRAVPe00836 DRAVPe00836.cif Linear Free Amidtion None L glycoprotein G1 "Cecropin A caused an altered intracellular distribution and membrane expression of the viral glycoprotein G1, as it was shown by membrane and cytoplasmic IF assays,which indicate that the inhibition of G1 transport and/or insertion into the cell membrane might prevent the formation of infectious particles leading to the reduction of cell-associated infectivity." 3391.11 C154H269N45O40 CDHIMQSTWY AK 10.39 8 2 6 7 16 2.06 -1602 30 hour >20 hour >10 hour 103.53 0 0 15081088  Int J Antimicrob Agents. 2004 Apr;23(4):382-9. "Albiol Matanic VC, Castilla V. " Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus.  10.1016/j.ijantimicag.2003.07.022 "Anti-Tacaribe virus,Anti-JV,Anti-Pichinde virus" DRAVPe00837 GIGAVLKVLTTGLPALISWIKRKRQQ 26 Melittin Apis mellifera (Honeybee) P01501 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2MLT "JV,HSV, Influenza A virus, EV-71, RSV,VSV, HIV" "Arenaviridae, Herpesviridae, Orthomyxoviridae, Picornaviridae, Pneumoviridae, Rhabdoviridae, Retroviridae" [Ref.15081088]Junin virus(JV):inhibtion of JV infection in Vero cells(EC50=0.86 μM);##Herpes simplex virus type 1 (HSV-1):inhibition of HSV-1 infection in Vero cells(EC50=1.35 μM);##Herpes simplex virus type 2 (HSV-2):inhibition of HSV-2 infection in Vero cells(EC50=2.05 μM).##[Ref.31422545] GFP-fused influenza A (PR8):exerts antiviral activity in MDCK cells(EC50=1.15 ± 0.09 μg/mL);##Enterovirus A71 (EV-A71):exerts antiviral activity in HeLa cells(EC50=0.76 ± 0.03 μg/mL);##GFP-fused coxsakievirus (H3):exerts antiviral activity in HeLa cells(EC50=0.99 ± 0.09 μg/mL);## GFP-fused RSV:exerts antiviral activity in HEp2 cells(EC50=0.99 ± 0.09 μg/mL);## GFP-fused VSV:exerts antiviral activity in Vero cells(EC50=1.18 ± 0.09 μg/mL);## HIV-1 (NLHX):exerts antiviral activity in Vaginal epithelial cells (VK2)(EC50=2.4 μM);## HIV-2 (NLYU2):exerts antiviral activity in Vaginal epithelial cells (VK2)(EC50=3.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15081088]Vero cells:CC50=8.51 μM. DRAVPe00837 DRAVPe00837.cif Linear Free Amidtion None L Not found "Melittin suppresses cell fusion mediated by HSV-1 syncytial mutants probably by interfering with the activity of the Na, K ATPase, cellular enzyme involved in the membrane fusion process." 2847.49 C131H228N38O32 CDEFHMNY L 12.02 5 0 5 6 12 27.31 -1482 30 hour >20 hour >10 hour 135 5500 220 15081088##31422545  Int J Antimicrob Agents. 2004 Apr;23(4):382-9.##Eur J Clin Microbiol Infect Dis. 2020 Jan;39(1):5-17. "Albiol Matanic VC, Castilla V. ##Memariani H, Memariani M, Moravvej H, Shahidi-Dadras M. " Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus. ##Melittin: a venom-derived peptide with promising anti-viral properties. 10.1016/j.ijantimicag.2003.07.022##10.1007/s10096-019-03674-0 "Anti-JV,Anti-HSV, Anti-Anti-Influenza A virus, EV-71, Anti-RSV,Anti-VSV, Anti-HIV" DRAVPe00838 GIGKFLHSAGKFGKAFVGEIMKS 23 Magainin-1 Xenopus laevis (African clawed frog) P11006 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.15081088]Herpes simplex virus type 1 (HSV-1):inhibition of HSV-1 infection in Vero cells(EC50=36.59 μM);##Herpes simplex virus type 2 (HSV-2):inhibition of HSV-2 infection in Vero cells(EC50=33.20 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15081088]Vero cells:CC50>100 μM. DRAVPe00838 DRAVPe00838.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2409.87 C112H177N29O28S CDNPQRTWY G 10 5 1 4 7 9 21.74 -206 30 hour >20 hour >10 hour 72.17 0 0 15081088  Int J Antimicrob Agents. 2004 Apr;23(4):382-9. "Albiol Matanic VC, Castilla V. " Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus.  10.1016/j.ijantimicag.2003.07.022 Anti-HSV DRAVPe00839 GIGKFLHSAKKFGKAFVGEIMNS 23 Magainin II Xenopus ruwenzoriensis (Uganda clawed frog) C0HKN6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2MAG##2LSA "CCV,HSV" Herpesviridae [Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 48 μM).##[Ref.15081088]Herpes simplex virus type 1 (HSV-1):inhibition of HSV-1 infection in Vero cells(EC50=22.16 μM);##Herpes simplex virus type 2 (HSV-2):inhibition of HSV-2 infection in Vero cells(EC50=19.80 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15081088]Vero cells:CC50>100 μM. DRAVPe00839 DRAVPe00839.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2466.93 C114H180N30O29S CDPQRTWY GK 10 5 1 4 7 9 8.26 -964 30 hour >20 hour >10 hour 72.17 0 0 15193922##15081088 Virology. 2004 Jun 1;323(2):268-75.## Int J Antimicrob Agents. 2004 Apr;23(4):382-9. "Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L.##Albiol Matanic VC, Castilla V. " Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides.##Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus. 10.1016/j.virol.2004.02.029##10.1016/j.ijantimicag.2003.07.022 "Anti-CCV,Anti-HSV" DRAVPe00840 PACQDFLGAMIHLKAKTNISIR 22 3(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(28% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00840 DRAVPe00840.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2427.91 C107H179N31O29S2 EVWY AI 9.37 4 1 3 5 9 19.09 -1997 >20 hour >20 hour ? 102.27 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00841 LKAKTNISIREGPTLGNWAR 20 4(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(24% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00841 DRAVPe00841.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2225.58 C98H165N31O28 CDFHMQVY AGIKLNRT 11 4 1 3 7 7 -63 -4206 5.5 hour 3 min 2 min 88 5500 289.47 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00842 EGPTLGNWAREIWATLFKKA 20 5(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(100% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00842 DRAVPe00842.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2288.63 C107H162N28O28 CDHMQSVY A 8.69 3 2 1 5 9 -40.5 -2171 1 hour 30 min >10 hour 73.5 11000 578.95 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00843 EIWATLFKKATRQCRRGRIW 20 6(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(100% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00843 DRAVPe00843.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2520 C114H183N37O26S DHMNPSVY R 11.56 6 1 5 4 8 -73.5 -6003 1 hour 30 min >10 hour 68.5 11000 578.95 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00844 TRQCRRGRIWKRWNETITGP 20 7(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(94% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00844 DRAVPe00844.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2514.9 C108H176N40O28S ADFHLMSVY R 11.83 6 1 5 7 4 -158.5 -8919 7.2 hour >20 hour >10 hour 39 11000 578.95 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00845 SGCANNTCYNVSVIVPDYQC 20 9(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(24% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00845 DRAVPe00845.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2150.38 C89H136N24O32S3 EFHKLMRW CNV 3.8 0 1 -1 12 5 10 -2020 1.9 hour >20 hour >10 hour 68 3105 163.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00846 YLDRVDTWLQGKINISLCLT 20 11(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(9% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00846 DRAVPe00846.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2351.75 C106H171N27O31S AEFHMP L 5.95 2 2 0 7 8 18.5 -2066 2.8 hour 10 min 2 min 131.5 6990 367.89 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00847 GKINISLCLTGGKMLYNKVT 20 12(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(10% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00847 DRAVPe00847.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2153.63 C95H165N25O27S2 ADEFHPQRW GKL 9.63 3 0 3 10 6 28 -352 30 hour >20 hour >10 hour 112 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00848 GGKMLYNKVTKQLSYCTDPL 20 13(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00848 DRAVPe00848.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2259.66 C100H163N25O30S2 AEFHIRW KL 9.05 3 1 2 9 4 -47 -2206 30 hour >20 hour >10 hour 73 2980 156.84 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00849 KQLSYCTDPLQIPLINYTFG 20 14(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(15% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00849 DRAVPe00849.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2314.68 C107H164N24O31S AEHMRVW L 5.83 1 1 0 8 6 -3 -1101 1.3 hour 3 min 2 min 97.5 2980 156.84 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00850 PNQTCMWNTSQIQDPEIPKC 20 16(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00850 DRAVPe00850.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2333.63 C98H153N27O33S3 AFGHLRVY PQ 4.37 1 2 -1 7 3 -102 -4244 >20 hour >20 hour ? 39 5625 296.05 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00851 QIQDPEIPKCGWWNQMAYYN 20 17(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(2% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00851 DRAVPe00851.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2484.79 C113H158N28O32S2 FHLRSTV Q 4.37 1 2 -1 6 5 -106 -3038 0.8 hour 10 min >10 hour 44 13980 735.79 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00852 FHCQRTQSQPGSWFRAISSWKQ 22 20(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(4% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00852 DRAVPe00852.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2665.97 C119H173N37O32S DELMNVY QS 10.86 4 0 4 7 6 -106.36 -5881 1.1 hour 3 min 2 min 22.27 11000 523.81 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00853 GSWFRAISSWKQRNRWEWRPDF 22 21(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00853 DRAVPe00853.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2896.23 C135H187N41O32 CHLMTVY RW 11.54 5 2 3 5 8 -145.45 -8019 30 hour >20 hour >10 hour 22.27 22000 1047.62 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00854 KQRNRWEWRPDFKSKKVKISLPC 23 22(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00854 DRAVPe00854.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2930.47 C133H213N41O32S AGHMTY K 10.56 8 2 6 4 6 -155.65 -8422 1.3 hour 3 min 2 min 46.52 11000 500 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00855 KSKKVKISLPCNSTKNLTFA 20 23(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(10% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00855 DRAVPe00855.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2207.66 C98H171N27O28S DEGHMQRWY K 10.2 5 0 5 8 6 -42.5 -3150 1.3 hour 3 min 2 min 78 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00856 CNSTKNLTFAMRSSGDYGEV 20 24(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(25% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00856 DRAVPe00856.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2180.39 C90H142N26O33S2 HIPQW S 6.06 2 2 0 11 4 -56.5 -4550 1.2 hour >20 hour >10 hour 39 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00857 MRSSGDYGEVTGAWIEFGCH 20 25(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(27% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00857 DRAVPe00857.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2202.4 C95H136N26O31S2 KLNPQ G 4.65 2 3 -1 9 5 -33 -2796 30 hour >20 hour >10 hour 39 6990 367.89 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00858 TGAWIEFGCHRNKSNLHTEA 20 26(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00858 DRAVPe00858.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2271.49 C98H147N31O30S DMPQVY AEGHNT 6.62 4 2 2 8 6 -77.5 -4330 7.2 hour >20 hour >10 hour 49 5500 289.47 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00859 RNKSNLHTEARFRIRCRWNV 20 27(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(2% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00859 DRAVPe00859.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2556.94 C109H178N42O28S DGMPQY R 11.83 7 1 6 6 6 -132 -9523 1 hour 2 min 2 min 58.5 5500 289.47 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00860 RFRIRCRWNVGSDTSLIDTC 20 28(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(40% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00860 DRAVPe00860.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2398.74 C101H164N34O30S2 AEHKMPQY R 9.02 4 2 2 8 6 -40 -6809 1 hour 2 min 2 min 73 5625 296.05 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00861 GSDTSLIDTCGNTPNVSGAN 20 29(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(12% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00861 DRAVPe00861.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 1923 C75H123N23O34S EFHKMQRWY GNST 3.56 0 2 -2 13 4 -40 -3548 30 hour >20 hour >10 hour 58.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00862 PVDCTMYSNKMYNCSLQNGF 20 31(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(8% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00862 DRAVPe00862.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2315.63 C98H147N25O32S4 AEHIRW N 6.17 1 1 0 11 3 -43.5 -2924 >20 hour >20 hour ? 34 3105 163.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00863 MYNCSLQNGFTMKVDDLIVH 20 32(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(33% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00863 DRAVPe00863.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2328.7 C101H158N26O31S3 AEPRW DLMNV 5.19 2 2 0 7 6 9 -1984 30 hour >20 hour >10 hour 87.5 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00864 TMKVDDLIVHFNMTKAVEMV 20 33(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(25% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00864 DRAVPe00864.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2321.79 C102H169N25O30S3 CGPQRSWY V 5.35 3 3 0 3 8 45 -1395 7.2 hour >20 hour >10 hour 102 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00865 FNMTKAVEMVNIAGNWSCTS 20 34(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(15% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00865 DRAVPe00865.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2203.53 C94H147N25O30S3 DHLPQRY N 5.99 1 1 0 9 7 17 -1537 1.1 hour 3 min 2 min 58.5 5500 289.47 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00866 NIAGNWSCTSDLPSSWGYMN 20 35(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(22% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00866 DRAVPe00866.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2203.39 C95H135N25O32S2 EFHKQRV S 3.8 0 1 -1 12 5 -44.5 -2313 1.4 hour 3 min >10 hour 44 12490 657.37 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00867 CTSDLPSSWGYMNCNCTNSSSS 22 36(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00867 DRAVPe00867.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2344.5 C92H138N26O38S4 AEFHIKQRV S 3.8 0 1 -1 17 2 -54.55 -4334 1.2 hour >20 hour >10 hour 17.73 7115 338.81 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00868 CNCTNSSSSYSGTKMACPSNRG 22 37(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00868 DRAVPe00868.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2255.45 C85H139N29O35S4 DEFHILQVW S 8.68 2 0 2 17 1 -80 -5619 1.2 hour >20 hour >10 hour 4.55 1615 76.9 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00869 SGTKMACPSNRGILRNWYNP 20 38(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(52% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00869 DRAVPe00869.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2265.59 C97H153N31O28S2 DEFHQV N 10.05 3 0 3 10 4 -87 -4533 1.9 hour >20 hour >10 hour 44 6990 367.89 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00870 RGILRNWYNPFAGLRQSLEQ 20 39(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00870 DRAVPe00870.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2418.74 C109H168N34O29 CDHKMTV LR 10.74 3 1 2 6 7 -79.5 -5079 1 hour 2 min 2 min 83 6990 367.89 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00871 VAGLRQSLEQYQVVKQPDYL 20 40(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(48% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00871 DRAVPe00871.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2334.66 C105H168N28O32 CFHIMNTW Q 6.04 2 2 0 4 7 -45 -3221 100 hour >20 hour >10 hour 107 2980 156.84 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00872 YQVVKQPDYLLVPEEVMEYK 20 41(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(38% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00872 DRAVPe00872.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2470.86 C115H176N24O34S ACFGHINRSTW V 4.41 2 4 -2 3 6 -48 -2340 2.8 hour 10 min 2 min 97 4470 235.26 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00873 PDYLLVPEEVMEYKPRRKRAAI 22 42(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(54% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00873 DRAVPe00873.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2674.16 C121H197N33O33S CFGHNQSTW EPR 8.83 5 4 1 2 7 -75.91 -5648 >20 hour >20 hour ? 88.64 2980 141.9 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00874 YKPRRKRAAIHVMLALATVLSI 22 43(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(52% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00874 DRAVPe00874.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2508.11 C114H199N35O26S CDEFGNQW A 11.73 6 0 6 3 11 40.91 -2436 2.8 hour 10 min 2 min 133.18 1490 70.95 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00875 HVMLALATVLSIAGAGTGATAI 22 44(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(58% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00875 DRAVPe00875.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2038.43 C90H156N24O27S CDEFKNPQRWY A 6.74 1 0 1 7 13 155.45 3294 3.5 hour 10 min >10 hour 142.27 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00876 AGAGTGATAIGMVTQYHQVL 20 45(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00876 DRAVPe00876.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 1946.21 C84H136N24O27S CDEFKNPRSW AG 6.78 1 0 1 8 8 53 768 4.4 hour >20 hour >10 hour 88 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00877 GMVTQYHQVLATHQEAIEKV 20 46(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(43% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00877 DRAVPe00877.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2282.6 C100H160N28O31S CDFNPRSW QV 6 3 2 1 4 7 -22.5 -2152 30 hour >20 hour >10 hour 92.5 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00878 ATHQEAIEKVTGALKINNLR 20 47(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(44% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00878 DRAVPe00878.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2206.53 C95H164N30O30 CDFMPSWY A 8.64 4 2 2 5 8 -43 -3817 4.4 hour >20 hour >10 hour 107.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00879 TGALKINNLRLVTLEHQVLV 20 48(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(73% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00879 DRAVPe00879.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2231.67 C100H175N29O28 CDFMPSWY L 8.44 3 1 2 5 10 52.5 -1151 7.2 hour >20 hour >10 hour 165.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00880 LVTLEHQVLVIGLKVEAMEK 20 49(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(45% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00880 DRAVPe00880.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2249.74 C102H177N25O29S CDFNPRSWY LV 5.5 3 3 0 2 10 70.5 156 5.5 hour 3 min 2 min 160.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00881 IGLKVEAMEKFLYTAFAMQE 20 50(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(74% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00881 DRAVPe00881.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2319.76 C107H167N23O30S2 CDHNPRSW AE 4.79 2 3 -1 3 9 34.5 -395 20 hour 30 min >10 hour 88 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00882 FLYTAFAMQELGCNQNQFFC 20 51(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(18% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00882 DRAVPe00882.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2375.72 C108H151N25O30S3 DHIKPRSVW F 4 0 1 -1 7 8 29.5 -819 1.1 hour 3 min 2 min 49 1615 85 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00883 LGCNQNQFFCKIPLELWTRY 20 52(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(21% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00883 DRAVPe00883.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2473.89 C114H169N29O29S2 ADHMSV L 8.05 2 1 1 7 7 -21.5 -2288 5.5 hour 3 min 2 min 78 7115 374.47 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00884 NMTINQTIWNHGNITLGEWY 20 54(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(4% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00884 DRAVPe00884.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2405.67 C108H157N29O32S ACDFKPRSV N 5.24 1 1 0 10 6 -55 -2285 1.4 hour 3 min >10 hour 78 12490 657.37 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00885 HGNITLGEWYNQTKDLQQKF 20 55(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(35% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00885 DRAVPe00885.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2420.67 C109H162N30O33 ACMPRSV Q 6.75 3 2 1 7 5 -125 -4452 3.5 hour 10 min >10 hour 58.5 6990 367.89 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00886 NQTKDLQQKFYEIIMDIEQN 20 56(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(68% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00886 DRAVPe00886.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2498.79 C109H172N28O37S ACGHPRSVW Q 4.32 2 4 -2 4 5 -114 -5530 1.4 hour 3 min >10 hour 78 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00887 YEIIMDIEQNNVQGKTGIQQ 20 57(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(37% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00887 DRAVPe00887.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2321.59 C99H161N27O35S ACFHLPRSW IQ 4.14 1 3 -2 6 5 -70.5 -3809 2.8 hour 10 min 2 min 92.5 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00888 NVQGKTGIQQLQKWEDWVRW 20 58(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(96% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00888 DRAVPe00888.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2499.81 C114H171N33O31 ACFHMPSY Q 8.59 3 2 1 4 7 -121.5 -4613 1.4 hour 3 min >10 hour 68 16500 868.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00889 LQKWEDWVRWIGNIPQYLKG 20 59(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(98% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00889 DRAVPe00889.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2529.93 C121H177N31O29 ACFHMST W 8.5 3 2 1 4 8 -77 -2682 5.5 hour 3 min 2 min 92.5 17990 946.84 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00890 IGNIPQYLKGLLGGILGIGL 20 60(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00890 DRAVPe00890.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2009.46 C95H161N23O24 ACDEFHMRSTVW G 8.59 1 0 1 8 9 104 3205 20 hour 30 min >10 hour 175.5 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00891 LLGGILGIGLGVLLLILCLP 20 61(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(88% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00891 DRAVPe00891.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 1960.58 C95H170N20O21S ADEFHKMNQRSTWY L 5.52 0 0 0 6 13 254 6906 5.5 hour 3 min 2 min 248.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00892 GVLLLILCLPTLVDCIRNCI 20 62(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(32% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00892 DRAVPe00892.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2184.79 C98H174N24O25S3 AEFHKMQSWY L 5.82 1 1 0 6 11 190 2429 30 hour >20 hour >10 hour 204.5 125 6.58 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00893 TLVDCIRNCIHKILGYTVIA 20 63(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(9% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00893 DRAVPe00893.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2245.73 C100H169N27O27S2 EFMPQSW I 7.76 3 1 2 7 9 95.5 -286 7.2 hour >20 hour >10 hour 151 1615 85 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00894 HKILGYTVIAMPEVEGEEIQ 20 64(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(8% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00894 DRAVPe00894.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2256.6 C101H162N24O32S CDFNRSW E 4.48 2 4 -2 4 7 2 -1190 3.5 hour 10 min >10 hour 112 1490 78.42 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00895 MPEVEGEEIQPQMELRRNGR 20 65(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(7% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00895 DRAVPe00895.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2398.69 C98H164N32O34S2 ACDFHKSTWY E 4.65 3 5 -2 3 3 -146 -7607 30 hour >20 hour >10 hour 53.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00896 PQMELRRNGRQCGMSEKEEE 20 66(derived from FIV envelope glycoprotein ) Synthetic construct(derived from FIV envelope glycoprotein (gE)) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae Syncitia assay [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00896 DRAVPe00896.cif Linear Free Free None L Syncytium formation The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. 2407.68 C94H159N33O35S3 ADFHITVWY E 5.07 4 5 -1 5 1 -192.5 -9270 >20 hour >20 hour ? 19.5 0 0 8661378 Virology. 1996 Jun 15;220(2):274-84.  "Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C." Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. 10.1006/viro.1996.0315 Anti-FIV DRAVPe00897 IINFYDPLVFPSDEFDASISQVNEKINQSLAFIRK 35 T-104 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2cell from viral cytopathic effect(CPE)(EC50=91 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00897 DRAVPe00897.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4059.59 C187H285N45O56 CGHMTW I 4.44 3 5 -2 8 15 -4.86 -5248 20 hour 30 min >10 hour 100.29 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1211 Anti-RSV DRAVPe00898 INFYDPLVFPSDEFDASISQVNEKINQSLAFIRKS 35 T-105 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=93 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00898 DRAVPe00898.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4033.51 C184H279N45O57 CGHMTW S 4.44 3 5 -2 9 14 -20 -6080 20 hour 30 min >10 hour 89.14 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1212 Anti-RSV DRAVPe00899 NFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSD 35 T-106 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00899 DRAVPe00899.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4035.44 C182H273N45O59 CGHMTW S 4.23 3 6 -3 9 13 -42.86 -7444 1.4 hour 3 min >10 hour 78 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-RSV DRAVPe00900 FYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDE 35 T-107 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=20 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00900 DRAVPe00900.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4050.45 C183H274N44O60 CGHMTW S 4.14 3 7 -4 8 13 -42.86 -7461 1.1 hour 3 min 2 min 78 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0681 Anti-RSV DRAVPe00901 YDPLVFPSDEFDASISQVNEKINQSLAFIRKSDEL 35 T-108 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00901 DRAVPe00901.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4016.43 C180H276N44O60 CGHMTW S 4.14 3 7 -4 8 13 -40 -7267 2.8 hour 10 min 2 min 89.14 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1214 Anti-RSV DRAVPe00902 DPLVFPSDEFDASISQVNEKINQSLAFIRKSDELL 35 T-109 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00902 DRAVPe00902.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3966.41 C177H278N44O59 CGHMTWY S 4.14 3 7 -4 7 14 -25.43 -6761 1.1 hour 3 min >10 hour 100.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0712 Anti-RSV DRAVPe00903 PLVFPSDEFDASISQVNEKINQSLAFIRKSDELLH 35 T-110 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=30 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00903 DRAVPe00903.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3988.47 C179H280N46O57 CGMTWY S 4.58 4 6 -2 7 14 -24.57 -6355 >20 hour >20 hour ? 100.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1216 Anti-RSV DRAVPe00904 LVFPSDEFDASISQVNEKINQSLAFIRKSDELLHN 35 T-111 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=9 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00904 DRAVPe00904.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4005.45 C178H279N47O58 CGMTWY S 4.58 4 6 -2 8 14 -30 -7019 5.5 hour 3 min 2 min 100.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1217 Anti-RSV DRAVPe00905 VFPSDEFDASISQVNEKINQSLAFIRKSDELLHNV 35 T-112 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=19 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00905 DRAVPe00905.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3991.43 C177H277N47O58 CGMTWY S 4.58 4 6 -2 8 14 -28.86 -7107 100 hour >20 hour >10 hour 97.43 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1218 Anti-RSV DRAVPe00906 FPSDEFDASISQVNEKINQSLAFIRKSDELLHNVN 35 T-113 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00906 DRAVPe00906.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4006.4 C176H274N48O59 CGMTWY S 4.58 4 6 -2 9 13 -50.86 -8175 1.1 hour 3 min 2 min 89.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1219 Anti-RSV DRAVPe00907 PSDEFDASISQVNEKINQSLAFIRKSDELLHNVNA 35 T-114 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00907 DRAVPe00907.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3930.3 C170H270N48O59 CGMTWY S 4.58 4 6 -2 9 13 -53.71 -8292 >20 hour >20 hour ? 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1220 Anti-RSV DRAVPe00908 SDEFDASISQVNEKINQSLAFIRKSDELLHNVNAG 35 T-115 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00908 DRAVPe00908.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3890.24 C167H266N48O59 CMPTWY S 4.58 4 6 -2 10 13 -50.29 -8198 1.9 hour >20 hour >10 hour 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1221 Anti-RSV DRAVPe00909 DEFDASISQVNEKINQSLAFIRKSDELLHNVNAGK 35 T-116 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=12 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00909 DRAVPe00909.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3931.33 C170H273N49O58 CMPTWY NS 4.95 5 6 -1 9 13 -59.14 -8413 1.1 hour 3 min >10 hour 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1222 Anti-RSV DRAVPe00910 EFDASISQVNEKINQSLAFIRKSDELLHNVNAGKS 35 T-117 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=13 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00910 DRAVPe00910.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3903.32 C169H273N49O57 CMPTWY S 5.56 5 5 0 10 13 -51.43 -7881 1 hour 30 min >10 hour 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1223 Anti-RSV DRAVPe00911 FDASISQVNEKINQSLAFIRKSDELLHNVNAGKST 35 T-118 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "RSV,HPIV,MeV" Paramyxoviridae "Cytopathic effect(CPE) assay,antifusion assay,plaque reduction assay" [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6 μg/ml);inhibition of cell-cell fusion in HEp2 cell(EC50=0.051 μg/ml);##measles virus(MV):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##Human parainfluenza virus type 3(HPIV3):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##HIV-1 LAI:inhibition of cell-cell fusion in HEp2 cell(EC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00911 DRAVPe00911.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3875.31 C168H273N49O56 CMPWY S 6.76 5 4 1 11 13 -43.43 -7457 1.1 hour 3 min 2 min 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1144 "Anti-RSV,Anti-HPIV,Anti-MeV" DRAVPe00912 DASISQVNEKINQSLAFIRKSDELLHNVNAGKSTT 35 T-119 Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00912 DRAVPe00912.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3829.24 C163H271N49O57 CMPWY S 6.76 5 4 1 12 12 -53.43 -8012 1.1 hour 3 min >10 hour 92 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa1225 Anti-RSV DRAVPe00913 YTPNDITLNNSVALDPIDISIELNKAKSDLEESKE 35 T-189 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00913 DRAVPe00913.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3890.27 C168H274N42O63 CFGHMQRW DEILNS 4.07 3 8 -5 11 11 -62.29 -7719 2.8 hour 10 min 2 min 103.14 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-HPIV-3 DRAVPe00914 TPNDITLNNSVALDPIDISIELNKAKSDLEESKEW 35 T-190 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00914 DRAVPe00914.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3913.3 C170H275N43O62 CFGHMQRY DEILNS 4.07 3 8 -5 10 12 -61.14 -7472 7.2 hour >20 hour >10 hour 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-HPIV-3 DRAVPe00915 PNDITLNNSVALDPIDISIELNKAKSDLEESKEWI 35 T-191 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00915 DRAVPe00915.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3925.36 C172H279N43O61 CFGHMQRY I 4.07 3 8 -5 9 13 -46.29 -6723 >20 hour >20 hour ? 114.29 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-HPIV-3 DRAVPe00916 NDITLNNSVALDPIDISIELNKAKSDLEESKEWIR 35 T-192 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00916 DRAVPe00916.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3984.43 C173H284N46O61 CFGHMQY I 4.29 4 8 -4 9 13 -54.57 -8215 1.4 hour 3 min >10 hour 114.29 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-HPIV-3 DRAVPe00917 DITLNNSVALDPIDISIELNKAKSDLEESKEWIRR 35 T-193 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00917 DRAVPe00917.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4026.51 C175H290N48O60 CFGHMQY I 4.51 5 8 -3 8 13 -57.43 -9043 1.1 hour 3 min >10 hour 114.29 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-HPIV-3 DRAVPe00918 ITLNNSVALDPIDISIELNKAKSDLEESKEWIRRS 35 T-194 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=62 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00918 DRAVPe00918.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3998.5 C174H290N48O59 CFGHMQY IS 4.72 5 7 -2 9 13 -49.71 -8511 20 hour 30 min >10 hour 114.29 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0742 Anti-HPIV-3 DRAVPe00919 TLNNSVALDPIDISIELNKAKSDLEESKEWIRRSN 35 T-195 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=72 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00919 DRAVPe00919.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3999.45 C172H285N49O60 CFGHMQY S 4.71 5 7 -2 10 12 -72.57 -9667 7.2 hour >20 hour >10 hour 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0358 Anti-HPIV-3 DRAVPe00920 LNNSVALDPIDISIELNKAKSDLEESKEWIRRSNQ 35 T-196 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00920 DRAVPe00920.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4026.47 C173H286N50O60 CFGHMTY S 4.72 5 7 -2 9 12 -80.57 -9964 5.5 hour 3 min 2 min 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0359 Anti-HPIV-3 DRAVPe00921 NNSVALDPIDISIELNKAKSDLEESKEWIRRSNQK 35 T-197 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00921 DRAVPe00921.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4041.49 C173H287N51O60 CFGHMTY S 5.1 6 7 -1 9 11 -102.57 -11011 1.4 hour 3 min >10 hour 92 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0360 Anti-HPIV-3 DRAVPe00922 NSVALDPIDISIELNKAKSDLEESKEWIRRSNQKL 35 T-198 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00922 DRAVPe00922.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4040.54 C175H292N50O59 CFGHMTY S 5.1 6 7 -1 8 12 -81.71 -9855 1.4 hour 3 min >10 hour 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0361 Anti-HPIV-3 DRAVPe00923 SVALDPIDISIELNKAKSDLEESKEWIRRSNQKLD 35 T-199 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00923 DRAVPe00923.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4041.53 C175H291N49O60 CFGHMTY S 4.77 6 8 -2 7 12 -81.71 -10063 1.9 hour >20 hour >10 hour 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0362 Anti-HPIV-3 DRAVPe00924 VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDS 35 T-200 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00924 DRAVPe00924.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4041.53 C175H291N49O60 CFGHMTY S 4.77 6 8 -2 7 12 -81.71 -10063 100 hour >20 hour >10 hour 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0363 Anti-HPIV-3 DRAVPe00925 ALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI 35 T-201 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00925 DRAVPe00925.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4055.55 C176H293N49O60 CFGHMTVY IS 4.77 6 8 -2 7 12 -80.86 -9975 4.4 hour >20 hour >10 hour 106 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0364 Anti-HPIV-3 DRAVPe00926 LDPIDISIELNKAKSDLEESKEWIRRSNQKLDSIG 35 T-202 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.03 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00926 DRAVPe00926.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4041.53 C175H291N49O60 CFHMTVY IS 4.77 6 8 -2 8 11 -87.14 -10062 5.5 hour 3 min 2 min 103.14 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0365 Anti-HPIV-3 DRAVPe00927 DPIDISIELNKAKSDLEESKEWIRRSNQKLDSIGN 35 T-203 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00927 DRAVPe00927.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4042.47 C173H286N50O61 CFHMTVY IS 4.77 6 8 -2 9 10 -108 -11218 1.1 hour 3 min >10 hour 92 5500 161.76 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0366 Anti-HPIV-3 DRAVPe00928 PIDISIELNKAKSDLEESKEWIRRSNQKLDSIGNW 35 T-204 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.07 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00928 DRAVPe00928.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4113.6 C180H291N51O59 CFHMTVY IS 5.1 6 7 -1 9 11 -100.57 -10113 >20 hour >20 hour ? 92 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0367 Anti-HPIV-3 DRAVPe00929 IDISIELNKAKSDLEESKEWIRRSNQKLDSIGNWH 35 T-205 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HPIV-3,MeV,RSV,HIV" "Paramyxoviridae, Retroviridae" Luminescence fusion assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=0.11 μg/ml);inhibition of cell-cell fusion in HEp2 cell(EC50=0.038 μg/ml);##measles virus(MV):inhibition of cell-cell fusion in HEp2 cell(EC50=1.19 μg/ml);##Respiratory syncytial virus(RSV):inhibition of cell-cell fusion in HEp2 cell(EC50=1.76 μg/ml);##HIV-1 LAI:inhibition of cell-cell fusion in HEp2 cell(EC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00929 DRAVPe00929.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4153.62 C181H291N53O59 CFMPTVY IS 5.64 7 7 0 9 11 -105.14 -10579 20 hour 30 min >10 hour 92 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0368 "Anti-HPIV-3,Anti-MeV,Anti-RSV,Anti-HIV" DRAVPe00930 IDISIELNKAKSDLEESKEWIRRSNQKLDSIGNWH 35 HPIV3 F HRC derived peptide(454-488) Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HeV,HPIV-3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Hendra virus(HeV):inhibition of virus infection in HeLa cells(IC50=50 nM);inhibition of fusion in HeLa cells(IC50=5000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=1500 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe00930.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 10HB structure that is required for fusion." 4153.62 C181H291N53O59 CFMPTVY IS 5.64 7 7 0 9 11 -105.14 -10579 20 hour 30 min >10 hour 92 11000 323.53 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV-3" DRAVPe00931 DISIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQ 35 T-206 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00931 DRAVPe00931.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4168.59 C180H288N54O60 CFMPTVY S 5.64 7 7 0 9 10 -128 -11625 1.1 hour 3 min >10 hour 80.86 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0369 Anti-HPIV-3 DRAVPe00932 ISIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQS 35 T-207 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00932 DRAVPe00932.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4140.58 C179H288N54O59 CFMPTVY S 6.78 7 6 1 10 10 -120.29 -11093 20 hour 30 min >10 hour 80.86 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0370 Anti-HPIV-3 DRAVPe00933 SIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSS 35 T-208 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00933 DRAVPe00933.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4114.5 C176H282N54O60 CFMPTVY S 6.5 7 6 1 11 9 -135.43 -11925 1.9 hour >20 hour >10 hour 69.71 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0371 Anti-HPIV-3 DRAVPe00934 IELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSST 35 T-209 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00934 DRAVPe00934.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4128.53 C177H284N54O60 CFMPVY S 6.78 7 6 1 11 9 -135.14 -11842 20 hour 30 min >10 hour 69.71 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0372 Anti-HPIV-3 DRAVPe00935 ELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSSTT 35 T-210 Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPIV-3 Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2.4 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00935 DRAVPe00935.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 4116.47 C175H280N54O61 CFMPVY S 6.87 7 6 1 12 8 -150 -12591 1 hour 30 min >10 hour 58.57 11000 323.53 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0373 Anti-HPIV-3 DRAVPe00936 PDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLED 35 T-252 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00936 DRAVPe00936.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3786.3 C168H274N46O53 CFMQW L 4.52 4 6 -2 8 14 -8 -4733 >20 hour >20 hour ? 125.43 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 DRAVPa0399 Anti-MeV DRAVPe00937 DAVYLHRIDLGPPISLERLDVGTNLQNAIAKLEDA 35 T-253 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00937 DRAVPe00937.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3831.34 C169H277N47O54 CFMW L 4.52 4 6 -2 7 15 -7.14 -5200 1.1 hour 3 min >10 hour 128.29 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00938 AVYLHRIDLGPPISLERLDVGTNLQNAIAKLEDAK 35 T-254 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00938 DRAVPe00938.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3844.43 C171H284N48O52 CFMW L 5.52 5 5 0 7 15 -8.29 -4883 4.4 hour >20 hour >10 hour 128.29 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00939 VYLHRIDLGPPISLERLDVGTNLQNAIAKLEDAKE 35 T-255 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=85.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00939 DRAVPe00939.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3902.46 C173H286N48O54 CFMW L 4.95 5 6 -1 7 14 -23.43 -5745 100 hour >20 hour >10 hour 125.43 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00940 YLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKEL 35 T-256 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=90.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00940 DRAVPe00940.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3845.41 C171H283N47O53 CFMQW L 4.95 5 6 -1 8 14 -15.71 -5009 2.8 hour 10 min 2 min 128.29 1490 43.82 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00941 LHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELL 35 T-257 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MeV,RSV,HPIV-3,HIV" "Paramyxoviridae, Retroviridae" "Cytopathic effect(CPE) assay,antifusion assay,plaque reduction assay" [Ref.8700906]measles virus(MeV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.5 μg/ml);inhibition of cell-cell fusion in HEp2 cell(EC50=0.068 μg/ml);##Human parainfluenza virus type 3(HPIV-3):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##Respiratory syncytial virus(RSV):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##HIV-1 LAI:inhibition of cell-cell fusion in HEp2 cell(EC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00941 DRAVPe00941.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3795.39 C168H285N47O52 CFMQWY L 4.95 5 6 -1 7 15 -1.14 -4503 5.5 hour 3 min 2 min 139.43 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 "Anti-MeV,Anti-RSV,Anti-HPIV-3,Anti-HIV" DRAVPe00942 HRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLE 35 T-258 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2.2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00942 DRAVPe00942.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3811.35 C167H281N47O54 CFMQWY L 4.7 5 7 -2 7 14 -22 -5676 3.5 hour 10 min >10 hour 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00943 RIDLGPPISLERLDVGTNLGNAIAKLEDAKELLES 35 T-259 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00943 DRAVPe00943.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3761.29 C164H279N45O55 CFHMQWY L 4.44 4 7 -3 8 14 -15.14 -5550 1 hour 2 min 2 min 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00944 IDLGPPISLERLDVGTNLGNAIAKLEDAKELLESS 35 T-260 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=4.9 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00944 DRAVPe00944.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3692.18 C161H272N42O56 CFHMQWY L 4.2 3 7 -4 9 14 -4.57 -4398 20 hour 30 min >10 hour 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00945 DLGPPISLERLDVGTNLGNAIAKLEDAKELLESSD 35 T-261 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=5.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00945 DRAVPe00945.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3694.11 C159H266N42O58 CFHMQWY L 4.07 3 8 -5 9 13 -27.43 -5762 1.1 hour 3 min >10 hour 117.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00946 LGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQ 35 T-262 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6.5 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00946 DRAVPe00946.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3707.15 C160H269N43O57 CFHMWY L 4.2 3 7 -4 9 13 -27.43 -5444 5.5 hour 3 min 2 min 117.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00947 GPPISLERLDVGTNLGNAIAKLEDAKELLESSDQI 35 T-263 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=10.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00947 DRAVPe00947.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3707.15 C160H269N43O57 CFHMWY L 4.2 3 7 -4 9 13 -25.43 -5444 30 hour >20 hour >10 hour 117.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00948 PPISLERLDVGTNLGNAIAKLEDAKELLESSDQIL 35 T-264 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00948 DRAVPe00948.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3763.26 C164H277N43O57 CFHMWY L 4.2 3 7 -4 8 14 -13.43 -5046 >20 hour >20 hour ? 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00949 PISLERLDVGTNLGNAIAKLEDAKELLESSDQILR 35 T-265 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=3.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00949 DRAVPe00949.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3822.33 C165H282N46O57 CFHMWY L 4.44 4 7 -3 8 14 -21.71 -6538 >20 hour >20 hour ? 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00950 ISLERLDVGTNLGNAIAKLEDAKELLESSDQILRS 35 T-266 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=13.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00950 DRAVPe00950.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3812.29 C163H280N46O58 CFHMPWY L 4.44 4 7 -3 9 14 -19.43 -6878 20 hour 30 min >10 hour 128.29 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00951 SLERLDVGTNLGNAIAKLEDAKELLESSDQILRSM 35 T-267 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=12.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00951 DRAVPe00951.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3830.32 C162H278N46O58S CFHPWY L 4.44 4 7 -3 9 13 -26.86 -7135 1.9 hour >20 hour >10 hour 117.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00952 LERLDVGTNLGNAIAKLEDAKELLESSDQILRSMK 35 T-268 Synthetic construct(derived from measles virus(MV) fusion (F) protein) P69353 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MeV Paramyxoviridae Cytopathic effect(CPE) assay [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=7.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). DRAVPe00952 DRAVPe00952.cif Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3871.42 C165H285N47O57S CFHPWY L 4.72 5 7 -2 8 13 -35.71 -7350 5.5 hour 3 min 2 min 117.14 0 0 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. "Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr." Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  10.1073/pnas.93.5.2186 Anti-MeV DRAVPe00953 DDSVVCAAMSYSYA 14 P1(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00953 DRAVPe00953.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1481.61 C62H92N14O24S2 EFGHIKLNPQRTW AS 3.56 0 2 -2 6 5 44.29 -1078 1.1 hour 3 min >10 hour 62.86 2980 229.23 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00954 DDSVVCAAMSYSFA 14 P2(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(29% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00954 DRAVPe00954.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1465.61 C62H92N14O23S2 EGHIKLNPQRTW AS 3.56 0 2 -2 5 6 73.57 -766 1.1 hour 3 min >10 hour 62.86 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00955 DDSVVCAAMSYSHA 14 P3(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00955 DRAVPe00955.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1455.58 C59H90N16O23S2 EFGIKLNPQRTW AS 4.2 1 2 -1 5 5 30.71 -1530 1.1 hour 3 min >10 hour 62.86 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00956 DDSVVSAAMSYSYA 14 P4(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±9% inhibition at 1 µM; 47±1% inhibition at 3 µM; 89±6% inhibition at 10 µM; IC50=3.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00956 DRAVPe00956.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1465.55 C62H92N14O25S CEFGHIKLNPQRTW S 3.56 0 2 -2 6 5 20.71 -1546 1.1 hour 3 min >10 hour 62.86 2980 229.23 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00957 DDSVVSAAMSYSFA 14 P5(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00957 DRAVPe00957.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1449.55 C62H92N14O24S CEGHIKLNPQRTW S 3.56 0 2 -2 5 6 50 -1234 1.1 hour 3 min >10 hour 62.86 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00958 DDSVVAAMSYSYA 13 P7(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00958 DRAVPe00958.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1378.47 C59H87N13O23S CEFGHIKLNPQRTW AS 3.56 0 2 -2 5 5 28.46 -1206 1.1 hour 3 min >10 hour 67.69 2980 248.33 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00959 DDSVVAAMSYSFA 13 P8(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00959 DRAVPe00959.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1362.47 C59H87N13O22S CEGHIKLNPQRTW AS 3.56 0 2 -2 4 6 60 -894 1.1 hour 3 min >10 hour 67.69 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00960 DDSVVAAMSYSHA 13 P9(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00960 DRAVPe00960.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1352.44 C56H85N15O22S CEFGIKLNPQRTW AS 4.2 1 2 -1 4 5 13.85 -1658 1.1 hour 3 min >10 hour 67.69 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00961 ADLEVVAATYVLVA 14 P10(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 6±11% inhibition at 1 µM;27±5% inhibition at 3 µM; 75±1% inhibition at 10 µM; IC50=6.3µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00961 DRAVPe00961.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1433.66 C66H108N14O21 CFGHIKMNPQRSW AV 3.67 0 2 -2 2 10 161.43 1500 4.4 hour >20 hour >10 hour 167.14 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00962 ADLEVVAATFVLVA 14 P11(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(-2±7% inhibition at 1 µM; 29±5% inhibition at 3 µM; 83±5% inhibition at 10 µM; IC50=5.72 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00962 DRAVPe00962.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1417.67 C66H108N14O20 CGHIKMNPQRSWY AV 3.67 0 2 -2 1 11 190.71 1812 4.4 hour >20 hour >10 hour 167.14 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00963 ADLEVVAATHVLVA 14 P12(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 11±16% inhibition at 1 µM; 77±3% inhibition at 3 µM; 95±1% inhibition at 10 µM; IC50=2.2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00963 DRAVPe00963.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1407.63 C63H106N16O20 CFGIKMNPQRSWY AV 4.35 1 2 -1 1 10 147.86 1048 4.4 hour >20 hour >10 hour 167.14 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00964 ADLEVVAATYV 11 P13(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00964 DRAVPe00964.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1150.29 C52H83N11O18 CFGHIKMNPQRSW AV 3.67 0 2 -2 2 7 116.36 423 4.4 hour >20 hour >10 hour 141.82 1490 149 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00965 KKKKVVAATYVLVA 14 P15(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(30% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00965 DRAVPe00965.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1517.92 C72H128N18O17 CDEFGHIMNPQRSW KV 10.18 4 0 4 2 8 60 160 1.3 hour 3 min 2 min 132.14 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00966 DDDEVVAATYVLVA 14 P17(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00966 DRAVPe00966.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1479.6 C65H102N14O25 CFGHIKMNPQRSW V 3.37 0 4 -4 2 8 71.43 -917 1.1 hour 3 min >10 hour 132.14 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00967 ADLEVVAATYVDDD 14 P19(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00967 DRAVPe00967.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1495.56 C64H98N14O27 CFGHIKMNPQRSW D 3.28 0 5 -5 2 7 16.43 -2193 4.4 hour >20 hour >10 hour 111.43 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00968 ADLEVVAATYVDVA 14 P20(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 18±21% inhibition at 1 µM; 75±1% inhibition at 3 µM; 96±1% inhibition at 10 µM; IC50=2.1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00968 DRAVPe00968.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1435.59 C64H102N14O23 CFGHIKMNPQRSW AV 3.49 0 3 -3 2 9 109.29 136 4.4 hour >20 hour >10 hour 139.29 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00969 ADLEVVAATYVLDA 14 P21(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00969 DRAVPe00969.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1449.62 C65H104N14O23 CFGHIKMNPQRSW A 3.49 0 3 -3 2 9 106.43 224 4.4 hour >20 hour >10 hour 146.43 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00970 ADLEVVAATYVLVD 14 P22(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(38% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00970 DRAVPe00970.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1477.67 C67H108N14O23 CFGHIKMNPQRSW V 3.49 0 3 -3 2 9 123.57 447 4.4 hour >20 hour >10 hour 160 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00971 ADLEVVAATYVDDA 14 P23(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(20% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00971 DRAVPe00971.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1451.55 C63H98N14O25 CFGHIKMNPQRSW A 3.37 0 4 -4 2 8 54.29 -1140 4.4 hour >20 hour >10 hour 118.57 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00972 ADLEVVAATYVLDD 14 P24(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 5±4% inhibition at 1 µM; 26±4% inhibition at 3 µM; 65±3% inhibition at 10 µM; IC50=7.4 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00972 DRAVPe00972.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1493.63 C66H104N14O25 CFGHIKMNPQRSW ADV 3.37 0 4 -4 2 8 68.57 -829 4.4 hour >20 hour >10 hour 139.29 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00973 ADLEVVAATYVDVD 14 P25(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00973 DRAVPe00973.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1479.6 C65H102N14O25 CFGHIKMNPQRSW V 3.37 0 4 -4 2 8 71.43 -917 4.4 hour >20 hour >10 hour 132.14 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00974 KKKKVVAATYVKKA 14 P27(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00974 DRAVPe00974.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1561.98 C73H132N20O17 CDEFGHILMNPQRSW K 10.4 6 0 6 2 6 -52.86 -1846 1.3 hour 3 min 2 min 83.57 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00975 KKKKVVAATYFFFA 14 P30(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00975 DRAVPe00975.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1648.02 C83H126N18O17 CDEGHILMNPQRSW K 10.18 4 0 4 2 8 32.86 -246 1.3 hour 3 min 2 min 62.86 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00976 KKKKVVAATYFLVA 14 P31(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00976 DRAVPe00976.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1565.96 C76H128N18O17 CDEGHIMNPQRSW K 10.18 4 0 4 2 8 50 54 1.3 hour 3 min 2 min 111.43 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00977 KKKKVVAATYVLVF 14 P33(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00977 DRAVPe00977.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1594.02 C78H132N18O17 CDEGHIMNPQRSW KV 10.18 4 0 4 2 8 67.14 277 1.3 hour 3 min 2 min 125 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00978 KKKKVVAATYVLFA 14 P34(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00978 DRAVPe00978.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1565.96 C76H128N18O17 CDEGHIMNPQRSW K 10.18 4 0 4 2 8 50 54 1.3 hour 3 min 2 min 111.43 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00979 KKKKVVAATYKKVA 14 P37(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00979 DRAVPe00979.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1561.98 C73H132N20O17 CDEFGHILMNPQRSW K 10.4 6 0 6 2 6 -52.86 -1846 1.3 hour 3 min 2 min 83.57 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00980 AKLKVVAATYVLKK 14 P38(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00980 DRAVPe00980.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1531.95 C73H130N18O17 CDEFGHIMNPQRSW K 10.18 4 0 4 2 8 57.14 248 4.4 hour >20 hour >10 hour 139.29 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00981 KKKKVVAATYKKKK 14 P42(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00981 DRAVPe00981.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1648.11 C77H142N22O17 CDEFGHILMNPQRSW K 10.54 8 0 8 2 4 -151.43 -3541 1.3 hour 3 min 2 min 55.71 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00982 ADLEVVAATYVKKK 14 P44(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00982 DRAVPe00982.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1534.82 C70H119N17O21 CFGHIMNPQRSW AKV 8.47 3 2 1 2 7 7.86 -1242 4.4 hour >20 hour >10 hour 111.43 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00983 ADLEVVAATYKKKK 14 P45(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00983 DRAVPe00983.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1563.86 C71H122N18O21 CFGHIMNPQRSW K 9.41 4 2 2 2 6 -50 -2201 4.4 hour >20 hour >10 hour 90.71 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00984 ADLEVVAATYAAAA 14 P47(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00984 DRAVPe00984.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1335.48 C59H94N14O21 CFGHIKMNPQRSW A 3.67 0 2 -2 2 10 112.86 743 4.4 hour >20 hour >10 hour 119.29 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00985 KDLKVVAATYVKKK 14 P48(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(21% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00985 DRAVPe00985.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1590.97 C74H131N19O19 CEFGHIMNPQRSW K 10 5 1 4 2 6 -35.71 -1852 1.3 hour 3 min 2 min 104.29 1490 114.62 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00986 KKKKAVAATYVLV 13 P49(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(59% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00986 DRAVPe00986.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1418.79 C67H119N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 32.31 -244 1.3 hour 3 min 2 min 120 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00987 KKKKVAAATYVLV 13 P50(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±1% inhibition at 1 µM; 51±10% inhibition at 3 µM; 74±1% inhibition at 10 µM; IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00987 DRAVPe00987.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1418.79 C67H119N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 32.31 -244 1.3 hour 3 min 2 min 120 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00988 KKKKVVAAAYVLV 13 P51(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00988 DRAVPe00988.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1416.81 C68H121N17O15 CDEFGHIMNPQRSTW KV 10.18 4 0 4 1 8 70 417 1.3 hour 3 min 2 min 142.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00989 KKKKVVAATAVLV 13 P52(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00989 DRAVPe00989.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1354.74 C63H119N17O15 CDEFGHIMNPQRSWY KV 10.48 4 0 4 1 8 74.62 174 1.3 hour 3 min 2 min 142.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00990 KKKKVVAATYVAV 13 P54(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(21% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00990 DRAVPe00990.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1404.76 C66H117N17O16 CDEFGHILMNPQRSW KV 10.18 4 0 4 2 7 35.38 -332 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00991 KKKKVVAATYVLA 13 P55(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00991 DRAVPe00991.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1418.79 C67H119N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 32.31 -244 1.3 hour 3 min 2 min 120 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00992 KKKKVLAATYVLV 13 P57(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00992 DRAVPe00992.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1460.87 C70H125N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 47.69 67 1.3 hour 3 min 2 min 142.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00993 KKKKVVLATYVLV 13 P58(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 21±8% inhibition at 1 µM; 30±5% inhibition at 3 µM; 61±15% inhibition at 10 µM; IC50=7.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00993 DRAVPe00993.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1488.92 C72H129N17O16 CDEFGHIMNPQRSW KV 10.18 4 0 4 2 7 66.15 290 1.3 hour 3 min 2 min 156.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00994 KKKKVVAALYVLV 13 P60(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00994 DRAVPe00994.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1458.89 C71H127N17O15 CDEFGHIMNPQRSTW KV 10.18 4 0 4 1 8 85.38 728 1.3 hour 3 min 2 min 164.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00995 KKKKVVAATYLLV 13 P61(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00995 DRAVPe00995.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1460.87 C70H125N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 47.69 67 1.3 hour 3 min 2 min 142.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00996 KKKKVVAATYVLL 13 P62(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(25% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00996 DRAVPe00996.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1460.87 C70H125N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 47.69 67 1.3 hour 3 min 2 min 142.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00997 KKKKFVAATYVLV 13 P63(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 32±7% inhibition at 1 µM; 35±8% inhibition at 3 µM; 61±6% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00997 DRAVPe00997.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1494.88 C73H123N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 40 -127 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00998 KKKKVFAATYVLV 13 P64(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00998 DRAVPe00998.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1494.88 C73H123N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 40 -127 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe00999 KKKKVVFATYVLV 13 P65(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(34% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe00999 DRAVPe00999.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1522.94 C75H127N17O16 CDEGHIMNPQRSW KV 10.18 4 0 4 2 7 58.46 96 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01000 KKKKVVAFTYVLV 13 P66(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(23% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01000 DRAVPe01000.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1522.94 C75H127N17O16 CDEGHIMNPQRSW KV 10.18 4 0 4 2 7 58.46 96 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01001 KKKKVVAAFYVLV 13 P67(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01001 DRAVPe01001.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1492.91 C74H125N17O15 CDEGHIMNPQRSTW KV 10.18 4 0 4 1 8 77.69 534 1.3 hour 3 min 2 min 134.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01002 KKKKVVAATFVLV 13 P68(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(28% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01002 DRAVPe01002.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1430.84 C69H123N17O15 CDEGHIMNPQRSWY KV 10.48 4 0 4 1 8 82.31 291 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01003 KKKKVVAATYFLV 13 P69(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01003 DRAVPe01003.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1494.88 C73H123N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 40 -127 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01004 KKKKVVAATYVFV 13 P70(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01004 DRAVPe01004.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1480.86 C72H121N17O16 CDEGHILMNPQRSW KV 10.18 4 0 4 2 7 43.08 -215 1.3 hour 3 min 2 min 104.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01005 KKKKVVAATYVLF 13 P71(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01005 DRAVPe01005.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1494.88 C73H123N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 40 -127 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01006 KKKKEVAATYVLV 13 P72(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01006 DRAVPe01006.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1476.82 C69H121N17O18 CDFGHIMNPQRSW K 9.83 4 1 3 2 6 -8.46 -1106 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01007 KKKKVVAETYVLV 13 P75(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01007 DRAVPe01007.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1504.88 C71H125N17O18 CDFGHIMNPQRSW KV 9.83 4 1 3 2 6 10 -883 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01008 KKKKVVAAEYVLV 13 P76(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01008 DRAVPe01008.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1474.85 C70H123N17O17 CDFGHIMNPQRSTW KV 9.83 4 1 3 1 7 29.23 -445 1.3 hour 3 min 2 min 134.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01009 KKKKVVAATEVLV 13 P77(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01009 DRAVPe01009.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1412.78 C65H121N17O17 CDFGHIMNPQRSWY KV 10 4 1 3 1 7 33.85 -688 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01010 KKKKVKAATYVLV 13 P82(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(25% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01010 DRAVPe01010.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1475.88 C70H126N18O16 CDEFGHIMNPQRSW K 10.3 5 0 5 2 6 -11.54 -980 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01011 KKKKVVKATYVLV 13 P83(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 26±12% inhibition at 1 µM; 37±10% inhibition at 3 µM; 63±2% inhibition at 10 µM; IC50=6.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01011 DRAVPe01011.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1503.94 C72H130N18O16 CDEFGHIMNPQRSW K 10.3 5 0 5 2 6 6.92 -757 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01012 KKKKVVAKTYVLV 13 P84(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01012 DRAVPe01012.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1503.94 C72H130N18O16 CDEFGHIMNPQRSW K 10.3 5 0 5 2 6 6.92 -757 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01013 KKKKTVAATYVLV 13 P89(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(27% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01013 DRAVPe01013.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1448.81 C68H121N17O17 CDEFGHIMNPQRSW K 10.18 4 0 4 3 6 13.08 -682 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01014 KKKKVTAATYVLV 13 P90(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 15±12% inhibition at 1 µM; 44±3% inhibition at 3 µM; 77±6% inhibition at 10 µM; IC50=4.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01014 DRAVPe01014.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1448.81 C68H121N17O17 CDEFGHIMNPQRSW K 10.18 4 0 4 3 6 13.08 -682 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01015 KKKKVVTATYVLV 13 P91(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01015 DRAVPe01015.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1476.87 C70H125N17O17 CDEFGHIMNPQRSW KV 10.18 4 0 4 3 6 31.54 -459 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01016 KKKKVVATTYVLV 13 P92(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01016 DRAVPe01016.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1476.87 C70H125N17O17 CDEFGHIMNPQRSW KV 10.18 4 0 4 3 6 31.54 -459 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01017 KKKKVVAATTVLV 13 P93(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2223% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01017 DRAVPe01017.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1384.77 C64H121N17O16 CDEFGHIMNPQRSWY KV 10.48 4 0 4 2 7 55.38 -264 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01018 KKKKVVAATYVLT 13 P96(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01018 DRAVPe01018.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1448.81 C68H121N17O17 CDEFGHIMNPQRSW K 10.18 4 0 4 3 6 13.08 -682 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01019 KKKKVVGATYVLV 13 P99(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01019 DRAVPe01019.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1432.81 C68H121N17O16 CDEFHIMNPQRSW KV 10.18 4 0 4 3 6 33.85 -108 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01020 KKKKVVAGTYVLV 13 P100(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(30% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01020 DRAVPe01020.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1432.81 C68H121N17O16 CDEFHIMNPQRSW KV 10.18 4 0 4 3 6 33.85 -108 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01021 KKKKVVAAGYVLV 13 P101(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01021 DRAVPe01021.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1402.79 C67H119N17O15 CDEFHIMNPQRSTW KV 10.18 4 0 4 2 7 53.08 330 1.3 hour 3 min 2 min 134.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01022 KKKKVVAATGVLV 13 P102(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01022 DRAVPe01022.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1340.72 C62H117N17O15 CDEFHIMNPQRSWY KV 10.48 4 0 4 2 7 57.69 87 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01023 KKKKVVAATYVGV 13 P104(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01023 DRAVPe01023.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1390.73 C65H115N17O16 CDEFHILMNPQRSW KV 10.18 4 0 4 3 6 18.46 -419 1.3 hour 3 min 2 min 104.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01024 KKKKVVAATYVLG 13 P105(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01024 DRAVPe01024.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1404.76 C66H117N17O16 CDEFHIMNPQRSW K 10.18 4 0 4 3 6 15.38 -331 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01025 KKKKVVAATYVLV 13 P106(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(17% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01025 DRAVPe01025.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1446.84 C69H123N17O16 CDEFGHIMNPQRSW KV 10.18 4 0 4 2 7 50.77 -21 1.3 hour 3 min 2 min 134.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01026 KKKKPVAATYVLV 13 P107(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(24% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01026 DRAVPe01026.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1444.82 C69H121N17O16 CDEFGHIMNQRSW K 10.18 4 0 4 2 6 6.15 -425 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01027 KKKKVPAATYVLV 13 P108(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01027 DRAVPe01027.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1444.82 C69H121N17O16 CDEFGHIMNQRSW K 10.18 4 0 4 2 6 6.15 -425 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01028 KKKKVVAATYVPV 13 P113(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(10% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01028 DRAVPe01028.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1430.8 C68H119N17O16 CDEFGHILMNQRSW KV 10.18 4 0 4 2 6 9.23 -513 1.3 hour 3 min 2 min 104.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01029 KKKKVVLATLVLV 13 P116(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01029 DRAVPe01029.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1438.9 C69H131N17O15 CDEFGHIMNPQRSWY KV 10.48 4 0 4 1 8 105.38 796 1.3 hour 3 min 2 min 186.92 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01030 KKKKLVLPFLFFV 13 P119(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(6% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01030 DRAVPe01030.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1607.1 C84H135N17O14 ACDEGHIMNQRSTWY K 10.48 4 0 4 0 8 84.62 958 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01031 KKKKLLAPFLFFV 13 P120(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01031 DRAVPe01031.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1579.05 C82H131N17O14 CDEGHIMNQRSTWY K 10.48 4 0 4 0 8 66.15 735 1.3 hour 3 min 2 min 120 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01032 KKKKLLLAFLFFV 13 P121(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01032 DRAVPe01032.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1595.09 C83H135N17O14 CDEGHIMNPQRSTWY KL 10.48 4 0 4 0 9 107.69 1227 1.3 hour 3 min 2 min 150 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01033 KKKKLLLPTLFFV 13 P122(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01033 DRAVPe01033.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1575.06 C80H135N17O15 ACDEGHIMNQRSWY KL 10.48 4 0 4 1 7 54.62 491 1.3 hour 3 min 2 min 142.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01034 KKKKLVLATYVLV 13 P126(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01034 DRAVPe01034.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1502.95 C73H131N17O16 CDEFGHIMNPQRSW K 10.18 4 0 4 2 7 63.08 378 1.3 hour 3 min 2 min 164.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01035 KKKKLVAAFYVLV 13 P128(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01035 DRAVPe01035.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1506.94 C75H127N17O15 CDEGHIMNPQRSTW K 10.18 4 0 4 1 8 74.62 622 1.3 hour 3 min 2 min 142.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01036 KKKKLVAATYVFV 13 P129(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01036 DRAVPe01036.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1494.88 C73H123N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 40 -127 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01037 KKKKLVAATYVLF 13 P130(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01037 DRAVPe01037.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1508.91 C74H125N17O16 CDEGHIMNPQRSW K 10.18 4 0 4 2 7 36.92 -39 1.3 hour 3 min 2 min 120 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01038 KKKKVLAPTYVLV 13 P132(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01038 DRAVPe01038.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1486.9 C72H127N17O16 CDEFGHIMNQRSW K 10.18 4 0 4 2 6 21.54 -114 1.3 hour 3 min 2 min 134.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01039 KKKKVVLAFYVLV 13 P138(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(10% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01039 DRAVPe01039.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1534.99 C77H131N17O15 CDEGHIMNPQRSTW KV 10.18 4 0 4 1 8 93.08 845 1.3 hour 3 min 2 min 156.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01040 KKKKVVAPFYVLV 13 P140(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01040 DRAVPe01040.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1518.95 C76H127N17O15 CDEGHIMNQRSTW KV 10.18 4 0 4 1 7 51.54 353 1.3 hour 3 min 2 min 126.92 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01041 KKKKVVAPTLVLV 13 P141(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01041 DRAVPe01041.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1422.86 C68H127N17O15 CDEFGHIMNQRSWY KV 10.48 4 0 4 1 7 63.85 304 1.3 hour 3 min 2 min 156.92 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01042 KKKKVVAPTYFLV 13 P142(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01042 DRAVPe01042.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1520.92 C75H125N17O16 CDEGHIMNQRSW K 10.18 4 0 4 2 6 13.85 -308 1.3 hour 3 min 2 min 104.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01043 KKKKVVAPTYVLF 13 P144(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01043 DRAVPe01043.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1520.92 C75H125N17O16 CDEGHIMNQRSW K 10.18 4 0 4 2 6 13.85 -308 1.3 hour 3 min 2 min 104.62 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01044 KKKKVVAAFLVLV 13 P145(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(20% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01044 DRAVPe01044.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1442.9 C71H127N17O14 CDEGHIMNPQRSTWY KV 10.48 4 0 4 0 9 116.92 1040 1.3 hour 3 min 2 min 164.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01045 KKKKVVAAFYFLV 13 P146(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01045 DRAVPe01045.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1540.96 C78H125N17O15 CDEGHIMNPQRSTW K 10.18 4 0 4 1 8 66.92 428 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01046 KKKKVVAAFYVLF 13 P148(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01046 DRAVPe01046.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1540.96 C78H125N17O15 CDEGHIMNPQRSTW K 10.18 4 0 4 1 8 66.92 428 1.3 hour 3 min 2 min 112.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01047 KKKKVVAATLVLF 13 P151(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01047 DRAVPe01047.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1444.87 C70H125N17O15 CDEGHIMNPQRSWY K 10.48 4 0 4 1 8 79.23 379 1.3 hour 3 min 2 min 142.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01048 KKKKVLLPFLFFF 13 P154(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01048 DRAVPe01048.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1655.15 C88H135N17O14 ACDEGHIMNQRSTWY FK 10.48 4 0 4 0 8 73.85 852 1.3 hour 3 min 2 min 112.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01049 KKKKLVLPFLFFF 13 P155(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01049 DRAVPe01049.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1655.15 C88H135N17O14 ACDEGHIMNQRSTWY FK 10.48 4 0 4 0 8 73.85 852 1.3 hour 3 min 2 min 112.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01050 KKKKLLAPFLFFF 13 P156(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01050 DRAVPe01050.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1627.09 C86H131N17O14 CDEGHIMNQRSTVWY FK 10.48 4 0 4 0 8 55.38 629 1.3 hour 3 min 2 min 97.69 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01051 KKKKLLLAFLFFF 13 P157(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01051 DRAVPe01051.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1643.13 C87H135N17O14 CDEGHIMNPQRSTVWY FKL 10.48 4 0 4 0 9 96.92 1121 1.3 hour 3 min 2 min 127.69 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01052 KKKKLLLPFYFFF 13 P159(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(24% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01052 DRAVPe01052.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1719.19 C92H135N17O15 ACDEGHIMNQRSTVW FK 10.18 4 0 4 1 7 31.54 434 1.3 hour 3 min 2 min 90 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01053 KKKKLLLPFLFLF 13 P161(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01053 DRAVPe01053.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1635.16 C86H139N17O14 ACDEGHIMNQRSTVWY L 10.48 4 0 4 0 8 78.46 1134 1.3 hour 3 min 2 min 150 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01054 KKKKLLLPFLFFF 13 P162(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01054 DRAVPe01054.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1669.17 C89H137N17O14 ACDEGHIMNQRSTVWY FKL 10.48 4 0 4 0 8 70.77 940 1.3 hour 3 min 2 min 120 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01055 KKKKVVLPFLFFF 13 P163(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( -2±1% inhibition at 1 µM; 29±4% inhibition at 3 µM; 69±9% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01055 DRAVPe01055.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1641.12 C87H133N17O14 ACDEGHIMNQRSTWY FK 10.48 4 0 4 0 8 76.92 764 1.3 hour 3 min 2 min 104.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01056 KKKKLVAPFLFFF 13 P164(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01056 DRAVPe01056.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1613.06 C85H129N17O14 CDEGHIMNQRSTWY FK 10.48 4 0 4 0 8 58.46 541 1.3 hour 3 min 2 min 90 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01057 KKKKLLAAFLFFF 13 P165(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 29±5% inhibition at 1 µM; 28±9% inhibition at 3 µM; 61±17% inhibition at 10 µM; IC50=7.6 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01057 DRAVPe01057.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1601.05 C84H129N17O14 CDEGHIMNPQRSTVWY FK 10.48 4 0 4 0 9 81.54 810 1.3 hour 3 min 2 min 105.38 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01058 KKKKLLLATLFFF 13 P166(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01058 DRAVPe01058.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1597.06 C82H133N17O15 CDEGHIMNPQRSVWY KL 10.48 4 0 4 1 8 70 566 1.3 hour 3 min 2 min 127.69 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01059 KKKKLLLPTYFFF 13 P167(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01059 DRAVPe01059.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1673.12 C87H133N17O16 ACDEGHIMNQRSVW K 10.18 4 0 4 2 6 4.62 -121 1.3 hour 3 min 2 min 90 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01060 KKKKLLLPFLVLF 13 P169(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01060 DRAVPe01060.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1587.11 C82H139N17O14 ACDEGHIMNQRSTWY L 10.48 4 0 4 0 8 89.23 1240 1.3 hour 3 min 2 min 172.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01061 KKKKVLAPFLFFF 13 P170(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01061 DRAVPe01061.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1613.06 C85H129N17O14 CDEGHIMNQRSTWY FK 10.48 4 0 4 0 8 58.46 541 1.3 hour 3 min 2 min 90 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01062 KKKKVLLPFYFFF 13 P172(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(27% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01062 DRAVPe01062.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1705.16 C91H133N17O15 ACDEGHIMNQRSTW FK 10.18 4 0 4 1 7 34.62 346 1.3 hour 3 min 2 min 82.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01063 KKKKLVLAFLFFF 13 P175(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01063 DRAVPe01063.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1629.11 C86H133N17O14 CDEGHIMNPQRSTWY FK 10.48 4 0 4 0 9 100 1033 1.3 hour 3 min 2 min 120 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01064 KKKKLVLPTLFFF 13 P176(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(29% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01064 DRAVPe01064.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1609.07 C83H133N17O15 ACDEGHIMNQRSWY K 10.48 4 0 4 1 7 46.92 297 1.3 hour 3 min 2 min 112.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01065 KKKKLVLPFYFFF 13 P177(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01065 DRAVPe01065.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1705.16 C91H133N17O15 ACDEGHIMNQRSTW FK 10.18 4 0 4 1 7 34.62 346 1.3 hour 3 min 2 min 82.31 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01066 KKKKLVLPFLLFF 13 P178(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01066 DRAVPe01066.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1621.13 C85H137N17O14 ACDEGHIMNQRSTWY KL 10.48 4 0 4 0 8 81.54 1046 1.3 hour 3 min 2 min 142.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01067 KKKKLVLPFLFVF 13 P179(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 14±6% inhibition at 1 µM; 34±11% inhibition at 3 µM; 55±11% inhibition at 10 µM; IC50=8.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01067 DRAVPe01067.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1607.1 C84H135N17O14 ACDEGHIMNQRSTWY K 10.48 4 0 4 0 8 84.62 958 1.3 hour 3 min 2 min 134.62 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01068 KKKKLLAPFLVFF 13 P180(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01068 DRAVPe01068.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1579.05 C82H131N17O14 CDEGHIMNQRSTWY K 10.48 4 0 4 0 8 66.15 735 1.3 hour 3 min 2 min 120 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01069 KKKKLLLAFYFFF 13 P181(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01069 DRAVPe01069.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1693.15 C90H133N17O15 CDEGHIMNPQRSTVW FK 10.18 4 0 4 1 8 57.69 615 1.3 hour 3 min 2 min 97.69 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01070 KKKKLLLAFLFLF 13 P182(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01070 DRAVPe01070.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1609.12 C84H137N17O14 CDEGHIMNPQRSTVWY L 10.48 4 0 4 0 9 104.62 1315 1.3 hour 3 min 2 min 157.69 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01071 KKKKLLLPTLVFF 13 P183(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01071 DRAVPe01071.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1575.06 C80H135N17O15 ACDEGHIMNQRSWY KL 10.48 4 0 4 1 7 54.62 491 1.3 hour 3 min 2 min 142.31 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01072 KKKKLLLPFYFLF 13 P185(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01072 DRAVPe01072.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1685.17 C89H137N17O15 ACDEGHIMNQRSTVW KL 10.18 4 0 4 1 7 39.23 628 1.3 hour 3 min 2 min 120 1490 124.17 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01073 AKDLEVVTSTYVLVEA 16 P189(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 5±7% inhibition at 1 µM; 74±6% inhibition at 3 µM; 96±3% inhibition at 10 µM; IC50=2.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01073 DRAVPe01073.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1736.98 C78H129N17O27 CFGHIMNPQRW V 4.14 1 3 -2 4 8 63.13 -695 4.4 hour >20 hour >10 hour 133.75 1490 99.33 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01074 AKDLEVVCSTYVLVEA 16 P190(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available IDXP HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 24 ±15% inhibition at 1 µM; 86 ±3% inhibition at 3 µM; 99 ±2% inhibition at 10 µM; IC50=1.8 µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01074 DRAVPe01074.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1739.01 C77H127N17O26S FGHIMNPQRW V 4.14 1 3 -2 4 8 83.13 -310 4.4 hour >20 hour >10 hour 133.75 1490 99.33 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01075 AECVVSCSMSYTKA 14 P197(derived from HCV polyprotein) Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae NS3-6K inhibition assay(determined by Fluorescent probe) [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±7% inhibition at 1 µM; 29±6% inhibition at 3 µM; 66±3% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01075 DRAVPe01075.cif Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1478.71 C60H99N15O22S3 DFGHILNPQRW S 6.03 1 1 0 7 4 50.71 -866 4.4 hour >20 hour >10 hour 55.71 1615 124.23 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease.  10.1177/095632020301400501 Anti-HCV DRAVPe01076 SWLRDIWDWICEVLSDFK 18 C5A(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,DENV,MeV,RSV,HIV" "Flaviviridae, Paramyxoviridae, Retroviridae" RT-QPCR assay "[Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.79 μM);##HCV (JFH-1) genotype 2a:inhibition of infection in Huh-7.5.1 cells(IC50=0.6 μM);##HCV (H77 envelope) genotype 1a:inhibition of infection in Huh-7.5.1 cells(IC50=3.9 μM);##HCV (Con1 envelope) genotype 1b:inhibition of infection in Huh-7.5.1 cells(IC50=1.6 μM);##HCV (J6CF envelope) genotype 2a:inhibition of infection in Huh-7.5.1 cells(IC50=1.1 μM);##Dengue virus:inhibition of infection in Huh-7.5.1 cells(IC50=2.0 μM);##West Nile virus:inhibition of infection in Huh-7.5.1 cells(IC50=4.5 μM);##Measles virus:inhibition of infection in Huh-7.5.1 cells(IC50=2.7 μM);##Respiratory syncytial virus:inhibition of infection in Huh-7.5.1 cells(IC50=4.5 μM);##Human immunodeficiency virus:inhibition of infection in Huh-7.5.1 cells(IC50=1.3 μM);##IC50>18 μM against Adenovirus,Borna disease virus,Coronavirus 229E,Coxsackie virus,Hepatitis B virus,Influenza virus,Lymphocytic choriomeningitis virus,Rhinovirus,Rotavirus WISC2,Vaccinia virus,Vesicular stomatitis virus." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01076 DRAVPe01076.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 "Anti-HCV,Anti-DENV,Anti-MeV,Anti-RSV,Anti-HIV" DRAVPe01077 swlrdiwdwicevlsdfk 18 2(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.32 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01077 DRAVPe01077.cif Linear Free Free None D membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 H-34O-17 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 4.23 0 0 0 0 0 0 0 0 0 0 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01078 SWLRDIWDWICEVLSD 16 3(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.98 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01078 DRAVPe01078.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2036.29 C94H134N22O27S AFGHKMNPQTY DW 3.84 1 4 -3 3 8 3.13 -2270 1.9 hour >20 hour >10 hour 115.63 16500 1100 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01079 SWLRDIWDWICEVL 14 4(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=11.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01079 DRAVPe01079.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1834.12 C87H124N20O22S AFGHKMNPQTY W 4.03 1 3 -2 2 8 34.29 -1058 1.9 hour >20 hour >10 hour 132.14 16500 1269.23 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 DRAVPa1474 Anti-HCV DRAVPe01080 SWLRDIWDWICEV 13 5(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01080 DRAVPe01080.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1720.96 C81H113N19O21S AFGHKMNPQTY W 4.03 1 3 -2 2 7 7.69 -1550 1.9 hour >20 hour >10 hour 112.31 16500 1375 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01081 SWLRDIWDWICE 12 6(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01081 DRAVPe01081.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1621.83 C76H104N18O20S AFGHKMNPQTVY W 4.03 1 3 -2 2 6 -26.67 -1954 1.9 hour >20 hour >10 hour 97.5 16500 1500 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01082 SWLRDIWDWI 10 7(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01082 DRAVPe01082.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1389.58 C68H92N16O16 ACEFGHKMNPQTVY W 4.21 1 2 -1 1 6 -22 -1401 1.9 hour >20 hour >10 hour 117 16500 1833.33 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01083 SWLRDIWD 8 8(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01083 DRAVPe01083.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1090.2 C51H71N13O14 ACEFGHKMNPQTVY DW 4.21 1 2 -1 1 4 -72.5 -2126 1.9 hour >20 hour >10 hour 97.5 11000 1571.43 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01084 LRDIWDWICEVLSDFK 16 9(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01084 DRAVPe01084.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2038.35 C95H140N22O26S AGHMNPQTY D 4.23 2 4 -2 2 8 6.88 -2420 5.5 hour 3 min 2 min 115.63 11000 733.33 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01085 DIWDWICEVLSDFK 14 10(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01085 DRAVPe01085.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1769 C83H117N17O24S AGHMNPQRTY D 3.84 1 4 -3 2 7 12.86 -1420 1.1 hour 3 min >10 hour 104.29 11000 846.15 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01086 WDWICEVLSDFK 12 11(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01086 DRAVPe01086.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1540.75 C73H101N15O20S AGHMNPQRTY DW 4.03 1 3 -2 2 6 6.67 -1040 2.8 hour 3 min 2 min 89.17 11000 1000 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01087 WICEVLSDFK 10 12(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01087 DRAVPe01087.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 1239.45 C58H86N12O16S AGHMNPQRTY CDEFIKLSVW 4.37 1 2 -1 2 5 52 -401 2.8 hour 3 min 2 min 107 5500 611.11 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01088 CEVLSDFK 8 13(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01088 DRAVPe01088.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 940.08 C41H65N9O14S AGHIMNPQRTWY CDEFKLSV 4.37 1 2 -1 2 3 20 -1126 1.2 hour >20 hour >10 hour 85 0 0 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01089 SGSWLRDIWDWICEVLSDFK 20 14(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01089 DRAVPe01089.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2455.77 C114H163N27O32S AHMNPQTY DSW 4.23 2 4 -2 5 9 -9 -2773 1.9 hour >20 hour >10 hour 92.5 16500 868.42 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01090 GSWLRDIWDWICEVLSDFK 19 15(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.51 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01090 DRAVPe01090.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2368.69 C111H158N26O30S AHMNPQTY DW 4.23 2 4 -2 4 9 -5.26 -2433 30 hour >20 hour >10 hour 97.37 16500 916.67 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01091 SWLRDIWDWICEVLSDFKT 19 16(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01091 DRAVPe01091.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2412.74 C113H162N26O31S AGHMNPQY DW 4.23 2 4 -2 4 9 -6.84 -2784 1.9 hour >20 hour >10 hour 97.37 16500 916.67 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01092 SWLRDIWDWICEVLSDFKTW 20 17(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.51 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01092 DRAVPe01092.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2598.96 C124H172N28O32S AGHMNPQY W 4.23 2 4 -2 4 10 -11 -2551 1.9 hour >20 hour >10 hour 92.5 22000 1157.89 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01093 SWRLIDWDWICEVLSDFK 18 18(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=4.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01093 DRAVPe01093.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01094 SWRLDIWDWICESVLDFK 18 19(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01094 DRAVPe01094.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01095 DWLKAFYDKVAEKLKEAF 18 21(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>28 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01095 DRAVPe01095.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2201.55 C106H157N23O28 CGHIMNPQRST K 6.21 4 4 0 1 9 -50 -2580 1.1 hour 3 min >10 hour 76.11 6990 411.18 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 DRAVPa1305 Anti-HCV DRAVPe01096 VLDLIYSLHKQINRGLKKIVL 21 22(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>36 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01096 DRAVPe01096.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2464.04 C115H199N31O28 ACEFMPTW L 10 5 1 4 4 10 40.48 -1229 100 hour >20 hour >10 hour 176.19 1490 74.5 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01097 KFDSLVECIWDWIDRLWS 18 23(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.85 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01097 DRAVPe01097.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.3 hour 3 min 2 min 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01098 KWLCRIWSWISDVLDDFE 18 25(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01098 DRAVPe01098.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.3 hour 3 min 2 min 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01099 SIWRDWVDLICEFLSDWK 18 26(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.40 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01099 DRAVPe01099.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2311.64 C109H155N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -3.33 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01100 SWLRDVWDWICTVLTDFK 18 27(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=3.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01100 DRAVPe01100.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2283.63 C108H155N25O28S AEGHMNPQY DW 4.43 2 3 -1 4 9 11.11 -2108 1.9 hour >20 hour >10 hour 97.22 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01101 SWLRDVWDWVCTILTDFK 18 28(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01101 DRAVPe01101.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2283.63 C108H155N25O28S AEGHMNPQY DW 4.43 2 3 -1 4 9 11.11 -2108 1.9 hour >20 hour >10 hour 97.22 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01102 DWLRIIWDWVCSVVSDFK 18 29(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.55 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01102 DRAVPe01102.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2267.63 C108H155N25O27S AEGHMNPQTY DVW 4.43 2 3 -1 3 10 41.67 -1530 1.1 hour 3 min >10 hour 113.33 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01103 SWLWEVWDWVLHVLSDFK 18 30(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01103 DRAVPe01103.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2345.68 C117H157N25O27 ACGIMNPQRTY W 4.53 2 3 -1 2 11 22.22 -208 1.9 hour >20 hour >10 hour 113.33 22000 1294.12 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01104 TWLRAIWDWVCTALTDFK 18 31(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=7.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01104 DRAVPe01104.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2225.59 C106H153N25O26S EGHMNPQSY TW 5.62 2 2 0 4 10 27.78 -1195 7.2 hour >20 hour >10 hour 92.22 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01105 SWLRDVWDWVCTVLSDFK 18 32(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=3.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01105 DRAVPe01105.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2255.58 C106H151N25O28S AEGHIMNPQY DVW 4.43 2 3 -1 4 9 8.89 -2279 1.9 hour >20 hour >10 hour 91.67 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01106 SWLRDIWDWISEVLSDFK 18 33[11S](derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=13.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01106 DRAVPe01106.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2295.58 C109H155N25O30 ACGHMNPQTY DSW 4.23 2 4 -2 3 9 -21.67 -2995 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01107 SWLRDIWDWIREVLSDFK 18 34[11R](derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=12.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01107 DRAVPe01107.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2364.69 C112H162N28O29 ACGHMNPQTY DW 4.68 3 4 -1 2 9 -42.22 -4147 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01108 SWLRDIWDWIEEVLSDFK 18 35[11E](derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=13.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01108 DRAVPe01108.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2337.62 C111H157N25O31 ACGHMNPQTY DW 4.1 2 5 -3 2 9 -36.67 -3336 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01109 SWLDDIWDWICEVLSDFE 18 36(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01109 DRAVPe01109.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2271.48 C106H143N21O33S AGHKMNPQRTY D 3.25 0 6 -6 3 9 4.44 -2033 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01110 SWLRDIWDWICKVLSDFK 18 38(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=6.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01110 DRAVPe01110.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2310.7 C110H160N26O27S AEGHMNPQTY DW 5.76 3 3 0 3 9 -5.56 -2401 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01111 SWLDRIWRWICKVLSRFE 18 39(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01111 DRAVPe01111.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2393.84 C113H169N31O25S AGHMNPQTY RW 9.49 4 2 2 3 9 -14.44 -3767 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01112 SWLRDIWRWICKVLSRFK 18 40(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.84 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01112 DRAVPe01112.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2392.9 C114H174N32O23S AEGHMNPQTY RW 10.92 5 1 4 3 9 -16.67 -3641 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01113 SWLRRIWRWICKVLSRFK 18 41(derived from HCV C5A) Synthetic construct(derived from HCV non-structural protein 5A) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT-QPCR assay [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.89 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01113 DRAVPe01113.cif Linear Free Free None L membrane "The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation." 2434 C116H181N35O21S ADEGHMNPQTY R 12.01 6 0 6 3 9 -22.22 -4261 1.9 hour >20 hour >10 hour 102.78 16500 970.59 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. "Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV." A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. 10.1073/pnas.0712380105 Anti-HCV DRAVPe01114 RTQRRGRTGRGKPGIYR 17 HCVA(1484-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26664 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=27.1±2.4 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=37.1±3.9 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=49.8±4.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01114 DRAVPe01114.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 2015.31 C83H147N37O22 ACDEFHLMNSVW R 12.3 7 0 7 7 1 -210.59 -9721 1 hour 2 min 2 min 22.94 1490 93.13 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01115 STQRRGRTGRGRRGIYR 17 HCVB(1484-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=24.3±1.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=33.6±3.5 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=47.2±4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01115 DRAVPe01115.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 2033.29 C81H145N39O23 ACDEFHKLMNPVW R 12.4 7 0 7 8 1 -209.41 -10998 1.9 hour >20 hour >10 hour 22.94 1490 93.13 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01116 RRGRTGRGRRGIYR 14 HCV(1487-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=0.2±0.01 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=2.7±0.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=21.1±2.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01116 DRAVPe01116.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1716.98 C69H125N35O17 ACDEFHKLMNPQSVW R 12.4 7 0 7 6 1 -218.57 -9847 1 hour 2 min 2 min 27.86 1490 114.62 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01117 RTGRGRRGIYR 11 HCV(1490-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=34.6±3.2 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=106±6.1 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=322±9.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01117 DRAVPe01117.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1347.55 C55H98N26O14 ACDEFHKLMNPQSVW R 12.18 5 0 5 5 1 -192.73 -6957 1 hour 2 min 2 min 35.45 1490 149 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01118 RGRRGIYR 8 HCV(1493-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=313±11.3 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=397±10.6 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01118 DRAVPe01118.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1033.2 C43H76N20O10 ACDEFHKLMNPQSTVW R 12 4 0 4 3 1 -195 -5302 1 hour 2 min 2 min 48.75 1490 212.86 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01119 RGIYR 5 HCV(1496-1500) Synthetic construct(derived from HCV NS3 helicase protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01119 DRAVPe01119.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 663.78 C29H49N11O7 ACDEFHKLMNPQSTVW R 10.84 2 0 2 2 1 -124 -2412 1 hour 2 min 2 min 78 1490 372.5 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01120 SQVGD 5 WNV(1968-1972) Synthetic construct(derived from WNV NS3 helicase protein) P06935 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01120 DRAVPe01120.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 504.5 C19H32N6O10 ACEFHIKLMNPRTWY DGQSV 3.8 0 1 -1 2 1 -80 -1268 1.9 hour >20 hour >10 hour 58 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01121 RNPSQVGD 8 WNV(1965-1972) Synthetic construct(derived from WNV NS3 helicase protein) P06935 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=383±12.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=437±13.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01121 DRAVPe01121.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 871.91 C34H57N13O14 ACEFHIKLMTWY DGNPQRSV 5.84 1 1 0 3 1 -170 -3424 1 hour 2 min 2 min 36.25 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01122 RIGRNPSQVGD 11 WNV(1962-1972) Synthetic construct(derived from WNV NS3 helicase protein) P06935 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=417±17.6 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=285±8.1 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=334±12.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01122 DRAVPe01122.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1198.3 C48H83N19O17 ACEFHKLMTWY GR 9.6 2 1 1 4 2 -127.27 -4330 1 hour 2 min 2 min 61.82 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01123 RRGRIGRNPSQVGD 14 WNV(1959-1972) Synthetic construct(derived from WNV NS3 helicase protein) P06935 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=169±6.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=156±6.9 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=191±7.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01123 DRAVPe01123.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1567.73 C62H110N28O20 ACEFHKLMTWY R 12 4 1 3 5 2 -167.14 -7220 1 hour 2 min 2 min 48.57 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01124 AAQRRGRIGRNPSQVGD 17 WNV(1956-1972) Synthetic construct(derived from WNV NS3 helicase protein) P06935 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=358±13.2 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01124 DRAVPe01124.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1838.02 C73H128N32O24 CEFHKLMTWY R 12 4 1 3 5 4 -137.06 -7412 4.4 hour >20 hour >10 hour 51.76 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01125 NQVGD 5 JEV(1971-1975) Synthetic construct(derived from JEV NS3 helicase protein) P27395 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01125 DRAVPe01125.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 531.52 C20H33N7O10 ACEFHIKLMPRSTWY DGNQV 3.8 0 1 -1 2 1 -134 -1592 1.4 hour 3 min >10 hour 58 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01126 RNPNQVGD 8 JEV(1968-1975) Synthetic construct(derived from JEV NS3 helicase protein) P27395 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01126 DRAVPe01126.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 898.93 C35H58N14O14 ACEFHIKLMSTWY N 5.84 1 1 0 3 1 -203.75 -3748 1 hour 2 min 2 min 36.25 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01127 RVGRNPNQVGD 11 JEV(1965-1975) Synthetic construct(derived from JEV NS3 helicase protein) P27395 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=374±12.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=448±14.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01127 DRAVPe01127.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1211.3 C48H82N20O17 ACEFHIKLMSTWY GNRV 9.6 2 1 1 4 2 -154.55 -4742 1 hour 2 min 2 min 52.73 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01128 RRGRVGRNPNQVGD 14 JEV(1962-1975) Synthetic construct(derived from JEV NS3 helicase protein) P27395 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=196±9.4 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=215±7.2 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=253±6.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01128 DRAVPe01128.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1580.73 C62H109N29O20 ACEFHIKLMSTWY R 12 4 1 3 5 2 -188.57 -7632 1 hour 2 min 2 min 41.43 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01129 AAQRRGRVGRNPNQVGD 17 JEV(1959-1975) Synthetic construct(derived from JEV NS3 helicase protein) P27395 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,WNV,JEV" Flaviviridae Helicase assay [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=442±17.7 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01129 DRAVPe01129.cif Linear Free Free None L NTPase/helicase "The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism." 1851.02 C73H127N33O24 CEFHIKLMSTWY R 12 4 1 3 5 4 -154.71 -7824 4.4 hour >20 hour >10 hour 45.88 0 0 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  "Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A." Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). 10.1016/j.bcp.2008.03.018 "Anti-HCV,Anti-WNV,Anti-JEV" DRAVPe01130 TTPKFTVAWDWVPKR 15 gB64(gB346-360) Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=85 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01130 DRAVPe01130.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1832.14 C88H130N22O21 CEGHILMNQSY T 9.99 3 1 2 3 6 -66 -2492 7.2 hour >20 hour >10 hour 45.33 11000 785.71 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01131 KTTSSIEFARLQFTY 15 gB94(496-510) Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "beta-galactosidase activity(Comprehensive antiviral assay,Virus inactivation assay,cell protection assay,entry assay,attachment assay)" [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=6.5±1.3 µM);inhibition of virus entry in Vero cells(EC50>200 µM);inhibition of virus infection in Vero cells(EC50=165.0±71.9 µM);ability of inactive virus(EC50=125±11.4 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. DRAVPe01131 DRAVPe01131.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1792.02 C82H126N20O25 CDGHMNPVW T 8.59 2 1 1 6 5 -31.33 -2986 1.3 hour 3 min 2 min 58.67 1490 106.43 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01132 GHRRYFTFGGGYVYF 15 gB122(636-650) Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae "beta-galactosidase activity(Comprehensive antiviral assay,Virus inactivation assay,cell protection assay,entry assay,attachment assay)" [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=15.0±2.2 µM);inhibition of virus entry in Vero cells(EC50=17.6±2.6 µM);inhibition of virus infection in Vero cells(EC50=71.5±17.4 µM);ability of inactive virus(EC50=118±11.6 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. DRAVPe01132 DRAVPe01132.cif Linear Free Free None L Not found "It is also possible that gB122 could either prematurely trigger or inhibit a conformational change in the gB-1 molecule required for entry,and may be acting by blocking a protein-protein interaction." 1827.03 C89H115N23O20 ACDEIKLMNPQSW G 9.7 3 0 3 8 4 -38.67 -2075 30 hour >20 hour >10 hour 19.33 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01133 HEVVPLEVYTRHEIK 15 gB131(681-695) Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae "beta-galactosidase activity(Comprehensive antiviral assay,Virus inactivation assay,cell protection assay,entry assay,attachment assay)" [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=18.7±2.70 µM);inhibition of virus entry in Vero cells(EC50=12.2±6.56 µM);inhibition of virus infection in Vero cells(EC50>200 µM);ability of inactive virus(EC50>200 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. DRAVPe01133 DRAVPe01133.cif Linear Free Free None L Not found The gB131 peptide could be interfering with a conformational change involving interactions between residues in this region or by blocking a binding interaction. 1849.12 C84H133N23O24 ACDFGMNQSW EV 6.02 4 3 1 2 5 -53.33 -3097 3.5 hour 10 min >10 hour 110 1490 106.43 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01134 HRRYFTFGGGYVYF 14 gB122(637-650) Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=31.2 ± 5.1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01134 DRAVPe01134.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1769.98 C87H112N22O19 ACDEIKLMNPQSW FGY 9.7 3 0 3 7 4 -38.57 -2169 3.5 hour 10 min >10 hour 20.71 4470 343.85 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01135 GHRAYFTFGGGYVYF 15 gB122R4A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=26.4 ± 13.5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01135 DRAVPe01135.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1741.93 C86H108N20O20 CDEIKLMNPQSW G 8.5 2 0 2 8 5 3.33 -402 30 hour >20 hour >10 hour 26 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01136 GHRRAFTFGGGYVYF 15 gB122Y5A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=119.2 ± 26.6 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01136 DRAVPe01136.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1734.94 C83H111N23O19 CDEIKLMNPQSW G 9.99 3 0 3 7 5 -18 -1880 30 hour >20 hour >10 hour 26 2980 212.86 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01137 GHRRYATFGGGYVYF 15 gB122F6A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=67.6 ± 8.1 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01137 DRAVPe01137.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1750.94 C83H111N23O20 CDEIKLMNPQSW G 9.7 3 0 3 8 4 -45.33 -2192 30 hour >20 hour >10 hour 26 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01138 GHRRYFTAGGGYVYF 15 gB122F8A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=37.5 ± 4.2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01138 DRAVPe01138.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1750.94 C83H111N23O20 CDEIKLMNPQSW G 9.7 3 0 3 8 4 -45.33 -2192 30 hour >20 hour >10 hour 26 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01139 GHRRYFTFGAGYVYF 15 gB122G10L Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=25.1 ± 4.9 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01139 DRAVPe01139.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1841.06 C90H117N23O20 CDEIKLMNPQSW FGY 9.7 3 0 3 7 5 -24 -1988 30 hour >20 hour >10 hour 26 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01140 GHRRYFTFGGGYVAF 15 gB122Y14A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=58.0 ± 5.2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01140 DRAVPe01140.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1734.94 C83H111N23O19 CDEIKLMNPQSW G 9.99 3 0 3 7 5 -18 -1880 30 hour >20 hour >10 hour 26 2980 212.86 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01141 GHRRYFTFGGGYVYA 15 gB122F15A Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=48.6 ± 6.2 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01141 DRAVPe01141.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1750.94 C83H111N23O20 CDEIKLMNPQSW G 9.7 3 0 3 8 4 -45.33 -2192 30 hour >20 hour >10 hour 26 4470 319.29 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01142 RYFTFGGGYVYF 12 gB122Δ1-3 Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=34.9 ± 1.8 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01142 DRAVPe01142.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1476.65 C75H93N15O17 ACDEHIKLMNPQSW FGY 8.5 1 0 1 7 4 19.17 -211 1 hour 2 min 2 min 24.17 4470 406.36 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01143 TFGGGYVYF 9 gB122Δ1-6 Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01143 DRAVPe01143.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1010.11 C51H63N9O13 ACDEHIKLMNPQRSW G 5.18 0 0 0 6 3 58.89 997 7.2 hour >20 hour >10 hour 32.22 2980 372.5 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01144 GHRRYFTFGGGY 12 gB122Δ13-15 Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=91.4± 9.8 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01144 DRAVPe01144.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1417.55 C66H88N20O16 ACDEIKLMNPQSVW G 9.99 3 0 3 7 2 -95.83 -2763 30 hour >20 hour >10 hour 0 2980 270.91 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01145 GHRRYFTFG 9 gB122Δ10-15 Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae beta-galactosidase activity(Comprehensive antiviral assay) [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01145 DRAVPe01145.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1140.27 C53H73N17O12 ACDEIKLMNPQSVW FGR 10.84 3 0 3 4 2 -104.44 -2937 30 hour >20 hour >10 hour 0 1490 186.25 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe01146 MDVNPTLLFLKVPAQNAISTTFPYT 25 FluA-PB1(1-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=1.80 ±0.49 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01146 DRAVPe01146.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 2782.25 C129H201N29O37S CEGHRW T 5.59 1 1 0 8 10 31.2 -722 30 hour >20 hour >10 hour 93.6 1490 62.08 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01147 VNPTLLFLKVPAQNAISTTFPYT 23 FluA-PB1(3-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=661.77 ±22.08 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01147 DRAVPe01147.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 2535.97 C120H187N27O33 CDEGHMRW T 8.56 1 0 1 8 10 40.87 -85 100 hour >20 hour >10 hour 101.74 1490 67.73 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01148 PTLLFLKVPAQNAISTTFPYT 21 FluA-PB1(5-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=483.20 ±51.98 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01148 DRAVPe01148.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 2322.73 C111H172N24O30 CDEGHMRW T 9.01 1 0 1 7 9 41.43 175 >20 hour >20 hour ? 97.62 1490 74.5 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01149 LLFLKVPAQNAISTTFPYT 19 FluA-PB1(7-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01149 DRAVPe01149.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 2124.51 C102H158N22O27 CDEGHMRW LT 8.59 1 0 1 6 9 57.89 432 5.5 hour 3 min 2 min 107.89 1490 82.78 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01150 FLKVPAQNAISTTFPYT 17 FluA-PB1(9-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01150 DRAVPe01150.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1898.19 C90H136N20O25 CDEGHMRW T 8.59 1 0 1 6 7 20 -552 1.1 hour 3 min 2 min 74.71 1490 93.13 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01151 KVPAQNAISTTFPYT 15 FluA-PB1(11-25) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01151 DRAVPe01151.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1637.85 C75H116N18O23 CDEGHLMRW T 8.59 1 0 1 6 5 -21.33 -1342 1.3 hour 3 min 2 min 58.67 1490 106.43 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01152 MDVNPTLLFLKVPAQNAIST 20 FluA-PB1(1-20) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=33.80 ±5.53 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01152 DRAVPe01152.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 2172.57 C98H162N24O29S CEGHRWY L 5.59 1 1 0 5 9 46.5 -492 30 hour >20 hour >10 hour 117 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01153 MDVNPTLLFLKVPAQNAI 18 FluA-PB1(1-18) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=29.45 ±5.16 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01153 DRAVPe01153.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1984.38 C91H150N22O25S CEGHRSWY L 5.59 1 1 0 3 9 60 105 30 hour >20 hour >10 hour 130 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01154 MDVNPTLLFLKVPAQN 16 FluA-PB1(1-16) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=45.86 ±4.22 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01154 DRAVPe01154.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1800.15 C82H134N20O23S CEGHIRSWY L 5.59 1 1 0 3 7 28.13 -568 30 hour >20 hour >10 hour 115.63 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01155 MDVNPTLLFLKVPA 14 FluA-PB1(1-14) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=34.53±2.19 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01155 DRAVPe01155.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1557.91 C73H120N16O19S CEGHIQRSWY L 5.59 1 1 0 2 7 82.14 650 30 hour >20 hour >10 hour 132.14 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01156 MDVNPTLLFLKVP 13 FluA-PB1(1-13) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=138.17 ±7.88 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01156 DRAVPe01156.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1486.83 C70H115N15O18S ACEGHIQRSWY L 5.59 1 1 0 2 6 74.62 469 30 hour >20 hour >10 hour 134.62 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01157 MDVNPTLLFLKV 12 FluA-PB1(1-12) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=643.93 ±180.75 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01157 DRAVPe01157.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1389.72 C65H108N14O17S ACEGHIQRSWY L 5.59 1 1 0 2 6 94.17 469 30 hour >20 hour >10 hour 145.83 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01158 MDVNPTLLFLK 11 FluA-PB1(1-11) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=899.53 ±54.31 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01158 DRAVPe01158.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1290.58 C60H99N13O16S ACEGHIQRSWY L 5.59 1 1 0 2 5 64.55 65 30 hour >20 hour >10 hour 132.73 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01159 MDVNPTLLFL 10 FluA-PB1(1-10) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01159 DRAVPe01159.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1162.41 C54H87N11O15S ACEGHIKQRSWY L 3.8 0 1 -1 2 5 110 620 30 hour >20 hour >10 hour 146 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01160 MDVNPTLLF 9 FluA-PB1(1-9) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01160 DRAVPe01160.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1049.25 C48H76N10O14S ACEGHIKQRSWY L 3.8 0 1 -1 2 4 80 128 30 hour >20 hour >10 hour 118.89 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01161 MDVNPTLL 8 FluA-PB1(1-8) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01161 DRAVPe01161.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 902.07 C39H67N9O13S ACEFGHIKQRSWY L 3.8 0 1 -1 2 3 55 -170 30 hour >20 hour >10 hour 133.75 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01162 MDVNPTL 7 FluA-PB1(1-7) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01162 DRAVPe01162.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 788.91 C33H56N8O12S ACEFGHIKQRSWY DLMNPTV 3.8 0 1 -1 2 2 8.57 -662 30 hour >20 hour >10 hour 97.14 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01163 MDVNPT 6 FluA-PB1(1-6) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01163 DRAVPe01163.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 675.75 C27H45N7O11S ACEFGHIKLQRSWY DMNPTV 3.8 0 1 -1 2 1 -53.33 -1154 30 hour >20 hour >10 hour 48.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01164 MDVNPTLLFLKVPAQ 15 FluA-PB1(1-15) Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=43.32 ±5.31nM);##Influenza B(FluB):inhibition of PA-binding activity and virus replication(IC50>3000nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01164 DRAVPe01164.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1686.04 C78H128N18O21S CEGHIRSWY L 5.59 1 1 0 2 7 53.33 96 30 hour >20 hour >10 hour 123.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01165 MNINPYPLFIDVPIQ 15 PB1-1-15 B Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=45.0 ±12.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01165 DRAVPe01165.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1774.11 C84H128N18O22S ACEGHKRSTW IP 3.8 0 1 -1 3 6 40.67 137 30 hour >20 hour >10 hour 123.33 1490 106.43 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01166 MNINPTLLFLKVPIQ 15 "PB1-1-15 A D2N,V3I,L14I" Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=6.69 ±1.73 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01166 DRAVPe01166.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1741.16 C82H137N19O20S ACDEGHRSWY L 8.5 1 0 1 3 7 73.33 703 30 hour >20 hour >10 hour 149.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01167 MDVNPTLLFIDVPAQ 15 "PB1-1-15 A L10I,K11D" Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01167 DRAVPe01167.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1672.96 C76H121N17O23S CEGHKRSWY DLPV 3.56 0 2 -2 2 7 60.67 -221 30 hour >20 hour >10 hour 123.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01168 MNINPTLLFLKVPAQ 15 "PB1-1-15 A D2N,V3I" Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=12.96 ±3.98 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01168 DRAVPe01168.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1699.08 C79H131N19O20S CDEGHRSWY L 8.5 1 0 1 3 7 55.33 392 30 hour >20 hour >10 hour 130 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01169 MDVNPYFLFLKVPAQ 15 "PB1-1-15 A T6Y,L7F" Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=7.51 ±0.71 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=345.0 ±81.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01169 DRAVPe01169.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1782.13 C86H128N18O21S CEGHIRSTW FLPV 5.59 1 1 0 2 7 42.67 145 30 hour >20 hour >10 hour 97.33 1490 106.43 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01170 MDVNPTFLFLKVPAQ 15 PB1-1-15 A L7F Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01170 DRAVPe01170.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1720.06 C81H126N18O21S CEGHIRSWY FLPV 5.59 1 1 0 2 7 46.67 -98 30 hour >20 hour >10 hour 97.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01171 MDVNPYLLFLKVPAQ 15 PB1-1-15 A T6Y Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=21.64 ±1.48 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=107.1 ±31.3 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01171 DRAVPe01171.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1748.11 C83H130N18O21S CEGHIRSTW L 5.59 1 1 0 2 7 49.33 339 30 hour >20 hour >10 hour 123.33 1490 106.43 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01172 MDVNPFLLFLKVPAQ 15 PB1-1-15 A T6F Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=2.84 ±0.48 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=750.4 ±249.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01172 DRAVPe01172.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1732.11 C83H130N18O20S CEGHIRSTWY L 5.59 1 1 0 1 8 76.67 651 30 hour >20 hour >10 hour 123.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01173 MDVNPWLLFLKVPAQ 15 PB1-1-15 A T6W Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=3.40 ±0.51 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=628.3 ±389.1 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01173 DRAVPe01173.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1771.15 C85H131N19O20S CEGHIRSTY L 5.59 1 1 0 1 8 52 586 30 hour >20 hour >10 hour 123.33 5500 392.86 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01174 MDVNPHLLFLKVPAQ 15 PB1-1-15 A T6H Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=292.16 ±34.04 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01174 DRAVPe01174.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1722.08 C80H128N20O20S CEGIRSTWY L 6.5 2 1 1 1 7 36.67 -113 30 hour >20 hour >10 hour 123.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01175 MDVNPCLLFLKVPAQ 15 PB1-1-15 A T6C Synthetic construct(derived from INFV A polymerase (PB1)) Q6DNS6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A Orthomyxoviridae ELISA [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=43.58 ±5.67 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01175 DRAVPe01175.cif Linear Free Free None L PA subunit "Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication." 1688.08 C77H126N18O20S2 EGHIRSTWY L 5.59 1 1 0 2 7 74.67 481 30 hour >20 hour >10 hour 123.33 0 0 19841738 PLoS One. 2009 Oct 20;4(10):e7517. "Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M." Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  10.1371/journal.pone.0007517 Anti-Influenza A DRAVPe01176 GWWYKGRARPVSAVA 15 18-c01 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H3N2,H1N1" Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=3.2 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01176 DRAVPe01176.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1703.97 C80H118N24O18 CDEFHILMNQT A 11 3 0 3 4 7 -36 -1888 30 hour >20 hour >10 hour 58.67 12490 892.14 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y "Anti-H3N2,Anti-H1N1" DRAVPe01177 RAVWRHSVATPSHSV 15 C18-c03 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H3N2,H1N1" Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=6.5 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=68 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01177 DRAVPe01177.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1689.9 C74H116N26O20 CDEFGIKLMNQY SV 12 4 0 4 4 6 -32 -3386 1 hour 2 min 2 min 71.33 5500 392.86 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y "Anti-H3N2,Anti-H1N1" DRAVPe01178 GAWYKGRARPVSAVA 15 C18-c01W2A Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None H1N1 Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=53 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01178 DRAVPe01178.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1588.83 C72H113N23O18 CDEFHILMNQT A 11 3 0 3 4 7 -18 -1940 30 hour >20 hour >10 hour 65.33 6990 499.29 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y Anti-H1N1 DRAVPe01179 GWWYKGRARAVSAVA 15 C18-c01P10A Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None H1N1 Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=89 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01179 DRAVPe01179.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1677.93 C78H116N24O18 CDEFHILMNPQT A 11 3 0 3 4 8 -13.33 -1707 30 hour >20 hour >10 hour 65.33 12490 892.14 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y Anti-H1N1 DRAVPe01180 AVASVPRARGKYWWG 15 C18-c01r Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H3N2,H1N1" Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=44 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=17 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01180 DRAVPe01180.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1703.97 C80H118N24O18 CDEFHILMNQT A 11 3 0 3 4 7 -36 -1888 4.4 hour >20 hour >10 hour 58.67 12490 892.14 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y "Anti-H3N2,Anti-H1N1" DRAVPe01181 DFRRLPGAFWQLRQP 15 C18-p1b Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H3N2,H1N1" Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=52 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=19 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01181 DRAVPe01181.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1887.18 C88H131N27O20 CEHIKMNSTVY R 11.7 3 1 2 1 6 -90 -4368 1.1 hour 3 min >10 hour 58.67 5500 392.86 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y "Anti-H3N2,Anti-H1N1" DRAVPe01182 AETVESCLAKPHTEN 15 C18-cp3c Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H3N2,H1N1" Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=66 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01182 DRAVPe01182.cif Linear Alkylated(C18) Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1628.77 C67H109N19O26S DFGIMQRWY E 4.75 2 3 -1 5 4 -72 -3196 4.4 hour >20 hour >10 hour 58.67 0 0 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y "Anti-H3N2,Anti-H1N1" DRAVPe01183 GWWYKGRARPVSAVA 15 c01 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None H1N1 Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01183.cif Linear Free Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1703.97 C80H118N24O18 CDEFHILMNQT A 11 3 0 3 4 7 -36 -1888 30 hour >20 hour >10 hour 58.67 12490 892.14 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y Anti-H1N1 DRAVPe01184 RAVWRHSVATPSHSV 15 c03 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None H1N1 Orthomyxoviridae Plaque assay [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01184.cif Linear Free Amidation None L sialylgalactose The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. 1689.9 C74H116N26O20 CDEFGIKLMNQY SV 12 4 0 4 4 6 -32 -3386 1 hour 2 min 2 min 71.33 5500 392.86 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. "Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T." Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  10.1021/jm801570y Anti-H1N1 DRAVPe01185 RRKKAAVALLPAVLLALLAP 20 EB Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay "[Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(95 ± 2% inhibition at 10 μM,EC50=3.2 ± 0.0 μM)." [Ref.21220525]Did not lyse red blood cells up to 30 μM. [Ref.21220525]A549 cells:CD50=83.5 ± 22.0 μM;##MDCK cells:CD50=85.5 ± 1.3 μM. DRAVPe01185 DRAVPe01185.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 2084.67 C98H178N28O21 CDEFGHIMNQSTWY AL 12.02 4 0 4 0 14 110 752 1 hour 2 min 2 min 176 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1689 Anti-Influenza virus DRAVPe01186 RRKKAAVALLPAVLLALLA 19 A2 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 2% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01186 DRAVPe01186.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1987.55 C93H171N27O20 CDEFGHIMNQSTWY AL 12.02 4 0 4 0 14 124.21 752 1 hour 2 min 2 min 185.26 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1690 Anti-Influenza virus DRAVPe01187 RRKKAAVALLPAVLLALL 18 A3 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(95 ± 2% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01187 DRAVPe01187.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1916.47 C90H166N26O19 CDEFGHIMNQSTWY L 12.02 4 0 4 0 13 121.11 571 1 hour 2 min 2 min 190 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1691 Anti-Influenza virus DRAVPe01188 RRKKAAVALLPAVLLAL 17 A4 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(89 ± 3% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01188 DRAVPe01188.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1803.31 C84H155N25O18 CDEFGHIMNQSTWY AL 12.02 4 0 4 0 12 105.88 79 1 hour 2 min 2 min 178.24 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1692 Anti-Influenza virus DRAVPe01189 RRKKAAVALLPAVLLA 16 A5 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(96 ±32% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01189 DRAVPe01189.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1690.15 C78H144N24O17 CDEFGHIMNQSTWY A 12.02 4 0 4 0 11 88.75 -413 1 hour 2 min 2 min 165 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1693 Anti-Influenza virus DRAVPe01190 RRKKAAVALLP 11 A10 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(4 ±8% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01190 DRAVPe01190.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1222.54 C55H103N19O12 CDEFGHIMNQSTWY A 12.02 4 0 4 0 6 -10.91 -2163 1 hour 2 min 2 min 124.55 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1698 Anti-Influenza virus DRAVPe01191 RRKKAVALLPAVLLALLAP 19 B6 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 6% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01191 DRAVPe01191.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 2013.59 C95H173N27O20 CDEFGHIMNQSTWY L 12.02 4 0 4 0 13 106.32 571 1 hour 2 min 2 min 180 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1706 Anti-Influenza virus DRAVPe01192 RRKKVALLPAVLLALLAP 18 B7 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 4% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01192 DRAVPe01192.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1942.51 C92H168N26O19 CDEFGHIMNQSTWY L 12.02 4 0 4 0 12 102.22 390 1 hour 2 min 2 min 184.44 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1707 Anti-Influenza virus DRAVPe01193 RRKKALLPAVLLALLAP 17 B8 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 3% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01193 DRAVPe01193.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1843.38 C87H159N25O18 CDEFGHIMNQSTWY L 12.02 4 0 4 0 11 83.53 -14 1 hour 2 min 2 min 178.24 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1708 Anti-Influenza virus DRAVPe01194 RRKKLLPAVLLALLAP 16 B9 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 4% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01194 DRAVPe01194.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1772.3 C84H154N24O17 CDEFGHIMNQSTWY L 12.02 4 0 4 0 10 77.5 -195 1 hour 2 min 2 min 183.13 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1709 Anti-Influenza virus DRAVPe01195 RRKKLPAVLLALLAP 15 B10 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(94 ± 4% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01195 DRAVPe01195.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1659.14 C78H143N23O16 CDEFGHIMNQSTWY L 12.02 4 0 4 0 9 57.33 -687 1 hour 2 min 2 min 169.33 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1710 Anti-Influenza virus DRAVPe01196 RRKKPAVLLALLAP 14 B11 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(96 ± 0% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01196 DRAVPe01196.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1545.98 C72H132N22O15 CDEFGHIMNQSTWY L 12.02 4 0 4 0 8 34.29 -1179 1 hour 2 min 2 min 153.57 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1006 Anti-Influenza virus DRAVPe01197 RRKKAVLLALLAP 13 B12 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(97 ± 2% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01197 DRAVPe01197.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1448.86 C67H125N21O14 CDEFGHIMNQSTWY L 12.02 4 0 4 0 8 49.23 -1179 1 hour 2 min 2 min 165.38 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 Anti-Influenza virus DRAVPe01198 RRKKVLLALLAP 12 C1 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(40 ±19 % inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01198 DRAVPe01198.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1377.78 C64H120N20O13 CDEFGHIMNQSTWY L 12.02 4 0 4 0 7 38.33 -1360 1 hour 2 min 2 min 170.83 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1711 Anti-Influenza virus DRAVPe01199 RRKKAAVALLAVLLALLA 18 EBNP(EB without prolines) Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=3.0 ± 0.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01199 DRAVPe01199.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1890.43 C88H164N26O19 CDEFGHIMNPQSTWY AL 12.02 4 0 4 0 14 140 752 1 hour 2 min 2 min 195.56 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1721 Anti-Influenza virus DRAVPe01200 RRKKVALLAVLLALLA 16 B7NP(B7 without prolines) Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=0.3 ± 0.1 μM). [Ref.21220525]>50% hemolysis agaisnt human red blood cells at 30 μM. [Ref.21220525]A549 cells:CD50=126.3± 23.0 μM;##MDCK cells:CD50=105.3 ± 8.0 μM. DRAVPe01200 DRAVPe01200.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1748.28 C82H154N24O17 CDEFGHIMNPQSTWY L 12.02 4 0 4 0 12 135 390 1 hour 2 min 2 min 207.5 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1720 Anti-Influenza virus DRAVPe01201 RRKKALLAVLLALLA 15 B8NP Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=0.4 ± 0.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01201 DRAVPe01201.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1649.14 C77H145N23O16 CDEFGHIMNPQSTWY L 12.02 4 0 4 0 11 116 -14 1 hour 2 min 2 min 202 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 Anti-Influenza virus DRAVPe01202 RRKKLLAVLLALLA 14 B9NP Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=3.1 ± 0.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01202 DRAVPe01202.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1578.06 C74H140N22O15 CDEFGHIMNPQSTWY L 12.02 4 0 4 0 10 111.43 -195 1 hour 2 min 2 min 209.29 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1722 Anti-Influenza virus DRAVPe01203 RRKKLAVLLALLA 13 B10NP Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Hemagglutinin assay [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=3.5 ± 2.6 μM). [Ref.21220525]Did not lyse human red blood cells up to 30 μM. [Ref.21220525]A549 cells:CD50=120.0 ± 28.0 μM;##MDCK cells:CD50=90.0 ± 16.3 μM. DRAVPe01203 DRAVPe01203.cif Linear Free Free None L Not found The peptide inhibits influenza virus replication by preventing attachment to cells. 1464.9 C68H129N21O14 CDEFGHIMNPQSTWY L 12.02 4 0 4 0 9 90.77 -687 1 hour 2 min 2 min 195.38 0 0 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. "Jones JC, Settles EW, Brandt CR, Schultz-Cherry S. " Identification of the minimal active sequence of an anti-influenza virus peptide.  10.1128/AAC.01428-10 DRAVPa1723 Anti-Influenza virus DRAVPe01204 LFRLIKSLIKRLVSAFK 17 Mucroporin-M1 Synthetic construct(derived from Mucroporin) B9UIY3 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "SARS-CoV,H5N1,MeV" "Coronaviridae, Orthomyxoviridae, Paramyxoviridae" Plaque formation assay [Ref.21620914]measles virus (MeV):inhibition of MeV infection in Vero cells(EC50=7.15 μg/ml (3.52 μM));##SARS-CoV(pseudoviruse):inhibition of SARS-CoV infection in MDCK cells(EC50=14.46 μg/ml (7.12 μM));##H5N1(pseudovirus):inhibition of H5N1 infection in MDCK cells(EC50=2.10 μg/ml (1.03 μM)). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21620914]Vero cells:CC50=70.46μg/ ml(34.70μM);##HeLa-ACE2 cells:CC50=61.58 μg/ml (30.31 μM);##MDCK cells:CC50=83.35 μg/ml (41.03 μM). DRAVPe01204 DRAVPe01204.cif Linear Free Amidation None L membrane "Mucroporin-M1 may bind to the virus envelope by surface charge interactions and inhibits MeV, SARS-CoV and influenza H5N1 by direct virucidal action." 2032.59 C98H170N26O20 CDEGHMNPQTWY L 12.02 5 0 5 2 10 79.41 -1196 5.5 hour 3 min 2 min 160.59 0 0 21620914 Peptides. 2011 Jul;32(7):1518-25. "Li Q, Zhao Z, Zhou D, Chen Y, Hong W, Cao L, Yang J, Zhang Y, Shi W, Cao Z, Wu Y, Yan H, Li W. " "Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses. " 10.1016/j.peptides.2011.05.015 "Anti-SARS-CoV,Anti-H5N1,Anti-MeV" DRAVPe01205 KAKAKAKAKAKAKAKAKAKAK 21 RJ1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=53.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>455 μM. DRAVPe01205 DRAVPe01205.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2138.72 C96H184N32O22 CDEFGHILMNPQRSTVWY K 11 11 0 11 0 10 -118.57 -4295 1.3 hour 3 min 2 min 47.62 0 0 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01206 KAAKKAAKAAKKAAKWAKKAA 21 RJ3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=117.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>467 μM. DRAVPe01206 DRAVPe01206.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2139.66 C98H175N31O22 CDEFGHILMNPQRSTVY A 10.9 9 0 9 0 12 -77.14 -2771 1.3 hour 3 min 2 min 52.38 5500 275 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01207 AKKAAKKAKKAAKKAKKAAKK 21 RJ5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=41.0 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=14.3 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>468 μM. DRAVPe01207 DRAVPe01207.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2195.81 C99H191N33O22 CDEFGHILMNPQRSTVWY K 11.04 12 0 12 0 9 -145.71 -5031 4.4 hour >20 hour >10 hour 42.86 0 0 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01208 AKKAAKKAKKAAKKAKKWAKK 21 RJ6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=47.3 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>433 μM. DRAVPe01208 DRAVPe01208.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2310.95 C107H196N34O22 CDEFGHILMNPQRSTVY K 11.04 12 0 12 0 9 -158.57 -4979 4.4 hour >20 hour >10 hour 38.1 5500 275 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01209 AKKAWKKAKKAAKKAKKWAKK 21 RJ7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=40.8 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=44.9 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>412 μM. DRAVPe01209 DRAVPe01209.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2426.08 C115H201N35O22 CDEFGHILMNPQRSTVY K 11.04 12 0 12 0 9 -171.43 -4927 4.4 hour >20 hour >10 hour 33.33 11000 550 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01210 ARRAWRRARRAARRARRAARR 21 RJ8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=18.2 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=22.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>395 μM. DRAVPe01210 DRAVPe01210.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2647.11 C107H196N58O22 CDEFGHIKLMNPQSTVY R 13.04 12 0 12 0 9 -192.86 -16223 4.4 hour >20 hour >10 hour 38.1 5500 275 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01211 ARRAKRRARRAARRARRKARR 21 RJ9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=13.0 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=46.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>433 μM. DRAVPe01211 DRAVPe01211.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2646.17 C105H205N59O22 CDEFGHILMNPQSTVWY R 13.04 14 0 14 0 7 -234.29 -17747 4.4 hour >20 hour >10 hour 33.33 0 0 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01212 ARRAKRRARRAKRRARRKKRR 21 RJ10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "Plaque reduction assay,ELISA" [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=24.6 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=54.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>422 μM. DRAVPe01212 DRAVPe01212.cif Linear Free Free None L Not found "The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface." 2760.36 C111H219N61O22 CDEFGHILMNPQSTVWY R 13.04 16 0 16 0 5 -288.57 -19219 4.4 hour >20 hour >10 hour 23.81 0 0 15498607 Antiviral Res. 2004 Nov;64(2):119-26. "Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ. " "A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus." 10.1016/j.antiviral.2004.08.003 Anti-HSV DRAVPe01213 QLQKWEDWVRWIGNIPQYLKG 21 Peptide 59(FIV ectodomain 767-786) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.03 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01213 DRAVPe01213.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2658.06 C126H185N33O31 ACFHMST QW 8.5 3 2 1 4 8 -90 -3236 0.8 hour 10 min >10 hour 88.1 17990 899.5 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01214 QKWEDWVRWIGN 12 C12a(FIV ectodomain 768-779) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.25 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.18 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01214 DRAVPe01214.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1616.8 C76H105N21O19 ACFHLMPSTY W 6.07 2 2 0 2 5 -140 -3129 0.8 hour 10 min >10 hour 56.67 16500 1500 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01215 WEDWVRWIGNIP 12 C12b(FIV ectodomain 770-781) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.04 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.09 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01215 DRAVPe01215.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1570.77 C76H103N19O18 ACFHKLMQSTY W 4.37 1 2 -1 2 6 -54.17 -1528 2.8 hour 3 min 2 min 89.17 16500 1500 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01216 QLQKWEDWVRWI 12 C12c(FIV ectodomain 766-777) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.03 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.04 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01216 DRAVPe01216.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1686.93 C81H115N21O19 ACFGHMNPSTY W 6.07 2 2 0 0 6 -105 -2621 0.8 hour 10 min >10 hour 89.17 16500 1500 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01217 WEDWVRWI 8 C8(FIV ectodomain 770-777) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.07 ± 0.02 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.46 ± 0.20 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.05 ± 0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01217 DRAVPe01217.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1189.34 C59H76N14O13 ACFGHKLMNPQSTY W 4.37 1 2 -1 0 5 -68.75 -1450 2.8 hour 3 min 2 min 85 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01218 DWVRWI 6 C6a(FIV ectodomain 772-777) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.15 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.07 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01218 DRAVPe01218.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 874.01 C43H59N11O9 ACEFGHKLMNPQSTY W 5.84 1 1 0 0 4 -18.33 -1002 1.1 hour 3 min >10 hour 113.33 11000 2200 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01219 WEDWVR 6 C6b(FIV ectodomain 770-775) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01219 DRAVPe01219.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 889.97 C42H55N11O11 ACFGHIKLMNPQSTY W 4.37 1 2 -1 0 3 -151.67 -2175 2.8 hour 3 min 2 min 48.33 11000 2200 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01220 WVRWI 5 C5(FIV ectodomain 773-777) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.20 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.11 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01220 DRAVPe01220.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 758.92 C39H54N10O6 ACDEFGHKLMNPQSTY W 9.75 1 0 1 0 4 48 -130 2.8 hour 3 min 2 min 136 11000 2750 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01221 WVRW 4 C4a(FIV ectodomain 773-776) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=36 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=24 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01221 DRAVPe01221.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 645.76 C33H43N9O5 ACDEFGHIKLMNPQSTY W 9.75 1 0 1 0 3 -52.5 -622 2.8 hour 3 min 2 min 72.5 11000 3666.67 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01222 VRWI 4 C4b(FIV ectodomain 774-777) Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=7.80 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=4.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01222 DRAVPe01222.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 572.71 C28H44N8O5 ACDEFGHKLMNPQSTY IRVW 9.72 1 0 1 0 3 82.5 -363 100 hour >20 hour >10 hour 170 5500 1833.33 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01223 AEDWVRWI 8 C8W->A770 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=4.30 ± 0.70 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=2.10± 0.10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01223 DRAVPe01223.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1074.2 C51H71N13O13 CFGHKLMNPQSTY W 4.37 1 2 -1 0 5 -35 -1502 4.4 hour >20 hour >10 hour 97.5 11000 1571.43 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01224 WADWVRWI 8 C8E->A771 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.16 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.22 ± 0.05 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.12 ± 0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610148]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01224 DRAVPe01224.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1131.3 C57H74N14O11 CEFGHKLMNPQSTY W 5.84 1 1 0 0 6 -2.5 -588 2.8 hour 3 min 2 min 97.5 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01225 WEAWVRWI 8 C8D->A772 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.10± 0.02 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.40 ± 0.22 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.03 ± 0.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610149]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01225 DRAVPe01225.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1145.33 C58H76N14O11 CDFGHKLMNPQSTY W 6 1 1 0 0 6 -2.5 -397 2.8 hour 3 min 2 min 97.5 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01226 WEDAVRWI 8 C8W->A773 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610150]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01226 DRAVPe01226.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1074.2 C51H71N13O13 CFGHKLMNPQSTY W 4.37 1 2 -1 0 5 -35 -1502 2.8 hour 3 min 2 min 97.5 11000 1571.43 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01227 WEDWARWI 8 C8V->A774 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.07 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.54 ± 0.02 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.15 ± 0.12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610151]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01227 DRAVPe01227.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1161.28 C57H72N14O13 CFGHKLMNPQSTVY W 4.37 1 2 -1 0 5 -98.75 -1673 2.8 hour 3 min 2 min 61.25 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01228 WEDWVAWI 8 C8G->A775 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.09 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.38 ± 0.04 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.25 ± 0.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610152]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01228 DRAVPe01228.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1104.23 C56H69N11O13 CFGHKLMNPQRSTY W 3.67 0 2 -2 0 6 10 223 2.8 hour 3 min 2 min 97.5 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01229 WEDWVRAI 8 C8W->A776 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610153]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01229 DRAVPe01229.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1074.2 C51H71N13O13 CFGHKLMNPQSTY W 4.37 1 2 -1 0 5 -35 -1502 2.8 hour 3 min 2 min 97.5 11000 1571.43 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01230 WEDWVRWA 8 C8I->A777 Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) P16090 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae enzyme-linked immunosorbent assay(ELISA) [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.15 ± 0.01 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.64± 0.08 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.13 ± 0.04 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12610154]No detectable cytotoxicity on MBM cell viability and proliferation. DRAVPe01230 DRAVPe01230.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1147.26 C56H70N14O13 CFGHIKLMNPQSTY W 4.37 1 2 -1 0 5 -102.5 -1761 2.8 hour 3 min 2 min 48.75 16500 2357.14 12610147 J Virol. 2003 Mar;77(6):3724-33. "Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M." Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. 10.1128/jvi.77.6.3724-3733.2003 Anti-FIV DRAVPe01231 TDVILMCFSIDSPDSLENI 19 77-95(wild type) Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=7.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01231 DRAVPe01231.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2112.39 C91H146N20O33S2 AGHKQRWY DIS 3.37 0 4 -4 6 7 54.21 -1713 7.2 hour >20 hour >10 hour 117.89 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01232 CSIELSDIPLSVDFNTMID 19 77-95(scrambled) Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01232 DRAVPe01232.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2112.39 C91H146N20O33S2 AGHKQRWY DIS 3.37 0 4 -4 6 7 54.21 -1713 1.2 hour >20 hour >10 hour 117.89 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01233 ADVILMCFSIDSPDSLENI 19 77-95[77A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.56 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01233 DRAVPe01233.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2082.37 C90H144N20O32S2 GHKQRTWY DIS 3.37 0 4 -4 5 8 67.37 -1275 4.4 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01234 TAVILMCFSIDSPDSLENI 19 77-95[78A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.37 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01234 DRAVPe01234.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2068.38 C90H146N20O31S2 GHKQRWY IS 3.49 0 3 -3 6 8 82.11 -660 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01235 TDAILMCFSIDSPDSLENI 19 77-95[79A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.60 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01235 DRAVPe01235.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2084.34 C89H142N20O33S2 GHKQRVWY DIS 3.37 0 4 -4 6 7 41.58 -1936 7.2 hour >20 hour >10 hour 107.89 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01236 TDVALMCFSIDSPDSLENI 19 77-95[80A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=11.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01236 DRAVPe01236.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2070.31 C88H140N20O33S2 GHKQRWY DS 3.37 0 4 -4 6 7 40 -2024 7.2 hour >20 hour >10 hour 102.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01237 TDVIAMCFSIDSPDSLENI 19 77-95[81A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=5.42 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01237 DRAVPe01237.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2070.31 C88H140N20O33S2 GHKQRWY DIS 3.37 0 4 -4 6 7 43.68 -2024 7.2 hour >20 hour >10 hour 102.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01238 TDVILACFSIDSPDSLENI 19 77-95[82A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.43 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01238 DRAVPe01238.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2052.28 C89H142N20O33S GHKMQRWY DIS 3.37 0 4 -4 6 8 53.68 -1767 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01239 TDVILMAFSIDSPDSLENI 19 77-95[83A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01239 DRAVPe01239.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2080.33 C91H146N20O33S CGHKQRWY DIS 3.37 0 4 -4 5 8 50.53 -1660 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01240 TDVILMCASIDSPDSLENI 19 77-95[84A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.29 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01240 DRAVPe01240.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2036.3 C85H142N20O33S2 FGHKQRWY DIS 3.37 0 4 -4 6 7 48.95 -1830 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01241 TDVILMCFAIDSPDSLENI 19 77-95[85A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.82 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01241 DRAVPe01241.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2096.39 C91H146N20O32S2 GHKQRWY DI 3.37 0 4 -4 5 8 67.89 -1192 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01242 TDVILMCFSADSPDSLENI 19 77-95[86A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=3.52 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01242 DRAVPe01242.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2070.31 C88H140N20O33S2 GHKQRWY DS 3.37 0 4 -4 6 7 40 -2024 7.2 hour >20 hour >10 hour 102.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01243 TDVILMCFSIASPDSLENI 19 77-95[87A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.36 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01243 DRAVPe01243.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2068.38 C90H146N20O31S2 GHKQRWY IS 3.49 0 3 -3 6 8 82.11 -660 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01244 TDVILMCFSIDAPDSLENI 19 77-95[88A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.26 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01244 DRAVPe01244.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2096.39 C91H146N20O32S2 GHKQRWY DI 3.37 0 4 -4 5 8 67.89 -1192 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01245 TDVILMCFSIDSADSLENI 19 77-95[89A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=15.32 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01245 DRAVPe01245.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2086.36 C89H144N20O33S2 GHKPQRWY DIS 3.37 0 4 -4 6 8 72.11 -1532 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01246 TDVILMCFSIDSPASLENI 19 77-95[90A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.61 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01246 DRAVPe01246.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2068.38 C90H146N20O31S2 GHKQRWY IS 3.49 0 3 -3 6 8 82.11 -660 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01247 TDVILMCFSIDSPDALENI 19 77-95[91A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.19 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01247 DRAVPe01247.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2096.39 C91H146N20O32S2 GHKQRWY DI 3.37 0 4 -4 5 8 67.89 -1192 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01248 TDVILMCFSIDSPDSAENI 19 77-95[92A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.27 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01248 DRAVPe01248.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2070.31 C88H140N20O33S2 GHKQRWY DIS 3.37 0 4 -4 6 7 43.68 -2024 7.2 hour >20 hour >10 hour 102.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01249 TDVILMCFSIDSPDSLANI 19 77-95[93A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=9.83 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01249 DRAVPe01249.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2054.36 C89H144N20O31S2 EGHKQRWY DIS 3.42 0 3 -3 6 8 82.11 -851 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01250 TDVILMCFSIDSPDSLEAI 19 77-95[94A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=18.47 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01250 DRAVPe01250.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2069.37 C90H145N19O32S2 GHKNQRWY DIS 3.37 0 4 -4 5 8 82.11 -868 7.2 hour >20 hour >10 hour 123.16 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01251 TDVILMCFSIDSPDSLENA 19 77-95[95A] Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.89 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01251 DRAVPe01251.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2070.31 C88H140N20O33S2 GHKQRWY DS 3.37 0 4 -4 6 7 40 -2024 7.2 hour >20 hour >10 hour 102.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01252 TDVILMCFSI 10 77-86 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01252 DRAVPe01252.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1141.41 C51H84N10O15S2 AEGHKNPQRWY I 3.8 0 1 -1 3 5 192 1072 7.2 hour >20 hour >10 hour 146 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01253 TDVILMCFSIDSP 13 77–89 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01253 DRAVPe01253.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1440.69 C63H101N13O21S2 AEGHKNQRWY DIS 3.56 0 2 -2 4 5 102.31 -140 7.2 hour >20 hour >10 hour 112.31 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01254 TDVILMCFSIDSPDSL 16 77-92 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=10.86 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01254 DRAVPe01254.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1756.02 C76H122N16O27S2 AEGHKNQRWY DS 3.42 0 3 -3 5 6 80 -860 7.2 hour >20 hour >10 hour 115.63 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01255 DVILMCFSIDSPDSLENI 18 78-95 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.23 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01255 DRAVPe01255.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2011.29 C87H139N19O31S2 AGHKQRTWY DIS 3.37 0 4 -4 5 7 61.11 -1456 1.1 hour 3 min >10 hour 124.44 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01256 VILMCFSIDSPDSLENI 17 79-95 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=16.95 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01256 DRAVPe01256.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1896.2 C83H134N18O28S2 AGHKQRTWY IS 3.49 0 3 -3 5 7 85.29 -584 100 hour >20 hour >10 hour 131.76 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01257 ILMCFSIDSPDSLENI 16 80-95 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=7.17 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01257 DRAVPe01257.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1797.07 C78H125N17O27S2 AGHKQRTVWY IS 3.49 0 3 -3 5 6 64.38 -988 20 hour 30 min >10 hour 121.88 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01258 CFSIDSPDSLENI 13 83-95 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01258 DRAVPe01258.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1439.56 C61H94N14O24S AGHKMQRTVWY S 3.49 0 3 -3 5 4 0.77 -2207 1.2 hour >20 hour >10 hour 90 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01259 ILMCFSIDSPDSLEN 15 80-94 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.75 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01259 DRAVPe01259.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1683.91 C72H114N16O26S2 AGHKQRTVWY S 3.49 0 3 -3 5 5 38.67 -1480 20 hour 30 min >10 hour 104 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01260 ILMCFSIDSPDSLE 14 80-93 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=3.50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01260 DRAVPe01260.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1569.8 C68H108N14O24S2 AGHKNQRTVWY S 3.49 0 3 -3 4 5 66.43 -816 20 hour 30 min >10 hour 111.43 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01261 ILMCFSIDSPDSL 13 80-92 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=12.40 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01261 DRAVPe01261.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1440.69 C63H101N13O21S2 AEGHKNQRTVWY S 3.56 0 2 -2 4 5 98.46 -135 20 hour 30 min >10 hour 120 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01262 ILMCFSIDSPDS 12 80-91 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.36 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01262 DRAVPe01262.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1327.53 C57H90N12O20S2 AEGHKNQRTVWY S 3.56 0 2 -2 4 4 75 -627 20 hour 30 min >10 hour 97.5 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01263 ILMCFSIDSPD 11 80-90 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.61 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01263 DRAVPe01263.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1240.45 C54H85N11O18S2 AEGHKNQRTVWY DIS 3.56 0 2 -2 3 4 89.09 -287 20 hour 30 min >10 hour 106.36 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01264 ILMCFSIDSP 10 80-89 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=35.77 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01264 DRAVPe01264.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1125.36 C50H80N10O15S2 AEGHKNQRTVWY IS 3.8 0 1 -1 3 4 133 585 20 hour 30 min >10 hour 117 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01265 ILMCFSIDS 9 80-88 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01265 DRAVPe01265.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1028.25 C45H73N9O14S2 AEGHKNPQRTVWY IS 3.8 0 1 -1 3 4 165.56 585 20 hour 30 min >10 hour 130 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01266 ILMCFSID 8 80-87 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01266 DRAVPe01266.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 941.17 C42H68N8O12S2 AEGHKNPQRTVWY I 3.8 0 1 -1 2 4 196.25 925 20 hour 30 min >10 hour 146.25 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01267 ILMCFSI 7 80-86 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01267 DRAVPe01267.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 826.08 C38H63N7O9S2 ADEGHKNPQRTVWY I 5.52 0 0 0 2 4 274.29 1797 20 hour 30 min >10 hour 167.14 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01268 ILMCFS 6 80-85 Synthetic construct(derived from RhoA protein) P08134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae viral antigen reduction assay [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01268 DRAVPe01268.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 712.92 C32H52N6O8S2 ADEGHKNPQRTVWY CFILMS 5.52 0 0 0 2 3 245 1305 20 hour 30 min >10 hour 130 0 0 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. "Budge PJ, Lebowitz J, Graham BS. " Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. 10.1128/AAC.47.11.3470-3477.2003 Anti-RSV DRAVPe01269 NGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTA 38 HR1-1(HR1 region 889–926) Synthetic construct(derived from SARS-CoV spike protein) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae luciferase assay [Ref.15184046]HIV-luc/SARS pseudotyped virus:inhibition of virus infection in 293T cells(EC50=0.14 μM);##SARS-CoV(wild-type):inhibition of virus infection in 293T cells(EC50=3.68 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01269 DRAVPe01269.cif Linear Free Free None L membrane "soluble synthesized HR1, HR2 or homologues can bind the exposed HR1 or HR2 region and block the formation of the six-helix bundle, thus inhibiting virus fusion with the target cell." 4153.57 C178H291N51O63 CDHMPRW Q 6.14 2 2 0 16 12 -50.26 -6646 1.4 hour 3 min >10 hour 84.74 1490 40.27 15184046 Biochem Biophys Res Commun. 2004 Jul 2;319(3):746-52. "Yuan K, Yi L, Chen J, Qu X, Qing T, Rao X, Jiang P, Hu J, Xiong Z, Nie Y, Shi X, Wang W, Ling C, Yin X, Fan K, Lai L, Ding M, Deng H." Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein. 10.1016/j.bbrc.2004.05.046 Anti-SARS-CoV DRAVPe01270 IQKEIDRLNEVAKNLNESLIDLQELGK 27 HR2-18(HR2 region 1161–1187) Synthetic construct(derived from SARS-CoV spike protein) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae luciferase assay [Ref.15184046]HIV-luc/SARS pseudotyped virus:inhibition of virus infection in 293T cells(EC50=1.19 μM);##SARS-CoV(wild-type):inhibition of virus infection in 293T cells(EC50=5.22 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01270.cif Linear Free Free None L membrane "soluble synthesized HR1, HR2 or homologues can bind the exposed HR1 or HR2 region and block the formation of the six-helix bundle, thus inhibiting virus fusion with the target cell." 3123.55 C135H232N38O46 CFHMPTWY L 4.66 4 6 -2 5 10 -64.44 -6450 20 hour 30 min >10 hour 130 0 0 15184046 Biochem Biophys Res Commun. 2004 Jul 2;319(3):746-52. "Yuan K, Yi L, Chen J, Qu X, Qing T, Rao X, Jiang P, Hu J, Xiong Z, Nie Y, Shi X, Wang W, Ling C, Yin X, Fan K, Lai L, Ding M, Deng H." Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein. 10.1016/j.bbrc.2004.05.046 Anti-SARS-CoV DRAVPe01271 HRILMRIRQMMT 12 p9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=56.47 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50=473.00 μM. DRAVPe01271 DRAVPe01271.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1586.01 C66H120N24O15S3 ACDEFGKNPSVWY MR 12.3 4 0 4 1 3 -20 -3572 3.5 hour 10 min >10 hour 97.5 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01272 ARILMRIRQMMT 12 1-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=56.12263 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01272 DRAVPe01272.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1519.95 C63H118N22O15S3 CDEFGHKNPSVWY MR 12.3 3 0 3 1 4 21.67 -2925 4.4 hour >20 hour >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01273 HRALMRIRQMMT 12 3-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=34.18095 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01273 DRAVPe01273.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1543.93 C63H114N24O15S3 CDEFGKNPSVWY MR 12.3 4 0 4 1 3 -42.5 -3883 3.5 hour 10 min >10 hour 73.33 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01274 HRIAMRIRQMMT 12 4-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=54.5872 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01274 DRAVPe01274.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1543.93 C63H114N24O15S3 CDEFGKLNPSVWY MR 12.3 4 0 4 1 3 -36.67 -3883 3.5 hour 10 min >10 hour 73.33 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01275 HRILARIRQMMT 12 5-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=435.4996 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01275 DRAVPe01275.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1525.9 C64H116N24O15S2 CDEFGKNPSVWY R 12.3 4 0 4 1 4 -20.83 -3626 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01276 HRILMRARQMMT 12 7-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=150.1405 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01276 DRAVPe01276.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1543.93 C63H114N24O15S3 CDEFGKNPSVWY MR 12.3 4 0 4 1 3 -42.5 -3883 3.5 hour 10 min >10 hour 73.33 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01277 HRILMRIAQMMT 12 8-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=60.60846 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01277 DRAVPe01277.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1500.9 C63H113N21O15S3 CDEFGKNPSVWY M 12 3 0 3 1 4 32.5 -1899 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01278 HRILMRIRAMMT 12 9-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=34.13563 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01278 DRAVPe01278.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1528.96 C64H117N23O14S3 CDEFGKNPQSVWY MR 12.3 4 0 4 1 4 24.17 -2837 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01279 HRILMRIRQAMT 12 10-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=57.98146 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01279 DRAVPe01279.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1525.9 C64H116N24O15S2 CDEFGKNPSVWY R 12.3 4 0 4 1 4 -20.83 -3626 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01280 HRILMRIRQMAT 12 11-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=120.5239 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01280 DRAVPe01280.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1525.9 C64H116N24O15S2 CDEFGKNPSVWY R 12.3 4 0 4 1 4 -20.83 -3626 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01281 HRILMRIRQMMA 12 12-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=89.41235 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50=186.2536 μM. DRAVPe01281 DRAVPe01281.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1555.98 C65H118N24O14S3 CDEFGKNPSTVWY MR 12.3 4 0 4 0 4 0.83 -3134 3.5 hour 10 min >10 hour 105.83 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01282 LMRIRQMMT 9 a-p9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=263.8101 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01282 DRAVPe01282.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1179.52 C48H90N16O12S3 ACDEFGHKNPSVWY M 12 2 0 2 1 2 8.89 -2106 5.5 hour 3 min 2 min 86.67 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01283 HRILMRIR 8 b-p9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=43.50202 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01283 DRAVPe01283.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1094.39 C47H87N19O9S ACDEFGKNPQSTVWY R 12.3 4 0 4 0 3 -25 -3231 3.5 hour 10 min >10 hour 146.25 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01284 LMRIR 5 c-p9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=716.4193 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22743126]MARC-145 cells:CC50>500 μM. DRAVPe01284 DRAVPe01284.cif Linear Free Free None L PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 687.9 C29H57N11O6S ACDEFGHKNPQSTVWY R 12 2 0 2 0 2 24 -1765 5.5 hour 3 min 2 min 156 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01285 hrilmrirqmmt 12 D-P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PRRSV Arteriviridae MTT assay [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=16.12312 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01285 DRAVPe01285.cif Linear Free Free None D PRRSV polymerase "PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase." 1586.01 H-22O-11 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 12.3 0 0 0 0 0 0 0 0 0 0 22743126 Virology. 2012 Oct 10;432(1):73-80. "Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. " Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. 10.1016/j.virol.2012.05.010 Anti-PRRSV DRAVPe01286 AWDFGSIGGVFTSVGKLVHQVFGTAYGVL 29 DV1(419-447) Synthetic construct(derived from DENV1 E protein stem) P27909 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Plaque assay [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90=1.5 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90>6 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90>6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01286 DRAVPe01286.cif Linear Free Free None L Not found The peptide shows antiviral activity by inhibiting virus entry. 3013.45 C143H210N34O38 CEMNPR G 6.79 2 1 1 11 14 80.69 1894 4.4 hour >20 hour >10 hour 97.24 6990 249.64 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-DENV DRAVPe01287 AWDFGSLGGVFTSIGKALHQVFGAIYGAA 29 DV2(419-447) Synthetic construct(derived from DENV2 E protein stem) P29984 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Plaque assay [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90<0.1 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=0.3 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=0.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01287 DRAVPe01287.cif Linear Free Free None L Not found The peptide shows antiviral activity by inhibiting virus entry. 2941.34 C139H202N34O37 CEMNPR G 6.79 2 1 1 10 15 73.79 1974 4.4 hour >20 hour >10 hour 91.03 6990 249.64 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-DENV DRAVPe01288 AWDFGSVGGVLNSLGKMVHQIFGSAYTAL 29 DV3(419-447) Synthetic construct(derived from DENV3 E protein stem) Q99D35 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Plaque assay [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90<0.1 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90=4 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01288 DRAVPe01288.cif Linear Free Free None L Not found The peptide shows antiviral activity by inhibiting virus entry. 3026.46 C139H209N35O39S CEPR G 6.79 2 1 1 11 13 56.9 855 4.4 hour >20 hour >10 hour 94.14 6990 249.64 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-DENV DRAVPe01289 AWDFGSVGGLFTSLGKAVHQVFGSVYTTM 29 DV4(419-447) Synthetic construct(derived from DENV4 E protein stem) P27909 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Plaque assay [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90=5 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=6 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90>6 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01289 DRAVPe01289.cif Linear Free Free None L Not found The peptide shows antiviral activity by inhibiting virus entry. 3063.48 C142H208N34O40S CEINPR G 6.79 2 1 1 12 12 53.45 542 4.4 hour >20 hour >10 hour 73.79 6990 249.64 20881042 J Virol. 2010 Dec;84(24):12549-54. "Schmidt AG, Yang PL, Harrison SC." Peptide inhibitors of flavivirus entry derived from the E protein stem. 10.1128/JVI.01440-10 Anti-DENV DRAVPe01290 YENQKQIANQFNKAISQIQESLTTTSTA 28 HR1-a(899-926) Synthetic construct(derived from SARS-CoV spike protein) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Luciferase assay [Ref.18442051]HIV‐luc/SARS Pseudotyped Virus:inhibition of viral-entry in Vero E3 cells(EC50=1.16 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01290 DRAVPe01290.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3157.44 C135H218N38O49 CDGHMPRVW Q 6.14 2 2 0 11 8 -85 -6487 2.8 hour 10 min 2 min 66.43 1490 55.19 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. "Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM." Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.  10.1002/jcb.21790 Anti-SARS-CoV DRAVPe01291 DVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI 48 GST-removed HR2(1145-1192) Synthetic construct(derived from SARS-CoV spike protein) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Luciferase assay [Ref.18442051]HIV‐luc/SARS Pseudotyped Virus:inhibition of viral-entry in Vero E3 cells(EC50=2.15 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01291 DRAVPe01291.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 5390 C235H384N62O82 CFHMPTW IL 4.11 4 10 -6 13 18 -31.67 -8788 1.1 hour 3 min >10 hour 125.83 2980 63.4 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. "Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM." Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.  10.1002/jcb.21790 Anti-SARS-CoV DRAVPe01292 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 64 sHR2-1(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=43 ± 6.4 μM);##murine coronavirus:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01292 DRAVPe01292.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR1 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 7244.99 C316H507N83O111 CMW ELD 4.34 8 15 -7 17 20 -73.75 -14963 1 hour 30 min >10 hour 100.47 2980 47.3 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01293 PKEELDKYFKNHTSPDVDLGLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 62 sHR2-2(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=24 ± 2.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01293 DRAVPe01293.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR2 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 6970.76 C306H493N81O104 CMW LE 4.49 8 13 -5 17 20 -64.19 -12976 >20 hour >20 hour ? 103.71 2980 48.85 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01294 LDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 56 sHR2-3(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01294 DRAVPe01294.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR3 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 6317.03 C277H446N74O94 CMW LDN 4.5 7 11 -4 16 19 -54.82 -11645 5.5 hour 3 min 2 min 107.86 2980 54.18 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01295 FKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 52 sHR2-4(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01295 DRAVPe01295.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR4 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 5797.43 C252H409N69O87 CMW LNDEI 4.45 6 10 -4 15 18 -49.62 -10696 1.1 hour 3 min 2 min 108.65 1490 29.22 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01296 TSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 48 sHR2-5(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01296 DRAVPe01296.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR5 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 5270.83 C227H375N61O82 CFHMW L 4.11 4 10 -6 14 17 -37.5 -9309 7.2 hour >20 hour >10 hour 117.71 1490 31.7 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01297 VDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 44 sHR2-6(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01297 DRAVPe01297.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR6 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 4870.45 C211H351N57O74 CFHMPTW L 4.21 4 9 -5 12 17 -25.91 -7840 100 hour >20 hour >10 hour 128.41 1490 34.65 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01298 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 40 sHR2-7(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01298 DRAVPe01298.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR7 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 4486.01 C194H323N53O68 CFHMPTW EILN 4.33 4 8 -4 11 15 -38.75 -7958 1.1 hour 3 min >10 hour 124.25 1490 38.21 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01299 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 68 sHR2-8(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=17 ± 3.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01299 DRAVPe01299.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR8 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 7827.69 C346H549N89O117 CMW ELDK 4.46 9 15 -6 18 22 -69.12 -15296 1 hour 30 min >10 hour 100.29 4470 66.72 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01300 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 60 sHR2-9(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=34 ± 4.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01300 DRAVPe01300.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR9 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 6817.53 C298H478N78O104 CMW LDE 4.27 7 14 -7 15 21 -56.17 -13509 1 hour 30 min >10 hour 107.17 1490 25.25 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01301 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLID 56 sHR2-10(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01301 DRAVPe01301.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR10 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 6283.91 C272H439N73O97 CMW DELN 4.32 7 13 -6 15 18 -69.11 -13556 1 hour 30 min >10 hour 100.89 1490 27.09 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01302 DLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKE 39 mHR2(derived from SARS-CoV spike protein heptad repeat) Synthetic construct(derived from SARS-CoV spike protein heptad repeat) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Indirect immunofluorescence assay [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM);##murine coronavirus:inhibition of virus infection in Vero cells(EC50=0.9 ± 0.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01302 DRAVPe01302.cif Linear Free Free None L membrane "The peptide exhibits antiviral activity by competitive binding to the HR11 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion." 4644.31 C207H337N51O67S CGHPW L 4.51 5 8 -3 10 14 -42.56 -7826 1.1 hour 3 min >10 hour 120 2980 78.42 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe01303 ATCYCRTGRCATRESLSGVCEISGRLYRLCCR 32 "Human defensin-5 (HD-5; Defensin, alpha 5; Human, mammals, animals)" Homo sapiens (Human) Q01523##A0JDY6##Q3KNV2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZMP "SARS-CoV-2,HSV,HIV" "Coronaviridae, Herpesviridae, Retroviridae" Plaque assay "[Ref.34206990]SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(60% inhibition at 12.5 μg/mL (3.45 μM));##SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(72% inbibition at 50 μg/mL);##SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(32% inbibition at 50 μg/mL).##[Ref.23269800]Herpes simplex virus2(HSV-2):Potential for CaSki cell protection from HSV-2 infection(47.8% ±3.9% cell protection rates at 25 μg/ml,69.4% ± 5.4% cell protection at 50 μg/ml);neutralization activity against HSV-2 during the preinfection stage(IC50=35 μg/ml);##HIV-1:inhibition of virus infection in JLTRG cells(IC50=7.51 μg/ ml)." [Ref.26206286] It has 0% hemolysis at 100μM against human red blood cells. [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL.##[Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. DRAVPe01303 DRAVPe01303.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L Not found The peptide exhibits antiviral activity by inhibiting virus entry. 3588.19 C144H244N50O45S6 DFHKMNPQW CR 8.96 6 2 4 17 7 -11.25 -8349 4.4 hour >20 hour >10 hour 64.06 3355 108.23 34206990##26206286##23269800 Viruses. 2021 Jun 26;13(7):1246.##Peptides. 2015 Sep;71:128-40.##J Virol. 2013 Mar;87(5):2835-45. "Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Basil Mathew Ramakrishnan Nagaraj##Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J. " Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Antimicrobial activity of human -defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs.##Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. 10.3390/v13071246##10.1016/j.peptides.2015.07.009##10.1128/JVI.02209-12 "Anti-SARS-CoV-2,Anti-HSV,Anti-HIV" DRAVPe01304 ATCYCRTGRCATRESLSGVCRISGRLYRLCCR 32 HD5[E21R] Synthetic construct(derived from human alpha defensin(HD5)) Q01523 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV,HIV" "Herpesviridae, Retroviridae" Plaque assay "[Ref.23269800]Herpes simplex virus2(HSV-2):Potential for CaSki cell protection from HSV-2 infection(61.5% ± 7.1% cell protection rates at 25 μg/ml,90.2% ± 4.9% cell protection at 50 μg/ml);neutralization activity against HSV-2 during the preinfection stage(IC50=25 μg/ml);##HIV-1:inhibition of virus infection in JLTRG cells(IC50=3.53 μg/ ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. DRAVPe01304 DRAVPe01304.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L capsid protein gD "The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells." 3615.26 C145H249N53O43S6 DFHKMNPQW R 9.49 7 1 6 17 7 -14.38 -9160 4.4 hour >20 hour >10 hour 64.06 3355 108.23 23269800 J Virol. 2013 Mar;87(5):2835-45.  "Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J. " Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. 10.1128/JVI.02209-12 "Anti-HSV,Anti-HIV" DRAVPe01305 ATCYCRTGRCATRESLSGVCEIRGRLYRLCCR 32 HD5[S23R] Synthetic construct(derived from human alpha defensin(HD5)) Q01523 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Plaque assay [Ref.23269800]Herpes simplex virus2(HSV-2):neutralization activity against HSV-2 during the preinfection stage(IC50=36 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. DRAVPe01305 DRAVPe01305.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L capsid protein gD "The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells." 3657.3 C147H251N53O44S6 DFHKMNPQW R 9.22 7 2 5 16 7 -22.81 -9501 4.4 hour >20 hour >10 hour 64.06 3355 108.23 23269800 J Virol. 2013 Mar;87(5):2835-45. "Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J. " Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. 10.1128/JVI.02209-12 Anti-HSV DRAVPe01306 ATCYCRRGRCATRESLSGVCEISGRLYRLCCR 32 HD5[T7R] Synthetic construct(derived from human alpha defensin(HD5)) Q01523 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Plaque assay [Ref.23269800]Herpes simplex virus2(HSV-2):neutralization activity against HSV-2 during the preinfection stage(IC50=40 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. DRAVPe01306 DRAVPe01306.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L capsid protein gD "The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells." 3643.27 C146H249N53O44S6 DFHKMNPQW R 9.22 7 2 5 16 7 -23.13 -9584 4.4 hour >20 hour >10 hour 64.06 3355 108.23 23269800 J Virol. 2013 Mar;87(5):2835-45.  "Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J. " Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. 10.1128/JVI.02209-12 Anti-HSV DRAVPe01307 ATCYCRTGRCATRESRSGVCEISGRLYRLCCR 32 HD5[L16R] Synthetic construct(derived from human alpha defensin(HD5)) Q01523 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Plaque assay [Ref.23269800]Herpes simplex virus2(HSV-2):Potential for CaSki cell protection from HSV-2 infection(51.2% ± 7.2% cell protection at 100 μg/ml);neutralization activity against HSV-2 during the preinfection stage(IC50=67 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. DRAVPe01307 DRAVPe01307.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L capsid protein gD "The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells." 3631.22 C144H245N53O45S6 DFHKMNPQW R 9.22 7 2 5 17 6 -37.19 -10333 4.4 hour >20 hour >10 hour 51.88 3355 108.23 23269800 J Virol. 2013 Mar;87(5):2835-46.  "Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J. " Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. 10.1128/JVI.02209-12 Anti-HSV DRAVPe01308 PPVYTKDVDISSQISSMNQSLQQSKDYIKEAQKILDTVNPSL 42 HeV F HRC derived peptide(447-488) Synthetic construct(derived from HeV fusion (F) protein) O89342 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=75 nM);inhibition of fusion in HeLa cells(IC50=40 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01308 DRAVPe01308.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 6HB structure that is required for fusion. " 4710.29 C205H335N53O71S CFGHRW S 4.78 4 5 -1 13 11 -62.62 -8337 >20 hour >20 hour ? 88.1 2980 72.68 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01309 VYTDKVDISSQISSMNQSLQQSKDYIKEAQKILDTV 36 HeV F HRC derived peptide(449-484) Synthetic construct(derived from HeV fusion (F) protein) O89342 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=75 nM);inhibition of fusion in HeLa cells(IC50=40 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01309 DRAVPe01309.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 7HB structure that is required for fusion." 4104.6 C177H292N46O63S CFGHPRW S 4.78 4 5 -1 11 10 -58.33 -7825 100 hour >20 hour >10 hour 91.94 2980 85.14 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01310 DITLNNSVALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSIGN 45 HPIV3 F HRC derived peptide(442-486) Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=20 nM);inhibition of fusion in HeLa cells(IC50=7.5 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=500 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01310 DRAVPe01310.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 8HB structure that is required for fusion." 5083.64 C218H362N62O77 CFHMY IS 4.56 6 9 -3 13 15 -70.44 -11954 1.1 hour 3 min >10 hour 106.22 5500 125 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01311 VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI 36 HPIV3 F HRC derived peptide(449-484) Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=20 nM);inhibition of fusion in HeLa cells(IC50=7.5 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=500 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01311 DRAVPe01311.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 9HB structure that is required for fusion." 4154.69 C181H302N50O61 CFGHMTY IS 4.77 6 8 -2 7 13 -66.94 -9571 100 hour >20 hour >10 hour 111.11 5500 157.14 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01312 VANDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI 36 HPIV3 F HRC derived peptide(449-484)[L451N] Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=100 nM);inhibition of fusion in HeLa cells(IC50=3000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=1100 nM);inhibition of fusion in HeLa cells(IC50=750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01312 DRAVPe01312.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 11HB structure that is required for fusion." 4155.63 C179H297N51O62 CFGHMTY IS 4.77 6 8 -2 8 12 -87.22 -10727 100 hour >20 hour >10 hour 100.28 5500 157.14 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01313 VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSD 36 HPIV3 F HRC derived peptide(449-484)[I484D] Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=100 nM);inhibition of fusion in HeLa cells(IC50=8000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=350 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01313 DRAVPe01313.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 12HB structure that is required for fusion." 4156.62 C179H296N50O63 CFGHMTY DS 4.56 6 9 -3 7 12 -89.17 -10935 100 hour >20 hour >10 hour 100.28 5500 157.14 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01314 VANDPIDISIELNKAKSDLEESKEWIRRSNQKLDSD 36 "HPIV3 F HRC derived peptide(449-484)[L451N,I484D]" Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=1100 nM);inhibition of fusion in HeLa cells(IC50=750 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01314 DRAVPe01314.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 13HB structure that is required for fusion." 4157.56 C177H291N51O64 CFGHMTY DS 4.56 6 9 -3 8 11 -109.44 -12091 100 hour >20 hour >10 hour 89.44 5500 157.14 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01315 VALDPIDISIELNKAKSDLEESKEWIRR 28 HPIV3 F HRC derived peptide(449-476) Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01315 DRAVPe01315.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 14HB structure that is required for fusion." 3268.71 C144H239N39O47 CFGHMQTY EI 4.72 5 7 -2 4 11 -58.57 -7230 100 hour >20 hour >10 hour 115 5500 203.7 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01316 SIELNKAKSDLEESKEWIRRSNQKLDSI 28 HPIV3 F HRC derived peptide(457-484) Synthetic construct(derived from HPIV3 fusion (F) protein) P06828 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,HPIV3" Paramyxoviridae Luminescence fusion assay [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01316 DRAVPe01316.cif Linear Free Free None L membrane "The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 15HB structure that is required for fusion." 3317.7 C142H238N42O49 CFGHMPTVY S 6.06 6 6 0 7 8 -122.5 -9888 1.9 hour >20 hour >10 hour 87.14 5500 203.7 16973588 J Virol. 2006 Oct;80(19):9837-49. "Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A." Inhibition of hendra virus fusion. 10.1128/JVI.00736-06 "Anti-HeV,Anti-HPIV3" DRAVPe01317 MANAGLQLLGFILAFLGW 18 CL58 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=2.1 ± 0.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22378192]Huh7.5.1 cells:CC50~200 Μm. DRAVPe01317 DRAVPe01317.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1935.36 C94H143N21O21S CDEHKPRSTVY L 5.28 0 0 0 4 12 151.67 3623 30 hour >20 hour >10 hour 146.67 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-15.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01318 GLQLLGFILAFLGWIGAI 18 CL58.1 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01318 DRAVPe01318.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1902.35 C96H148N20O20 CDEHKMNPRSTVY L 5.52 0 0 0 4 13 198.33 4949 30 hour >20 hour >10 hour 184.44 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-16.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01319 LLGFILAFLGWIGAIVST 18 CL58.2 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=4.3 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01319 DRAVPe01319.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1891.33 C95H147N19O21 CDEHKMNPQRY L 5.52 0 0 0 5 13 213.89 4724 5.5 hour 3 min 2 min 178.89 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-17.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01320 FILAFLGWIGAIVSTALP 18 CL58.3 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=8.9± 1.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01320 DRAVPe01320.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1889.31 C95H145N19O21 CDEHKMNQRY AIL 5.52 0 0 0 4 13 196.11 4319 1.1 hour 3 min 2 min 162.78 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-18.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01321 AFLGWIGAIVSTALPQWR 18 CL58.4 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=12.5± 1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01321 DRAVPe01321.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1986.35 C96H144N24O22 CDEHKMNY A 9.79 1 0 1 4 11 85 1224 4.4 hour >20 hour >10 hour 119.44 11000 647.06 22378192 Hepatology. 2012 Aug;56(2):507-19.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01322 GWIGAIVSTALPQWRIYS 18 CL58.5 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=21.5± 1.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01322 DRAVPe01322.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2018.35 C96H144N24O24 CDEFHKMN I 8.75 1 0 1 6 9 51.67 391 30 hour >20 hour >10 hour 113.89 12490 734.71 22378192 Hepatology. 2012 Aug;56(2):507-20.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01323 GAIVSTALPQWRIYSYAG 18 CL58.6 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=23.8 ± 2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01323 DRAVPe01323.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1953.23 C91H137N23O25 CDEFHKMN A 8.59 1 0 1 7 8 34.44 -167 30 hour >20 hour >10 hour 97.78 8480 498.82 22378192 Hepatology. 2012 Aug;56(2):507-21.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01324 VSTALPQWRIYSYAGDNI 18 CL58.7 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01324 DRAVPe01324.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2054.29 C94H140N24O28 CEFHKM AISY 5.81 1 1 0 7 7 -12.22 -1978 100 hour >20 hour >10 hour 92.22 8480 498.82 22378192 Hepatology. 2012 Aug;56(2):507-22.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01325 ALPQWRIYSYAGDNIVTA 18 CL58.8 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01325 DRAVPe01325.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2038.29 C94H140N24O27 CEFHKM A 5.88 1 1 0 6 8 2.22 -1457 4.4 hour >20 hour >10 hour 97.78 8480 498.82 22378192 Hepatology. 2012 Aug;56(2):507-23.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01326 MANAGLQLLGFILA 14 CL58-4 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01326 DRAVPe01326.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1431.76 C66H110N16O17S CDEHKPRSTVWY L 5.28 0 0 0 3 9 157.14 2506 30 hour >20 hour >10 hour 160.71 0 0 22378192 Hepatology. 2012 Aug;56(2):507-24.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01327 MANAGLQLLGFILAFL 16 CL58-2 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=7.6± 0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01327 DRAVPe01327.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1692.09 C81H130N18O19S CDEHKPRSTVWY L 5.28 0 0 0 3 11 178.75 3296 30 hour >20 hour >10 hour 165 0 0 22378192 Hepatology. 2012 Aug;56(2):507-25.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01328 MANAGLQLLGFILAFLGWIG 20 CL58+2 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=17.8 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01328 DRAVPe01328.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2105.57 C102H157N23O23S CDEHKPRSTVY L 5.28 0 0 0 5 13 157 4209 30 hour >20 hour >10 hour 151.5 5500 289.47 22378192 Hepatology. 2012 Aug;56(2):507-26.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01329 MANAGLQLLGFILAFLGWIGAI 22 CL58+4 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=4.0 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01329 DRAVPe01329.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2289.81 C111H173N25O25S CDEHKPRSTVY L 5.28 0 0 0 5 15 171.36 4882 30 hour >20 hour >10 hour 160 5500 261.9 22378192 Hepatology. 2012 Aug;56(2):507-27.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01330 MANAGLQLLGFILAFLGWIGAIVS 24 CL58+6 Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=5.1 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01330 DRAVPe01330.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 2476.02 C119H187N27O28S CDEHKPRTY L 5.28 0 0 0 6 16 171.25 4946 30 hour >20 hour >10 hour 158.75 5500 239.13 22378192 Hepatology. 2012 Aug;56(2):507-28.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01331 managlqllgfilaflgw 18 CL58.d No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=1.8 ± 0.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01331.cif Linear Free Free None D membrane protein The peptide inhibits virus entry in a postbinding step. 1935.36 H-34O-17 ACDEFGHIKLMNPQRSTVWY ACDEFGHIKLMNPQRSTVWY 5.28 0 0 0 0 0 0 0 0 0 0 22378192 Hepatology. 2012 Aug;56(2):507-29.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01332 AGALMFAWLLLGLQGIFN 18 CL58.S Synthetic construct(derived from human claudin-1) O95832 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01332 DRAVPe01332.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1935.36 C94H143N21O21S CDEHKPRSTVY L 5.57 0 0 0 4 12 151.67 3623 4.4 hour >20 hour >10 hour 146.67 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-29.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01333 MASAGMQILGVVLTLLGW 18 CL-6 Synthetic construct(derived from human claudin-1) P56747 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01333 DRAVPe01333.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1860.3 C85H142N20O22S2 CDEFHKNPRY L 5.28 0 0 0 5 10 157.78 3464 30 hour >20 hour >10 hour 151.67 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-30.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01334 MANSGLQLLGFSMALLGW 18 CL-7 Synthetic construct(derived from human claudin-1) Q3B794 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01334 DRAVPe01334.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1909.29 C87H137N21O23S2 CDEHIKPRTVY L 5.28 0 0 0 6 9 102.78 2207 30 hour >20 hour >10 hour 119.44 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-31.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01335 MASTGLELLGMTLAVLGW 18 CL-9 Synthetic construct(derived from human claudin-1) O95484 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Pseudoviral particle infection assay [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01335 DRAVPe01335.cif Linear Free Free None L membrane protein The peptide inhibits virus entry in a postbinding step. 1863.26 C84H139N19O24S2 CDFHIKNPQRY L 4 0 1 -1 6 9 126.67 2676 30 hour >20 hour >10 hour 135.56 5500 323.53 22378192 Hepatology. 2012 Aug;56(2):507-32.  "Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W. " A human claudin-1-derived peptide inhibits hepatitis C virus entry. 10.1002/hep.25685 Anti-HCV DRAVPe01336 EELRVRLASHLRKLRKRLLRDADDLQKRLAVYEEQAQQIRLQAEAFQARLKSWFEPLVEDM 61 hEP-1 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.67 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22334503]Huh7.5.1 cell:CC50>100 μg/ ml(〜14μM). DRAVPe01336 DRAVPe01336.cif Linear Free Free None L "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 7405.56 C327H539N101O93S CGNT L 9.4 14 11 3 3 25 -74.1 -18940 1 hour 30 min >10 hour 102.46 6990 116.5 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01337 CEELRVRLASHLRKLRKRLLRDADDLQKRLAVY 33 hEP-2 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01337 DRAVPe01337.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 4034.79 C175H306N60O47S FGIMNPTW L 10.4 11 5 6 3 13 -69.09 -12046 1.2 hour >20 hour >10 hour 121.21 1490 46.56 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01338 EELRVRLASHLRKLRKRLLRDADDLQKRLAVY 32 hEP-2/deltaCys Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01338 DRAVPe01338.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3931.65 C172H301N59O46 CFGIMNPTW L 10.87 11 5 6 2 13 -79.06 -12174 1 hour 30 min >10 hour 125 1490 48.06 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01339 CEEIRARLSTHLRKMRKRLMRDADDLQKRLAVY 33 mEP-2 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01339 DRAVPe01339.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 4072.83 C172H300N60O48S3 FGNPW R 10.4 11 5 6 4 10 -93.33 -13221 1.2 hour >20 hour >10 hour 88.79 1490 46.56 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01340 CEEQAQQIRLQAEAFQARLKSWFEPLVEDM 30 hEP-3 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01340 DRAVPe01340.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3595.06 C158H245N43O49S2 GHNTY EQ 4.42 3 6 -3 2 12 -58 -6638 1.2 hour >20 hour >10 hour 75 5500 189.66 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01341 CVRLASHLRKLRKRLLRDADDL 22 hEP-4 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01341 DRAVPe01341.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 2648.17 C113H203N41O30S EFGIMNPQTWY L 10.79 8 3 5 2 9 -53.18 -8146 1.2 hour >20 hour >10 hour 128.64 0 0 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01342 CIRLQAEAFQARLKSWFEPLV 21 hEP-5 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01342 DRAVPe01342.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 2505.96 C116H181N31O29S DGHMNTY AL 8.22 3 2 1 2 11 16.19 -2477 1.2 hour >20 hour >10 hour 102.38 5500 275 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01343 VRLASHLRKLRKRLLRDADDLIRLQAEAFQARLKSWFEPLV 41 hEP-6 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01343 DRAVPe01343.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 4929.84 C223H372N70O56 CGMNTY L 11.29 11 5 6 2 20 -32.44 -10879 100 hour >20 hour >10 hour 121.46 5500 137.5 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01344 LRVRLASHLRKLRKRLLRDADDLQKRLAVY 30 hEP-7 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01344 DRAVPe01344.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3673.42 C162H287N57O40 CEFGIMNPTW L 11.63 11 3 8 2 13 -61 -10812 5.5 hour 3 min 2 min 133.33 1490 51.38 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01345 EELRVRLASHLRKLRKRLLRDADDL 25 hEP-8 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01345 DRAVPe01345.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3072.61 C132H235N47O37 CFGIMNPQTWY L 10.74 9 5 4 1 10 -87.6 -10636 1 hour 30 min >10 hour 128.8 0 0 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01346 VRLASHLRKLRKRLLRDADDLQKRLAVY 28 hEP-9 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01346 DRAVPe01346.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3404.07 C150H264N52O38 CEFGIMNPTW L 11.38 10 3 7 2 12 -62.86 -9812 100 hour >20 hour >10 hour 128.93 1490 55.19 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01347 CVRLASHLRKLRKRLLRDADDLQKRLAVY 29 hEP-10 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01347 DRAVPe01347.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 3507.21 C153H269N53O39S EFGIMNPTW L 10.91 10 3 7 3 12 -52.07 -9684 1.2 hour >20 hour >10 hour 124.48 1490 53.21 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01348 CLRVRLASHLRKLRKRLLRDADDL 24 hEP-11 Synthetic construct(derived from human apolipoprotein E) P02649 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01348 DRAVPe01348.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 2917.52 C125H226N46O32S EFGIMNPQTWY L 11.35 9 3 6 2 10 -51.67 -9146 1.2 hour >20 hour >10 hour 134.17 0 0 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01349 CLRKLRKRLLRC 12 hEP-12 Synthetic construct(derived from human apolipoprotein E) P28995 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae RT PCR [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01349 DRAVPe01349.cif Linear Free Free None L Not found "hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. " 1558.03 C66H128N26O13S2 ADEFGHIMNPQSTVWY LR 11.56 6 0 6 2 4 -46.67 -4854 1.2 hour >20 hour >10 hour 130 125 11.36 22334503 Hepatology. 2012 Aug;56(2):484-91. "Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T." Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. 10.1002/hep.25665 Anti-HCV DRAVPe01350 ECRSTSYAGAVVNDL 15 H2-(1-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=42 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01350 DRAVPe01350.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 1584.72 C65H105N19O25S FHIKMPQW ASV 4.37 1 2 -1 7 5 -4.67 -2776 1 hour 30 min >10 hour 78 1490 106.43 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01351 STSYAGAVVNDL 12 H2-(4-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=29 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01351 DRAVPe01351.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 1196.28 C51H81N13O20 CEFHIKMPQRW ASV 3.8 0 1 -1 6 5 40 -731 1.9 hour >20 hour >10 hour 97.5 1490 135.45 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01352 YAGAVVNDL 9 H2-(7-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=36-60 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01352 DRAVPe01352.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C41H64N10O14 CEFHIKMPQRSTW AV 3.8 0 1 -1 3 5 78.89 206 2.8 hour 10 min 2 min 130 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01353 AGAVVNDL 8 H2-(8-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=283 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01353 DRAVPe01353.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 757.84 C32H55N9O12 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 105 220 4.4 hour >20 hour >10 hour 146.25 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01354 GAVVNDL 7 H2-(9-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=225 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01354 DRAVPe01354.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 686.76 C29H50N8O11 CEFHIKMPQRSTWY V 3.8 0 1 -1 2 4 94.29 39 30 hour >20 hour >10 hour 152.86 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01355 AVVNDL 6 H2-(10-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01355 DRAVPe01355.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 629.71 C27H47N7O10 CEFGHIKMPQRSTWY V 3.8 0 1 -1 1 4 116.67 -55 4.4 hour >20 hour >10 hour 178.33 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01356 VVNDL 5 H2-(11-15) Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) P10224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=760 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01356 DRAVPe01356.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 558.63 C24H42N6O9 ACEFGHIKMPQRSTWY V 3.8 0 1 -1 1 3 104 -236 100 hour >20 hour >10 hour 194 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01357 YAGAVVNDL 9 Ac-H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01357.cif Linear Acetylation Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C41H64N10O14 CEFHIKMPQRSTW AV 3.8 0 1 -1 3 5 78.89 206 2.8 hour 10 min 2 min 130 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01358 YAGAVVNDL 9 H2-(7-15) amide Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01358.cif Linear Free Amidation None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C41H64N10O14 CEFHIKMPQRSTW AV 3.8 0 1 -1 3 5 78.89 206 2.8 hour 10 min 2 min 130 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01359 YAGAVVNDL 9 Ac-H2-(7-15) amide Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=76 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01359.cif Linear Acetylation Amidation None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C41H64N10O14 CEFHIKMPQRSTW AV 3.8 0 1 -1 3 5 78.89 206 2.8 hour 10 min 2 min 130 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01360 VVNDL 5 Ac-H2-(11-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=400 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01360.cif Linear Acetylation Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 558.63 C24H42N6O9 ACEFGHIKMPQRSTWY V 3.8 0 1 -1 1 3 104 -236 100 hour >20 hour >10 hour 194 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01361 YAVVNDL 7 [Tyr9]H2-(9-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=340 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01361 DRAVPe01361.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 792.89 C36H56N8O12 CEFGHIKMPQRSTW V 3.8 0 1 -1 2 4 81.43 -69 2.8 hour 10 min 2 min 152.86 1490 248.33 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01362 YAVVNDL 7 Ac-[Tyr9]H2-(9-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=330 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01362.cif Linear Acetylation Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 792.89 C36H56N8O12 CEFGHIKMPQRSTW V 3.8 0 1 -1 2 4 81.43 -69 2.8 hour 10 min 2 min 152.86 1490 248.33 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01363 YGAVVNDL 8 [Tyr8]H2-(8-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=330 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01363 DRAVPe01363.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 849.94 C38H59N9O13 CEFHIKMPQRSTW V 3.8 0 1 -1 3 4 66.25 25 2.8 hour 10 min 2 min 133.75 1490 212.86 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01364 YGAVVNDL 8 Ac-[Tyr8]H2-(8-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=150 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01364.cif Linear Acetylation Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 849.94 C38H59N9O13 CEFHIKMPQRSTW V 3.8 0 1 -1 3 4 66.25 25 2.8 hour 10 min 2 min 133.75 1490 212.86 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01365 AAGAVVNDL 9 [Ala7]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=280 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01365 DRAVPe01365.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 828.92 C35H60N10O13 CEFHIKMPQRSTWY A 3.8 0 1 -1 2 6 113.33 401 4.4 hour >20 hour >10 hour 141.11 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01366 yAGAVVNDL 9 [D-Tyr7]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=200 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01366.cif Linear Free Free None Mixed(D-Tyr1) ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C32H53N9O11 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 93.33 220 130 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01367 yAGAVVNDL 9 Ac-[D-Tyr7]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=165 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01367.cif Linear Acetylation Free None Mixed(D-Tyr1) ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C32H53N9O11 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 93.33 220 130 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01368 XAGAVVNDL 9 [Tyr7(OMe)]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=88 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01368.cif Linear Free Free The 'X' at position 1 is methoxy Tyrosine. L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 869.17 C32H53N9O11 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 93.33 220 130 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01369 XAGAVVNDL 9 Ac[Tyr7(OMe)]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=40 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01369.cif Linear Acetylation Free The 'X' at position 1 is methoxy Tyrosine. L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 869.17 C32H53N9O11 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 93.33 220 130 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01370 XAGAVVNDL 9 [desamino-Tyr7]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=33 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01370.cif Linear Free Free The 'X' at position 1 is 3-(4-hydroxyphenyl)propionic acid. L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 869.17 C32H53N9O11 CEFHIKMPQRSTWY AV 3.8 0 1 -1 2 5 93.33 220 130 0 0 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01371 YaGAVVNDL 9 [D-Ala8]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=200 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01371.cif Linear Free Free None Mixed(D-Ala2) ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C38H57N9O12 CEFHIKMPQRSTW V 3.8 0 1 -1 3 4 58.89 25 2.8 hour 10 min 2 min 118.89 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01372 YaGAVVNDL 9 Ac-[D-Ala8]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=230 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01372.cif Linear Acetylation Free None Mixed(D-Ala2) ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 921.02 C38H57N9O12 CEFHIKMPQRSTW V 3.8 0 1 -1 3 4 58.89 25 2.8 hour 10 min 2 min 118.89 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01373 YXGAVVNDL 9 [β-Ala8]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=100 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01373.cif Linear Free Free The 'X' at position 2 is 3-aminoproprionic acid. L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 961.27 C38H57N9O12 CEFHIKMPQRSTW V 3.8 0 1 -1 3 4 58.89 25 2.8 hour 10 min 2 min 118.89 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01374 YAGAVANDL 9 [Ala12]H2-(7-15) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=760 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01374 DRAVPe01374.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 892.96 C39H60N10O14 CEFHIKMPQRSTW A 3.8 0 1 -1 3 5 52.22 -17 2.8 hour 10 min 2 min 108.89 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01375 YTMLVVDDL 9 EBV H2-(7-15) Synthetic construct(derived from EBV ribonucleotide reductase subunit 2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=110 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01375 DRAVPe01375.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 1068.25 C48H77N9O16S ACEFGHIKNPQRSW DLV 3.56 0 2 -2 2 4 98.89 12 2.8 hour 10 min 2 min 151.11 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01376 YAGTVINDL 9 VZV H2-(7-15) Synthetic construct(derived from VZV ribonucleotide reductase subunit 2) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae Ribonucleotide reductase assay [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=15 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01376 DRAVPe01376.cif Linear Free Free None L ribonucleotide reductase The peptide inhibits the activity of ribonucleotide rductase. 965.07 C43H68N10O15 CEFHKMPQRSW ADGILNTVY 3.8 0 1 -1 4 4 54.44 -144 2.8 hour 10 min 2 min 130 1490 186.25 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. "Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P." Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. Not available Anti-HSV DRAVPe01377 FKLRAKIKVRLRAKIKL 17 D4E1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.46 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.43 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=5.90 μM. DRAVPe01377 DRAVPe01377.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2081.71 C98H181N31O18 CDEGHMNPQSTWY K 12.32 8 0 8 0 9 -11.76 -3727 1.1 hour 3 min 2 min 143.53 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01378 FAVAVKAVAVKAVAVKAVKKAVKKVKKAVKKAVKKKK 37 DC1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.75 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.78 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=9.20 μM. DRAVPe01378 DRAVPe01378.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3889.05 C184H340N52O38 CDEGHILMNPQRSTWY K 11.15 15 0 15 0 22 22.97 -1773 1.1 hour 3 min 2 min 113.24 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01379 FLAAARIAKRVAKKARKLAKRAARKRK 27 D1D6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.94 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=1.47 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=8.93 μM. DRAVPe01379 DRAVPe01379.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3077.86 C137H254N52O28 CDEGHMNPQSTWY A 12.71 13 0 13 0 14 -70.37 -9030 1.1 hour 3 min 2 min 87.41 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01380 FRFKIKFRLKFRFKARFKFRAKFRA 25 D4C3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=1.32 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=3.81 μM. DRAVPe01380 DRAVPe01380.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3341.15 C165H255N49O26 CDEGHMNPQSTVWY F 12.71 12 0 12 0 13 -57.2 -8371 1.1 hour 3 min 2 min 43.2 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01381 FAVGLRAIKRALKKLRRGVRKVAKDL 26 D5F Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=5.47 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=8.73 μM. DRAVPe01381 DRAVPe01381.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2963.7 C134H244N46O29 CEHMNPQSTWY KR 12.19 10 1 9 2 13 -15.38 -6225 1.1 hour 3 min 2 min 123.85 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01382 KRKRAVKRVGRRLKKLARKIARLGVAKLAGLRAVKLF 37 D5C1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.38 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=5.26 μM. DRAVPe01382 DRAVPe01382.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 4226.36 C191H355N69O38 CDEHMNPQSTWY KR 12.85 16 0 16 3 18 -28.92 -9650 1.3 hour 3 min 2 min 121.35 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01383 GAKKGAKKGKKGAKKGAKGAGAKGAGAFKKKK 32 D2B15 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=4.07 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=6.19 μM. DRAVPe01383 DRAVPe01383.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3041.73 C135H246N46O33 CDEHILMNPQRSTVWY K 11.11 14 0 14 9 9 -128.13 -5178 30 hour >20 hour >10 hour 25 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01384 FAKKFAKKFKKFAKKFAKFAFAF 23 D2A21 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.05 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=3.43 μM. DRAVPe01384 DRAVPe01384.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2775.47 C144H212N32O24 CDEGHILMNPQRSTVWY K 10.9 9 0 9 0 14 -8.26 -1525 1.1 hour 3 min 2 min 26.09 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01385 KKKKFVKKVAKKVKKVAKKVAKVAVAV 27 D2A3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.00 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=3.24 μM. DRAVPe01385 DRAVPe01385.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2979.91 C142H264N40O28 CDEGHILMNPQRSTWY K 11.08 13 0 13 0 14 -19.63 -2780 1.3 hour 3 min 2 min 104.44 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01386 FLFAFRIFKRVFKKFRKLFKRAF 23 D1A22 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=10.51 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=10.79 μM. DRAVPe01386 DRAVPe01386.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3041.82 C155H234N40O24 CDEGHMNPQSTWY F 12.49 9 0 9 0 14 20.87 -4117 1.1 hour 3 min 2 min 72.17 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01387 KRKRAVKRVGRRLKKKLARKIARLGVAF 28 D5C Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=7.82 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=6.84 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=7.48 μM. DRAVPe01387 DRAVPe01387.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3304.18 C148H276N56O29 CDEHMNPQSTWY KR 12.78 14 0 14 2 12 -75.36 -9939 1.3 hour 3 min 2 min 101.07 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01388 KRKRFAKKFLRFLRKVIRFLKRFIRRF 27 D3A15 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.69 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=3.28 μM. DRAVPe01388 DRAVPe01388.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 3655.63 C176H293N57O28 CDEGHMNPQSTWY R 12.85 14 0 14 0 13 -60 -10433 1.3 hour 3 min 2 min 86.67 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01389 FALALKALKKALKKLKKALKKAL 23 DP1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=7.07 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=5.17 μM. DRAVPe01389 DRAVPe01389.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2537.35 C123H226N32O24 CDEGHIMNPQRSTVWY K 10.9 9 0 9 0 14 22.17 -167 1.1 hour 3 min 2 min 144.78 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01390 FAIAIKAIKKAIKKIKKAIKKAI 23 D1D2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=8.71 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=5.87 μM. DRAVPe01390 DRAVPe01390.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2537.35 C123H226N32O24 CDEGHLMNPQRSTVWY K 10.9 9 0 9 0 14 43.48 -167 1.1 hour 3 min 2 min 144.78 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01391 FKVKAKVKAKVKAKVKAKKKK 21 D4B Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=2.85 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12208971]CrFK cell:TC50=0.92 μM. DRAVPe01391 DRAVPe01391.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2384.13 C113H211N33O22 CDEGHILMNPQRSTWY K 11.04 12 0 12 0 9 -95.24 -4022 1.1 hour 3 min 2 min 74.29 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01392 AVKRVGRRLKKLARKIARLGVAF 23 D5D Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FIV Retroviridae reverse transcriptase (RT) assay [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.37 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01392 DRAVPe01392.cif Linear Free Free None L Not found The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. 2607.28 C118H216N42O24 CDEHMNPQSTWY R 12.61 9 0 9 2 12 -1.74 -5290 4.4 hour >20 hour >10 hour 123.04 0 0 12208971 J Virol. 2002 Oct;76(19):9952-61. "Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA." Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  10.1128/jvi.76.19.9952-9961.2002 Anti-FIV DRAVPe01393 LPRRLHLEPAFLPYSVKAHECC 22 UL54(1221-1242) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01393 DRAVPe01393.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2580.06 C117H183N33O29S2 DGIMNQTW L 8.06 5 2 3 4 8 -10.91 -2899 5.5 hour 3 min 2 min 93.18 1615 76.9 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01394 PGGETARKDKFLHMVLPRRL 20 UL54(1206-1225) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01394 DRAVPe01394.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2321.77 C103H173N33O26S CINQSWY LR 10.91 6 2 4 3 6 -70.5 -5080 >20 hour >20 hour ? 78 0 0 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01395 EQVLKAVTNVLSPVFPGGET 20 UL54(1191-1210) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=280 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01395 DRAVPe01395.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2085.39 C94H153N23O30 CDHIMRWY V 4.53 1 2 -1 6 8 24.5 -722 1 hour 30 min >10 hour 102 0 0 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01396 YVREHGVPIHADKYFEQVLK 20 UL54(1176-1195) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01396 DRAVPe01396.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2428.78 C113H170N30O30 CMNSTW V 6.92 5 3 2 3 7 -59 -3581 2.8 hour 10 min 2 min 87.5 2980 156.84 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01397 PPSAVCNYEVAEDPSYVREH 20 UL54(1161-1180) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01397 DRAVPe01397.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2262.44 C98H144N26O34S FGIKLMQTW EPV 4.4 2 4 -2 6 5 -77.5 -4543 >20 hour >20 hour ? 53.5 2980 156.84 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01398 RRLHLEPAFLPYSVKAHECC 20 UL54(1223-1242) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01398 DRAVPe01398.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2369.79 C106H165N31O27S2 DGIMNQTW L 8.06 5 2 3 4 7 -23 -3391 1 hour 2 min 2 min 83 1615 85 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01399 LPRRLHLEPAFLPYSVKAHEC 21 UL54(1221-1241) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=75 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01399 DRAVPe01399.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2476.93 C114H178N32O28S DGIMNQTW L 8.22 5 2 3 3 8 -23.33 -3027 5.5 hour 3 min 2 min 97.62 1490 74.5 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01400 LPRRLHLEPAFLPYSVKAHE 20 UL54(1221-1240) Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) P08546 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae ELISA [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01400 DRAVPe01400.cif Linear Free Free None L DNA polymerase "Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase." 2373.79 C111H173N31O27 CDGIMNQTW L 8.6 5 2 3 2 8 -37 -3155 5.5 hour 3 min 2 min 102.5 1490 78.42 12857903 J Virol. 2003 Aug;77(15):8336-44. "Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS." Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. 10.1128/jvi.77.15.8336-8344.2003 Anti-HCMV DRAVPe01401 ACFPWGNTWCGGK 13 NTW (S-S) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=13.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01401 DRAVPe01401.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1426.63 C65H87N17O16S2 DEHILMQRSVY G 8.1 1 0 1 7 4 -23.85 7 4.4 hour >20 hour >10 hour 7.69 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01402 ACFPWGNTWCGGK 13 NTW (L) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01402.cif Linear Free Free None L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1426.63 C65H87N17O16S2 DEHILMQRSVY G 8.1 1 0 1 7 4 -23.85 7 4.4 hour >20 hour >10 hour 7.69 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01403 ACFPWGKEYCGGK 13 KEY (S-S) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=22.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01403 DRAVPe01403.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1445.67 C66H92N16O17S2 DHILMNQRSTV G 8.07 2 1 1 6 3 -51.54 -555 4.4 hour >20 hour >10 hour 7.69 7115 592.92 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01404 ACFPWGKEYCGGK 13 KEY (L) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01404.cif Linear Free Free None L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1445.67 C66H92N16O17S2 DHILMNQRSTV G 8.07 2 1 1 6 3 -51.54 -555 4.4 hour >20 hour >10 hour 7.69 7115 592.92 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01405 ACFPWGNQWCGGK 13 NQW (S-S) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=6.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01405 DRAVPe01405.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1453.66 C66H88N18O16S2 DEHILMRSTVY G 8.1 1 0 1 6 4 -45.38 -290 4.4 hour >20 hour >10 hour 7.69 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01406 ACFPWGNQWCGGK 13 NQW (L) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=37.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01406.cif Linear Free Free None L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1453.66 C66H88N18O16S2 DEHILMRSTVY G 8.1 1 0 1 6 4 -45.38 -290 4.4 hour >20 hour >10 hour 7.69 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01407 CFPWGC 6 FPWG (S-S) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01407 DRAVPe01407.cif Cyclic Cyclization of a n-terminal Cys residue (forming a disulfide bond) Cyclization of a C-terminal Cys residue (forming a disulfide bond) Disulfide bond between Cys1 and Cys6 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 711.85 C33H41N7O7S2 ADEHIKLMNQRSTVY C 5.51 0 0 0 3 2 81.67 881 1.2 hour >20 hour >10 hour 0 5625 1125 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01408 CFPWGC 6 FPWG (L) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 711.85 C33H41N7O7S2 ADEHIKLMNQRSTVY C 5.51 0 0 0 3 2 81.67 881 1.2 hour >20 hour >10 hour 0 5625 1125 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01409 ACAPWGNTWCGGK 13 NTW (S-S)[F1A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01409 DRAVPe01409.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1350.53 C59H83N17O16S2 DEFHILMQRSVY G 8.1 1 0 1 7 4 -31.54 -110 4.4 hour >20 hour >10 hour 15.38 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01410 ACFAWGNTWCGGK 13 NTW (S-S)[P2A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=39 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01410 DRAVPe01410.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1400.59 C63H85N17O16S2 DEHILMPQRSVY G 8.1 1 0 1 7 5 2.31 188 4.4 hour >20 hour >10 hour 15.38 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01411 ACFPAGNTWCGGK 13 NTW (S-S)[W3A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=43 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01411 DRAVPe01411.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1311.5 C57H82N16O16S2 DEHILMQRSVY G 8.1 1 0 1 7 4 -3.08 -45 4.4 hour >20 hour >10 hour 15.38 5625 468.75 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01412 ACFPWANTWCGGK 13 NTW (S-S)[G4A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=7.4 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01412 DRAVPe01412.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1440.66 C66H89N17O16S2 DEHILMQRSVY ACGW 8.1 1 0 1 6 5 -6.92 94 4.4 hour >20 hour >10 hour 15.38 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01413 ACFPWGATWCGGK 13 NTW (S-S)[N5A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=40 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01413 DRAVPe01413.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1383.61 C64H86N16O15S2 DEHILMNQRSVY G 8.1 1 0 1 6 5 16.92 852 4.4 hour >20 hour >10 hour 15.38 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01414 ACFPWGNAWCGGK 13 NTW (S-S)[T6A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=11 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01414 DRAVPe01414.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1396.6 C64H85N17O15S2 DEHILMQRSTVY G 8.1 1 0 1 6 5 -4.62 445 4.4 hour >20 hour >10 hour 15.38 11125 927.08 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01415 ACFPWGNTACGGK 13 NTW (S-S)[W7A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Surface plasmon resonance [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=80 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01415 DRAVPe01415.cif Cyclic Free Free Disulfide bond between Cys2 and Cys10 L RNA-dependent RNA polymerase "The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate." 1311.5 C57H82N16O16S2 DEHILMQRSVY G 8.1 1 0 1 7 4 -3.08 -45 4.4 hour >20 hour >10 hour 15.38 5625 468.75 12951030 Virology. 2003 Aug 15;313(1):158-69. "Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P." Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. 10.1016/s0042-6822(03)00313-1 Anti-HCV DRAVPe01416 MWKTPTLKYFGGFNFSQI 18 SARSWW-I(770-788) Synthetic construct(derived from SARS-CoV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(58% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01416 DRAVPe01416.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 2165.54 C105H149N23O25S ACDEHRV F 9.7 2 0 2 7 6 -16.67 -662 30 hour >20 hour >10 hour 43.33 6990 411.18 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01417 ATAGWTFGAGAALQIPFAMQMAY 23 SARSWW-II(864-886) Synthetic construct(derived from SARS-CoV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(39% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01417 DRAVPe01417.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 2374.76 C110H160N26O29S2 CDEHKNRSV A 5.57 0 0 0 6 12 73.48 2196 4.4 hour >20 hour >10 hour 64.35 6990 317.73 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01418 GYHLMSFPQAAPHGVVFLHVTW 22 SARSWW-III(1028-1049) Synthetic construct(derived from SARS-CoV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay "[Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(90% inhibition at ~30 μM,IC50=2 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01418 DRAVPe01418.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 2494.9 C120H168N30O27S CDEIKNR HV 7.02 3 0 3 5 10 47.73 1247 30 hour >20 hour >10 hour 84.09 6990 332.86 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01419 GVFVFNGTSWFITQRNFFS 19 SARSWW-IV(1075-1093) Synthetic construct(derived from SARS-CoV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay "[Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(83% inhibition at ~30 μM,IC50=2 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01419 DRAVPe01419.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 2254.53 C109H148N26O27 ACDEHKLMPY F 9.75 1 0 1 8 9 37.89 -1357 30 hour >20 hour >10 hour 51.05 5500 305.56 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01420 AACEVAKNLNESLIDLQELGKYEQYIKW 28 SARSWW-Vb(1169-1194) Synthetic construct(derived from SARS-CoV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(42% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01420 DRAVPe01420.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 3269.72 C147H230N36O46S FHMPRT EL 4.59 3 5 -2 7 11 -41.43 -3711 4.4 hour >20 hour >10 hour 104.64 8480 314.07 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01421 GYFVQDDGEWKFTGSSYYY 19 MHVWW-IV(1144-1162) Synthetic construct(derived from MHV spike protein) P11224 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Plaque formation assay [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. DRAVPe01421 DRAVPe01421.cif Linear Free Free None L membrane No machanism information found in the reference(s) presented in this entry 2312.43 C110H138N22O34 ACHILMNPR Y 4.03 1 3 -2 10 4 -93.16 -3012 30 hour >20 hour >10 hour 15.26 11460 636.67 16616792 Virus Res. 2006 Sep;120(1-2):146-55. "Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. " Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein 10.1016/j.virusres.2006.03.001 Anti-SARS-CoV DRAVPe01422 AAHLIDALYAEFLGGRVLTTPVVHRALFYASAVLRQPFLAGVPSA 45 gH493-537(derived from HSV-1 H glycoprotein) Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Q9DHD5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Plaque assay [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(50-60% inhibition at 250μM-500μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. DRAVPe01422 DRAVPe01422.cif Linear Free Free None L mambrane The peptide inhibits virus entry and thus protects cells from infection. 4780.6 C224H349N59O57 CKMNW A 8.64 5 2 3 9 25 77.11 24 4.4 hour >20 hour >10 hour 121.56 2980 67.73 18572274 Peptides. 2008 Sep;29(9):1461-71. "Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M." Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. 10.1016/j.peptides.2008.04.022 Anti-HSV DRAVPe01423 AAHLIDALYAEFLGGRVLTT 20 gH493-512(derived from HSV-1 H glycoprotein) Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Q9DHD5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Plaque assay [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(60% inhibition at 250μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. DRAVPe01423 DRAVPe01423.cif Linear Free Free None L mambrane The peptide inhibits virus entry and thus protects cells from infection. 2131.46 C98H155N25O28 CKMNPQSW AL 5.32 2 2 0 5 11 78.5 35 4.4 hour >20 hour >10 hour 132 1490 78.42 18572274 Peptides. 2008 Sep;29(9):1461-71. "Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M." Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. 10.1016/j.peptides.2008.04.022 Anti-HSV DRAVPe01424 GLASTLTRWAHYNALIRAF 19 gH626-644(derived from HSV-1 H glycoprotein) Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Q9DHD5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Plaque assay [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(50-60% inhibition at 250μM-500μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. DRAVPe01424 DRAVPe01424.cif Linear Free Free None L mambrane The peptide inhibits virus entry and thus protects cells from infection. 2161.49 C100H153N29O25 CDEKMPQV A 10.84 3 0 3 6 10 28.42 -1665 30 hour >20 hour >10 hour 103.16 6990 388.33 18572274 Peptides. 2008 Sep;29(9):1461-71. "Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M." Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. 10.1016/j.peptides.2008.04.022 Anti-HSV DRAVPe01425 CCFLNITNSHVSILQERPPLENRVLTGWGL 30 Pcr-400 Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) P14075 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HTLV Retroviridae Luciferase assay [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=0.18 ± 0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01425 DRAVPe01425.cif Linear Acetylation Amidation None L mambrane The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. 3410.96 C151H241N43O43S2 ADKMY L 6.74 3 2 1 11 11 10.33 -3325 1.2 hour >20 hour >10 hour 110.33 5625 193.97 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  "Lamb D, Mirsaliotis A, Kelly SM, Brighty DW." Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. 10.1074/jbc.M806725200 Anti-HTLV DRAVPe01426 LNITNSHVSILQERPPLENRVL 22 Pcr-Δ8 Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) P14075 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HTLV Retroviridae Luciferase assay [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01426 DRAVPe01426.cif Linear Acetylation Amidation None L membrane The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. 2542.92 C111H188N34O34 ACDFGKMWY L 6.76 3 2 1 6 8 -27.73 -4535 5.5 hour 3 min 2 min 132.73 0 0 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  "Lamb D, Mirsaliotis A, Kelly SM, Brighty DW." Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. 10.1074/jbc.M806725200 Anti-HTLV DRAVPe01427 CFLNITNSHVSILQERPPLENRV 23 Pcr-Δ7 Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) P14075 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HTLV Retroviridae Luciferase assay [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=0.19± 0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01427 DRAVPe01427.cif Linear Acetylation Amidation None L membrane The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. 2680.08 C117H191N35O35S ADGKMWY LN 6.75 3 2 1 7 8 -20 -4601 1.2 hour >20 hour >10 hour 110 0 0 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  "Lamb D, Mirsaliotis A, Kelly SM, Brighty DW." Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. 10.1074/jbc.M806725200 Anti-HTLV DRAVPe01428 CFLNITNSHVSILQEAPPLENRV 23 Pcr-R416A Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) P14075 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HTLV Retroviridae Luciferase assay [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=1.55 ± 0.08 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01428 DRAVPe01428.cif Linear Acetylation Amidation None L membrane The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. 2594.97 C114H184N32O35S DGKMWY LN 5.4 2 2 0 7 9 7.39 -2928 1.2 hour >20 hour >10 hour 114.35 0 0 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  "Lamb D, Mirsaliotis A, Kelly SM, Brighty DW." Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. 10.1074/jbc.M806725200 Anti-HTLV DRAVPe01429 CFLNITNSHVSILQEAPPLENAV 23 Pcr-R422A Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) P14075 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HTLV Retroviridae Luciferase assay [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=8.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01429 DRAVPe01429.cif Linear Acetylation Amidation None L membrane The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. 2509.86 C111H177N29O35S DGKMRWY LN 4.51 1 2 -1 7 10 34.78 -1255 1.2 hour >20 hour >10 hour 118.7 0 0 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  "Lamb D, Mirsaliotis A, Kelly SM, Brighty DW." Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. 10.1074/jbc.M806725200 Anti-HTLV DRAVPe01430 KQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKK 49 G149-197(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01430 DRAVPe01430.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 5687.62 C253H395N75O67S4 LMY K 9.88 11 2 9 16 11 -107.35 -11980 1.3 hour 3 min 2 min 37.76 5750 119.79 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01431 FHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKK 35 G163-197(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01431 DRAVPe01431.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 4054.82 C185H282N50O45S4 DLMQY K 9.44 7 1 6 12 11 -28 -4511 1.1 hour 3 min 2 min 52.86 5750 169.12 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01432 VPCSICSNNPTCWAICKRIPNKKPGKK 27 G171-197(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>165 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01432 DRAVPe01432.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2986.62 C129H217N39O34S4 DEFHLMQY K 9.7 6 0 6 11 6 -55.56 -4296 100 hour >20 hour >10 hour 57.78 5750 221.15 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01433 CSICSNNPTCWAICKRIPNKKPGKK 25 G173-197(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>177 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01433 DRAVPe01433.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2790.37 C119H201N37O32S4 DEFHLMQVY K 9.7 6 0 6 11 5 -70.4 -4700 1.2 hour >20 hour >10 hour 50.8 5750 239.58 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01434 KQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 41 G149-189(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=12 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01434 DRAVPe01434.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 4809.54 C213H324N62O58S4 GLMY N 9.21 7 2 5 14 11 -72.93 -9190 1.3 hour 3 min 2 min 45.12 5750 143.75 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01435 KPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 36 G154-189(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=12 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01435 DRAVPe01435.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 4154.81 C187H278N50O50S4 GLMQY NP 8.52 5 2 3 13 11 -30.56 -5371 1.3 hour 3 min 2 min 51.39 5750 164.29 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01436 KPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 32 G158-189(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01436 DRAVPe01436.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 3745.32 C168H247N45O45S4 GLMQY N 7.89 4 2 2 12 11 -9.69 -4476 1.3 hour 3 min 2 min 57.81 5750 185.48 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01437 KQRQNKPPSKPNNDFHFEVFN 21 G149-169(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>190 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01437 DRAVPe01437.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2571.84 C115H171N35O33 ACGILMTWY N 9.7 5 2 3 5 4 -192.38 -7982 1.3 hour 3 min 2 min 13.81 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01438 KQRQNKPPSKPNNDFHF 17 G149-165(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>240 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01438 DRAVPe01438.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2082.31 C92H140N30O26 ACEGILMTVWY KNP 10.29 5 1 4 4 2 -237.65 -7339 1.3 hour 3 min 2 min 0 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01439 KPPSKPNNDFHFEVFNFVP 19 G154-172(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=220 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01439 DRAVPe01439.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2260.54 C108H150N26O28 ACGILMQRTWY FP 6.75 3 2 1 4 6 -84.74 -3461 1.3 hour 3 min 2 min 30.53 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01440 KPPSKPNNDFHFEVFNFV 18 G154-171(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=14 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01440 DRAVPe01440.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2163.42 C103H143N25O27 ACGILMQRTWY F 6.75 3 2 1 4 6 -80.56 -3461 1.3 hour 3 min 2 min 32.22 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01441 KPPSKPNNDFHFEVFNF 17 G154-170(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01441 DRAVPe01441.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 2064.29 C98H134N24O26 ACGILMQRTWY F 6.75 3 2 1 4 5 -110 -3865 1.3 hour 3 min 2 min 17.06 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01442 KPPSKPNNDFHFEVFN 16 G154-169(derived from RSV attachment glycoprotein) Synthetic construct(derived from RSV attachment glycoprotein) P03423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>510 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01442 DRAVPe01442.cif Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 1917.11 C89H125N23O25 ACGILMQRTWY FNP 6.75 3 2 1 4 4 -134.38 -4163 1.3 hour 3 min 2 min 18.13 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01443 KQRQNKPPSKPNNDFHFEVFNFVPBSIBG 29 G149-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01443 DRAVPe01443.cif Linear Acetylation Amidation "The 'B' at position 25,28 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 3401.86 C145H211N41O38 ACLMTWY FNP 9.7 5 2 3 7 7 -109.31 -7034 1.3 hour 3 min 2 min 33.45 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01444 KPPSKPNNDFHFEVFNFVPBSIBG 24 G154-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01444 DRAVPe01444.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2747.13 C119H165N29O30 ACLMQRTWY FP 6.75 3 2 1 6 7 -53.33 -3215 1.3 hour 3 min 2 min 40.42 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01445 KPNNDFHFEVFNFVPBSIBG 20 G158-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01445 DRAVPe01445.cif Linear Acetylation Amidation "The 'B' at position 16,19 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2337.65 C100H134N24O25 ACLMQRTWY F 5.32 2 2 0 5 7 -24.5 -2320 1.3 hour 3 min 2 min 48.5 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01446 DFHFEVFNFVPBSIBG 16 G162-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=60 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01446 DRAVPe01446.cif Linear Acetylation Amidation "The 'B' at position 12,15 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 1884.15 C81H103N17O19 ACKLMQRTWY F 4.35 1 2 -1 3 7 47.5 -437 1.1 hour 3 min >10 hour 60.63 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01447 EVFNFVPBSIBG 12 G166-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01447 DRAVPe01447.cif Linear Acetylation Amidation "The 'B' at position 8,11 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 1337.57 C53H73N11O13 ACDHKLMQRTWY FV 4 0 1 -1 3 5 72.5 305 1 hour 30 min >10 hour 80.83 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01448 FVPBSIBG 8 G170-177 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50》500 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01448 DRAVPe01448.cif Linear Acetylation Amidation "The 'B' at position 4,7 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 848.04 C30H42N6O6 ACDEHKLMNQRTWY FGIPSV 5.52 0 0 0 2 3 108.75 948 1.1 hour 3 min 2 min 85 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01449 KQRQNKPPSKPNNDFHFEVFNFVPB 25 G149-173 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01449 DRAVPe01449.cif Linear Acetylation Amidation The 'B' at position 25 is S-acetamidomethyl cysteine. L Not found No machanism information found in the reference(s) presented in this entry 3029.92 C134H194N38O35 ACGILMTWY FNP 9.7 5 2 3 5 6 -140 -7280 1.3 hour 3 min 2 min 23.2 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01450 KPPSKPNNDFHFEVFNFVPBSIAG 24 G154-177[B176A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01450 DRAVPe01450.cif Linear Acetylation Amidation The 'B' at position 20 is S-acetamidomethyl cysteine. L Not found No machanism information found in the reference(s) presented in this entry 2703.56 C122H172N30O32 CLMQRTWY FP 6.75 3 2 1 6 8 -45.83 -3034 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01451 KPPSKPNNDFHFEVFNFVPBSABG 24 G154-177[I175A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=22 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01451 DRAVPe01451.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2705.05 C116H159N29O30 CILMQRTWY FP 6.75 3 2 1 6 7 -64.58 -3526 1.3 hour 3 min 2 min 28.33 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01452 KPPSKPNNDFHFEVFNFVPBAIBG 24 G154-177[S174A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01452 DRAVPe01452.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2731.13 C119H165N29O29 CLMQRTWY FP 6.75 3 2 1 5 8 -42.5 -2694 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01453 KPPSKPNNDFHFEVFNFVPASIBG 24 G154-177[B173A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01453 DRAVPe01453.cif Linear Acetylation Amidation The 'B' at position 23 is S-acetamidomethyl cysteine. L Not found No machanism information found in the reference(s) presented in this entry 2703.56 C122H172N30O32 CLMQRTWY FP 6.75 3 2 1 6 8 -45.83 -3034 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01454 KPPSKPNNDFHFEVFNFVABSIBG 24 G154-177[P172A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01454 DRAVPe01454.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2721.09 C117H163N29O30 CLMQRTWY F 6.75 3 2 1 6 8 -39.17 -3034 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01455 KPPSKPNNDFHFEVFNFAPBSIBG 24 G154-177[V171A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01455 DRAVPe01455.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2719.08 C117H161N29O30 CLMQRTWY FP 6.75 3 2 1 6 7 -63.33 -3438 1.3 hour 3 min 2 min 32.5 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01456 KPPSKPNNDFHFEVFNAVPBSIBG 24 G154-177[F170A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=22 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01456 DRAVPe01456.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2671.03 C113H161N29O30 CLMQRTWY P 6.75 3 2 1 6 7 -57.5 -3332 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01457 KPPSKPNNDFHFEVFAFVPBSIBG 24 G154-177[N169A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01457 DRAVPe01457.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2704.11 C118H164N28O29 CLMQRTWY FP 6.75 3 2 1 5 8 -31.25 -2370 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01458 KPPSKPNNDFHFEVANFVPBSIBG 24 G154-177[F168A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=90 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01458 DRAVPe01458.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2671.03 C113H161N29O30 CLMQRTWY P 6.75 3 2 1 6 7 -57.5 -3332 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01459 KPPSKPNNDFHFEAFNFVPBSIBG 24 G154-177[V167A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01459 DRAVPe01459.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2719.08 C117H161N29O30 CLMQRTWY FP 6.75 3 2 1 6 7 -63.33 -3438 1.3 hour 3 min 2 min 32.5 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01460 KPPSKPNNDFHFAVFNFVPBSIBG 24 G154-177[E166A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=0.75 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01460 DRAVPe01460.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2689.1 C117H163N29O28 CELMQRTWY FP 8.6 3 1 2 6 8 -31.25 -2353 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01461 KPPSKPNNDFHAEVFNFVPBSIBG 24 G154-177[F165A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01461 DRAVPe01461.cif Linear Acetylation Amidation "The 'B' at position 20,23 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 2671.03 C113H161N29O30 CLMQRTWY P 6.75 3 2 1 6 7 -57.5 -3332 1.3 hour 3 min 2 min 44.58 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01462 KQRQNKPPSKPNNDFHFEVANAVPBSIBG 29 G149-177[F168/170A] Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae NMR [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>165 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01462 DRAVPe01462.cif Linear Acetylation Amidation "The 'B' at position 25,28 are S-acetamidomethyl cysteine." L Not found No machanism information found in the reference(s) presented in this entry 3249.66 C133H203N41O38 CLMTWY NP 9.7 5 2 3 7 7 -116.21 -7268 1.3 hour 3 min 2 min 40.34 0 0 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. "Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ. " Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. 10.1074/jbc.M106288200 Anti-RSV DRAVPe01463 DTRACDVIALLCHLNT 16 P1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "WNV,DENV" Flaviviridae RT-QPCR "[Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P1 significantly inhibited WNV infectivity at a concentration of 1 mM,IC50=67.0 ± 0.1 μM);##Dengue virus serotype 2:inhibition of virus infection in Vero cells(99.3±0.7% inhibition at 200 μM)" No hemolysis information or data found in the reference(s) presented in this entry [Ref.17151121]No cytotoxicity against Vero cells up to 500μM. DRAVPe01463 DRAVPe01463.cif Linear Free Free None L E proteins No machanism information found in the reference(s) presented in this entry 1758.04 C73H124N22O24S2 EFGKMPQSWY L 5.21 2 2 0 5 7 56.88 -1890 1.1 hour 3 min >10 hour 128.13 125 8.33 17151121 J Virol. 2007 Feb;81(4):2047-55.  "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 "Anti-WNV,Anti-DENV" DRAVPe01464 CDVIALLCHLNT 12 P8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None WNV Flaviviridae RT-QPCR [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01464 DRAVPe01464.cif Linear Free Free None L E proteins No machanism information found in the reference(s) presented in this entry 1314.58 C56H95N15O17S2 EFGKMPQRSWY L 5.08 1 1 0 4 6 133.33 550 1.2 hour >20 hour >10 hour 162.5 125 11.36 17151121 J Virol. 2007 Feb;81(4):2047-55.  "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 Anti-WNV DRAVPe01465 CDVIALLACHLNT 13 P9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None WNV Flaviviridae RT-QPCR "[Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(96.3±2.8% inhibition at 100 μM,IC50=2.60 ± 0.01 μM);inhibition of virus entry in Vero cells(65.2±14.5% inhibition at 100 μM);inhibition of virus attachment to Vero cells(96.3±2.7% inhibition at 1mM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.17151121]No cytotoxicity against Vero cells up to 500μM. DRAVPe01465 DRAVPe01465.cif Linear Free Free None L E proteins P9 blocked cirus attachment 1385.66 C59H100N16O18S2 EFGKMPQRSWY L 5.08 1 1 0 4 7 136.92 731 1.2 hour >20 hour >10 hour 157.69 125 10.42 17151121 J Virol. 2007 Feb;81(4):2047-55.  "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 Anti-WNV DRAVPe01466 CDVIALLCHLNTPSF 15 P10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae RT-QPCR [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01466 DRAVPe01466.cif Linear Free Free None L E proteins No machanism information found in the reference(s) presented in this entry 1645.95 C73H116N18O21S2 EGKMQRWY L 5.08 1 1 0 5 7 109.33 508 1.2 hour >20 hour >10 hour 130 125 8.93 17151121 J Virol. 2007 Feb;81(4):2047-55.  "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 Anti-WNV DRAVPe01467 CDVIALLCHLNTPSFNTTHYRESWY 25 P11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae RT-QPCR [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01467 DRAVPe01467.cif Linear Free Free None L E proteins No machanism information found in the reference(s) presented in this entry 2984.35 C134H195N35O39S2 GKMQ LT 5.99 3 2 1 11 8 -16 -3444 1.2 hour >20 hour >10 hour 78 8605 358.54 17151121 J Virol. 2007 Feb;81(4):2047-55.  "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 Anti-WNV DRAVPe01468 SSCNMGWDTPACCVWFPYWV 20 A4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae GFP assay [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(70% inhibition). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01468 DRAVPe01468.cif Linear Free Free None L pUL84(nonconventional nuclear localization signal of the essential viral replication factor) The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. 2352.7 C108H142N24O28S4 EHIKLQR CW 3.8 0 1 -1 9 7 27.5 212 1.9 hour >20 hour >10 hour 34 18115 953.42 19740994 J Virol. 2009 Nov;83(22):11902-13.  "Kaiser N, Lischka P, Wagenknecht N, Stamminger T." Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. 10.1128/JVI.01378-09 Anti-HCMV DRAVPe01469 MAVGLVLCDWWLGEYLLEA 19 A8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae GFP assay [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(70% inhibition). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01469 DRAVPe01469.cif Linear Free Free None L pUL84(nonconventional nuclear localization signal of the essential viral replication factor) The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. 2181.59 C103H153N21O27S2 FHIKNPQRST L 3.57 0 3 -3 4 11 110.53 2399 30 hour >20 hour >10 hour 143.68 12490 693.89 19740994 J Virol. 2009 Nov;83(22):11902-13.  "Kaiser N, Lischka P, Wagenknecht N, Stamminger T." Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. 10.1128/JVI.01378-09 Anti-HCMV DRAVPe01470 PVLQPALSLSCGPEPLLLSC 20 A56 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae GFP assay [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(40% inhibition). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01470 DRAVPe01470.cif Linear Free Free None L pUL84(nonconventional nuclear localization signal of the essential viral replication factor) The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. 2037.46 C91H153N21O27S2 DFHIKMNRTWY L 4 0 1 -1 6 8 88 1632 >20 hour >20 hour ? 136.5 125 6.58 19740994 J Virol. 2009 Nov;83(22):11902-13.  "Kaiser N, Lischka P, Wagenknecht N, Stamminger T." Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. 10.1128/JVI.01378-09 Anti-HCMV DRAVPe01471 IEVTFVNRRGDGAELWYLSA 20 A110 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae GFP assay [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(35% inhibition). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01471 DRAVPe01471.cif Linear Free Free None L pUL84(nonconventional nuclear localization signal of the essential viral replication factor) The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. 2296.57 C104H158N28O31 CHKMPQ AEGLRV 4.68 2 3 -1 6 9 -3 -3128 20 hour 30 min >10 hour 97.5 6990 367.89 19740994 J Virol. 2009 Nov;83(22):11902-13.  "Kaiser N, Lischka P, Wagenknecht N, Stamminger T." Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. 10.1128/JVI.01378-09 Anti-HCMV DRAVPe01472 SFAIKWEYVLLLFLL 15 Peptide 75(710-725)[Δ1] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(91% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01472 DRAVPe01472.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1855.29 C96H143N17O20 CDGHMNPQRT L 5.72 1 1 0 2 11 164.67 2776 1.9 hour >20 hour >10 hour 182 6990 499.29 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01473 FAIKWEYVLLLFLL 14 Peptide 75(710-725)[Δ1-2] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(95% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01473 DRAVPe01473.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1768.22 C93H138N16O18 CDGHMNPQRST L 6 1 1 0 1 11 182.14 3116 1.1 hour 3 min 2 min 195 6990 537.69 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01474 AIKWEYVLLLFLL 13 Peptide 75(710-725)[Δ1-3] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(92% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01474 DRAVPe01474.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1621.04 C84H129N15O17 CDGHMNPQRST L 6.05 1 1 0 1 10 174.62 2818 4.4 hour >20 hour >10 hour 210 6990 582.5 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01475 IKWEYVLLLFLL 12 Peptide 75(710-725)[Δ1-4] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(88% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01475 DRAVPe01475.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1549.96 C81H124N14O16 ACDGHMNPQRST L 6 1 1 0 1 9 174.17 2637 20 hour 30 min >10 hour 219.17 6990 635.45 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01476 KWEYVLLLFLL 11 Peptide 75(710-725)[Δ1-5] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(78% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01476 DRAVPe01476.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1436.8 C75H113N13O15 ACDGHIMNPQRST L 6 1 1 0 1 8 149.09 2145 1.3 hour 3 min 2 min 203.64 6990 699 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01477 WEYVLLLFLL 10 Peptide 75(710-725)[Δ1-6] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(82% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01477 DRAVPe01477.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1308.63 C69H101N11O14 ACDGHIKMNPQRST L 4 0 1 -1 1 8 203 2700 2.8 hour 3 min 2 min 224 6990 776.67 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01478 VSFAIKWEYVLLLFL 15 Peptide 75(710-725)[Δ16] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(63% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01478 DRAVPe01478.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1841.27 C95H141N17O20 CDGHMNPQRT L 5.97 1 1 0 2 11 167.33 2688 100 hour >20 hour >10 hour 175.33 6990 499.29 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01479 VSFAIKWEYVLLLF 14 Peptide 75(710-725)[Δ15-16] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(49% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01479 DRAVPe01479.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1728.11 C89H130N16O19 CDGHMNPQRT L 5.97 1 1 0 2 10 152.14 2196 100 hour >20 hour >10 hour 160 6990 537.69 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01480 VSFAIKWEYVLLL 13 Peptide 75(710-725)[Δ14-16] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(49% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01480 DRAVPe01480.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1580.93 C80H121N15O18 CDGHMNPQRT L 5.97 1 1 0 2 9 142.31 1898 100 hour >20 hour >10 hour 172.31 6990 582.5 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01481 VSFAIKWEYVLL 12 Peptide 75(710-725)[Δ13-16] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(44% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01481 DRAVPe01481.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1467.77 C74H110N14O17 CDGHMNPQRT LV 5.97 1 1 0 2 8 122.5 1406 100 hour >20 hour >10 hour 154.17 6990 635.45 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01482 VSFAIKWEYVL 11 Peptide 75(710-725)[Δ12-16] Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(17% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01482 DRAVPe01482.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1354.61 C68H99N13O16 CDGHMNPQRT V 5.97 1 1 0 2 7 99.09 914 100 hour >20 hour >10 hour 132.73 6990 699 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01483 VSFAIKWEYVLLLFLL 16 Peptide 75(710-725) Synthetic construct(derived from HCV envelope protein) P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay "[Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(EC50=0.3 ± 0.4 μM,EC90=14 ± 12 μM);inhibition of virus infection in primary human hepatocytes(EC50=0.3μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.20156485]No cytotoxicity against Huh-7 cells. DRAVPe01483 DRAVPe01483.cif Linear Free Free None L envelope protein The peptide inhibits a post-binding step in HCV entry. 1954.43 C101H152N18O21 CDGHMNPQRT L 5.97 1 1 0 2 12 180.63 3180 100 hour >20 hour >10 hour 188.75 6990 466 20156485 Antiviral Res. 2010 May;86(2):172-9. "Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R." A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  10.1016/j.antiviral.2010.02.316 Anti-HCV DRAVPe01484 RWMVWRHWFHRLRLPYNPGKNKQNQQWP 28 DN57opt Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus reduction assay "[Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=8±1 μM,97% inhibition at 20μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.20582308]the peptide was found to be mildly toxic to LLC-MK2 cells at 40 µM. DRAVPe01484 DRAVPe01484.cif Linear Free Free None L E glycoprotein "The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein." 3760.35 C176H252N56O36S ACDEIST RW 12.01 8 0 8 5 8 -167.14 -8731 1 hour 2 min 2 min 38.21 23490 870 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  "Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF." Structural optimization and de novo design of dengue virus entry inhibitory peptides. 10.1371/journal.pntd.0000721 Anti-DENV DRAVPe01485 RQMRAWGQDYQHGGMGYSC 19 DN81opt Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus reduction assay "[Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=36±6 μM,57% inhibition at 50μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01485 DRAVPe01485.cif Linear Free Free None L E glycoprotein "The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein." 2231.47 C93H135N31O28S3 EFIKLNPTV G 8.21 3 1 2 8 2 -126.32 -4964 1 hour 2 min 2 min 5.26 8480 471.11 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  "Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF." Structural optimization and de novo design of dengue virus entry inhibitory peptides. 10.1371/journal.pntd.0000721 Anti-DENV DRAVPe01486 FWFTLIKTQAKQPARYRRFC 20 1OAN1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus reduction assay "[Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=7±4 μM,99% inhibition at 50 μM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.20582308]the peptide showed no toxic to LLC-MK2 cells at 50 µM. DRAVPe01486 DRAVPe01486.cif Linear Free Free None L E glycoprotein "The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein." 2561.05 C121H182N34O26S DEGHMNSV FR 11.01 5 0 5 4 8 -53.5 -4621 1.1 hour 3 min 2 min 49 6990 367.89 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  "Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF." Structural optimization and de novo design of dengue virus entry inhibitory peptides. 10.1371/journal.pntd.0000721 Anti-DENV DRAVPe01487 LLDCWVRLGRYLLRRLKT 18 GBVA1(1-18) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=10 μM,88% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01487 DRAVPe01487.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2274.8 C104H176N32O23S AEFHIMNPQS L 10.85 5 1 4 4 8 4.44 -3855 5.5 hour 3 min 2 min 146.11 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01488 LLDCWVRLGRYLLRRLKTPFTRL 23 GBVA2(1-23) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=15 μM,50% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01488 DRAVPe01488.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2889.55 C134H222N40O29S AEHIMNQS L 11.44 6 1 5 5 10 2.61 -4814 5.5 hour 3 min 2 min 131.3 6990 317.73 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01489 LLDCWVRLGRYLLRRLKTPFT 21 GBVA3(1-21) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01489 DRAVPe01489.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2620.2 C122H199N35O27S AEHIMNQS L 10.85 5 1 4 5 9 6.19 -3814 5.5 hour 3 min 2 min 125.24 6990 349.5 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01490 LLDCWVRLGRYLLRRLKTP 19 GBVA4(1-19) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=3 μM,99% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01490 DRAVPe01490.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2371.92 C109H183N33O24S AEFHIMNQS L 10.85 5 1 4 4 8 -4.21 -3855 5.5 hour 3 min 2 min 138.42 6990 388.33 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01491 LLDCWVRLGRYLLRRLK 17 GBVA5(1-17) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=5 μM,99% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01491 DRAVPe01491.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2173.7 C100H169N31O21S AEFHIMNPQST L 10.85 5 1 4 3 8 8.82 -3598 5.5 hour 3 min 2 min 154.71 6990 436.88 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01492 LDCWVRLGRYLLRRLKTPFTRL 22 GBVA6(2-23) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0 inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01492 DRAVPe01492.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2776.39 C128H211N39O28S AEHIMNQS L 11.44 6 1 5 5 9 -14.55 -5306 5.5 hour 3 min 2 min 119.55 6990 332.86 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01493 CWVRLGRYLLRRLKTPFTRL 20 GBVA7(4-23) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,89% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01493 DRAVPe01493.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2548.14 C118H195N37O24S ADEHIMNQS LR 11.83 6 0 6 5 8 -17.5 -4926 1.2 hour >20 hour >10 hour 112 6990 367.89 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01494 LDCWVRLGRYLLRRLKTP 18 GBVA8(2-19) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=4 μM,99% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01494 DRAVPe01494.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2258.76 C103H172N32O23S AEFHIMNQS L 10.85 5 1 4 4 7 -25.56 -4347 5.5 hour 3 min 2 min 124.44 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01495 DCWVRLGRYLLRRLKTPF 18 GBVA9(3-20) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,90% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01495 DRAVPe01495.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2292.78 C106H170N32O23S AEHIMNQS LR 10.85 5 1 4 4 7 -31.11 -4541 1.1 hour 3 min >10 hour 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01496 CWVRLGRYLLRRLKTPFT 18 GBVA10(4-21) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2 μM,100% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01496 DRAVPe01496.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2278.79 C106H172N32O22S ADEHIMNQS LR 11.56 5 0 5 5 7 -15.56 -3926 1.2 hour >20 hour >10 hour 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01497 WVRLGRYLLRRLKTPFTR 18 GBVA11(5-22) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,58% inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01497 DRAVPe01497.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2331.84 C109H179N35O22 ACDEHIMNQS R 12.18 6 0 6 4 7 -54.44 -5546 2.8 hour 3 min 2 min 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01498 VRLGRYLLRRLKTPFTRL 18 GBVA12(6-23) Synthetic construct(derived from GBVA non-structutal protein 5A) Q69422 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay "[Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0 inhibition at 20 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01498 DRAVPe01498.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2258.79 C104H180N34O22 ACDEHIMNQSW LR 12.18 6 0 6 4 7 -28.33 -5287 100 hour >20 hour >10 hour 124.44 1490 87.65 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01499 CWVRLGRYKLRRLKTPFT 18 GBVA10-1(L9K) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01499 DRAVPe01499.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2293.81 C106H173N33O22S ADEHIMNQS R 11.57 6 0 6 5 6 -58.33 -4973 1.2 hour >20 hour >10 hour 81.11 6990 411.18 23175360 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01500 CWVRLGRYSLRRLKTPFT 18 GBVA10-2(L9S) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=18 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01500 DRAVPe01500.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2252.71 C103H166N32O23S ADEHIMNQ R 11.56 5 0 5 6 6 -41.11 -4758 1.2 hour >20 hour >10 hour 81.11 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01501 CWVRLGRYALRRLKTPFT 18 GBVA10-3(L9A) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01501 DRAVPe01501.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2236.71 C103H166N32O22S DEHIMNQS R 11.56 5 0 5 5 7 -26.67 -4237 1.2 hour >20 hour >10 hour 86.67 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01502 CWVRLGRYVLRRLKTPFT 18 GBVA10-4(L9V) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=16 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01502 DRAVPe01502.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2264.77 C105H170N32O22S ADEHIMNQS R 11.56 5 0 5 5 7 -13.33 -4014 1.2 hour >20 hour >10 hour 97.22 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01503 CWVRLARYLLRRLKTPFT 18 GBVA10-5(G6A) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01503 DRAVPe01503.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2292.82 C107H174N32O22S DEGHIMNQS LR 11.56 5 0 5 4 8 -3.33 -3839 1.2 hour >20 hour >10 hour 108.33 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01504 CWVRLVRYLLRRLKTPFT 18 GBVA10-6(G6V) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01504 DRAVPe01504.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2320.87 C109H178N32O22S ADEGHIMNQS LR 11.56 5 0 5 4 8 10 -3616 1.2 hour >20 hour >10 hour 118.89 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01505 CWVRLLRYLLRRLKTPFT 18 GBVA10-7(G6L) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01505 DRAVPe01505.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2334.9 C110H180N32O22S ADEGHIMNQS L 11.56 5 0 5 4 8 7.78 -3528 1.2 hour >20 hour >10 hour 124.44 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01506 CWVRLLRYLLRRLKTLFT 18 GBVA10-8(G6L/P16L) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01506 DRAVPe01506.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2350.94 C111H184N32O22S ADEGHIMNPQS L 11.56 5 0 5 4 9 37.78 -3036 1.2 hour >20 hour >10 hour 146.11 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01507 CWVRLGRYLLRRLKTLFT 18 GBVA10-9(P16L) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=0.16 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.23175359]HepG2 cell:LC50=90 μM(4h of treatment);##HeLa cell:LC50=40 μM(4h of treatment);##Huh7.5.1 cell:LC50=90 μM(4h of treatment);LC50=50 μM(24h of treatment). DRAVPe01507 DRAVPe01507.cif Linear Free Free None L Not found GBVA10-9 can inhibit virus entry at a postattachment step. 2294.84 C107H176N32O22S ADEHIMNPQS L 11.56 5 0 5 5 8 14.44 -3434 1.2 hour >20 hour >10 hour 124.44 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01508 CWVRLGRYILRRLKTPFT 18 GBVA10-10(L9I) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01508 DRAVPe01508.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2278.79 C106H172N32O22S ADEHMNQS R 11.56 5 0 5 5 7 -11.67 -3926 1.2 hour >20 hour >10 hour 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01509 CWVRLGRYILRRIKTPFT 18 GBVA10-11(L9I/L13I) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=0.63 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01509 DRAVPe01509.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2278.79 C106H172N32O22S ADEHMNQS R 11.56 5 0 5 5 7 -7.78 -3926 1.2 hour >20 hour >10 hour 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01510 CWVRIGRYILRRIKTPFT 18 GBVA10-12(L5I/L9I/L13I) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01510 DRAVPe01510.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2278.79 C106H172N32O22S ADEHMNQS R 11.56 5 0 5 5 7 -3.89 -3926 1.2 hour >20 hour >10 hour 102.78 6990 411.18 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01511 KWVRLGRKLLRRLKKPFK 18 GBVA10-13(C1K/Y8K/T15K/T18K) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01511 DRAVPe01511.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2322.96 C110H192N36O19 ACDEHIMNQSTY K 12.49 9 0 9 1 7 -101.11 -5746 1.3 hour 3 min 2 min 102.78 5500 323.53 23175361 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01512 KWVRLGRKLLRRLKKPFT 18 GBVA10-14(C1K/Y8K/T15K) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01512 DRAVPe01512.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2295.9 C108H187N35O20 ACDEHIMNQSY KLR 12.48 8 0 8 2 7 -83.33 -5448 1.3 hour 3 min 2 min 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01513 CWVRLGRKLLRRLKKPFT 18 GBVA10-15(Y8K/T15K) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01513 DRAVPe01513.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2270.86 C105H180N34O20S ADEHIMNQSY LR 12.01 7 0 7 3 7 -47.78 -4765 1.2 hour >20 hour >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01514 CWVRLGRKLLRRLKTPFT 19 GBVA10-16(Y8K) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01514.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2243.79 C103H175N33O21S ADEHIMNQSY LR 12.01 6 0 6 4 7 -30 -4467 1.2 hour >20 hour >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01515 EWVRLGRELLRRLKEPFT 18 GBVA10-17(C1E/Y8E/T15E) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01515 DRAVPe01515.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2298.72 C105H172N32O26 ACDHIMNQSY LR 10.67 5 3 2 2 7 -76.67 -5826 1 hour 30 min >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01516 EWVRLGRELLRRLKEPFE 19 GBVA10-18(C1E/Y8E/T15E/T18E) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available DRAVPe01516.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2326.73 C106H172N32O27 ACDHIMNQSTY ELR 8.84 5 4 1 1 7 -92.22 -6250 1 hour 30 min >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01517 CWVRLGRELLRRLKEPFT 18 GBVA10-19(Y8E/T15E) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01517 DRAVPe01517.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2272.74 C103H170N32O24S ADHIMNQSY LR 10.69 5 2 3 3 7 -43.33 -5017 1.2 hour >20 hour >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01518 CWVRLGRELLRRLKTPFT 18 GBVA10-20(Y8E) Synthetic construct(derived from GBVA non-structutal protein 5A) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae qRT-PCR assay [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01518 DRAVPe01518.cif Linear Free Free None L Not found The peptide inhibits virus entry. 2244.73 C102H170N32O23S ADHIMNQSY LR 11.54 5 1 4 4 7 -27.78 -4593 1.2 hour >20 hour >10 hour 102.78 5500 323.53 23175359 J Virol. 2013 Feb;87(3):1649-57. "Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W." Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. 10.1128/JVI.02201-12 Anti-HCV DRAVPe01519 IPESSELTLQELLGEERR 18 E6ap18 Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=10.5±1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01519 DRAVPe01519.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 2099.33 C89H151N25O33 ACDFHKMNVWY E 4.33 2 5 -3 4 5 -81.11 -5326 20 hour 30 min >10 hour 108.33 0 0 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01520 YKFACPECPKRFMRSDHLTLHILLHENKK 29 E6apc1 Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50>1000 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01520 DRAVPe01520.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 3556.23 C160H252N46O40S3 GQVW KL 9.24 9 3 6 6 8 -69.66 -6383 2.8 hour 10 min 2 min 70.69 1615 57.68 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01521 YKFACPECPKRFMRSDHLSKHITLHELLGEERR 33 E6apc2 Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=19.3±2.9μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01521 DRAVPe01521.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 4028.68 C177H280N54O48S3 NQVW ELR 8.82 10 5 5 7 8 -90.91 -9756 2.8 hour 10 min 2 min 62.12 1615 50.47 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01522 ALQELLGQWLKDGGPSSGRPPPS 23 E6apn1 Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=36.8±3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01522 DRAVPe01522.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 2390.68 C106H168N30O33 CFHIMNTVY GLP 6.11 2 2 0 7 6 -72.61 -2970 4.4 hour >20 hour >10 hour 72.17 5500 250 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01523 ALQELLGEYIQWLKDGGPSSGRPPPS 26 E6apn2 Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=26.2±4.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01523 DRAVPe01523.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 2796.13 C126H195N33O39 CFHMNTV GLP 4.68 2 3 -1 8 7 -65.38 -3173 4.4 hour >20 hour >10 hour 78.85 6990 279.6 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01524 YLQELLGE 8 E6apm Synthetic construct(derived from E6-associated protein (E6AP)) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae CD spectroscopy [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=74.3±1.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01524 DRAVPe01524.cif Linear Acetylation Amidation None L E6 protein No machanism information found in the reference(s) presented in this entry 964.08 C44H69N9O15 ACDFHIKMNPRSTVW L 3.79 0 2 -2 2 3 -10 -360 2.8 hour 10 min 2 min 146.25 1490 212.86 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  "Liu Y, Liu Z, Androphy E, Chen J, Baleja JD." Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. 10.1021/bi049552a Anti-HPV DRAVPe01525 LLPIVGNLLKSLL 13 Temporin B Rana temporaria(European common frog) P79874 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 6GIL HSV Herpesviridae [Ref.29483113]Herpes simplex virus 1 (HSV-1):viral titer inhibition on Vero cells(IC50=2.507 μg/ml);inhibition of HSV-1 replication in HeLa S3 cells(IC50=93 μg/ml);inhibition of HSV-1 replication in HEK-293 cells(IC50=84 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29483113]Vero cells:CC50=90.4μg/ml;##no toxicity was observed at concentrations as high as 50 μg/ml against HeLa S3 and HEK-293 cells. DRAVPe01525 DRAVPe01525.cif Linear Free Amidation None L envelope "Temporin B could disrupt the envelope of virus,and partially affected different stages of the HSV-1 life cycle, including the attachment and the entry of the virus into the host cell, as well as the subsequent postinfection phase." 1392.79 C67H121N15O16 ACDEFHMQRTWY L 8.75 1 0 1 3 8 163.85 2383 5.5 hour 3 min 2 min 232.31 0 0 29483113 Antimicrob Agents Chemother. 2018 Apr 26;62(5):e02367-17. "Marcocci ME, Amatore D, Villa S, Casciaro B, Aimola P, Franci G, Grieco P, Galdiero M, Palamara AT, Mangoni ML, Nencioni L. " The Amphibian Antimicrobial Peptide Temporin B Inhibits In Vitro Herpes Simplex Virus 1 Infection. 10.1128/AAC.02367-17 Anti-HSV DRAVPe01526 VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR 32 RatNP-1 Rattus norvegicus Q62716 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.12543649]HSV-2:inhibition of HSV-2 infection in Vero cells(98.7%±0.7% inhibition at 25 μg/ ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.12543649]No cytotoxic effect on CaSki cells was observed at the concentration of 25 or 100 μg/ml. DRAVPe01526 DRAVPe01526.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30." L membrane NP-1 inactivates HSV and prevents viral entry and cell-to-cell spread. NP-1 blocks fusion events important in HSV acquisition and transmission. 3835.54 C158H261N59O41S6 DHKMNPQW R 9.99 9 1 8 16 6 -49.38 -11502 100 hour >20 hour >10 hour 48.75 4845 156.29 12543649 Antimicrob Agents Chemother. 2003 Feb;47(2):494-500. "Sinha S, Cheshenko N, Lehrer RI, Herold BC." "NP-1, a rabbit alpha-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2. " 10.1128/AAC.47.2.494-500.2003 Anti-HSV DRAVPe01527 FLSGIVGMLGKLF 13 "Temporin-SHa (temporin SHa; Temporin-1Sa, Temp-1Sa; XXA; UCLL1c; natural AMPs; frog, amphibians, animals)" "Pelophylax saharica, North Africa" B3KYH4 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae [Ref.30669255]HSV-1:inhibition of HSV-1 replication in human keratinocytes(52% inhibition at 10 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30669255]Significant cytotoxicity was observed on Keratinocyte at the concentration of 20 μM with a cell viability of 77% DRAVPe01527 DRAVPe01527.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1381.74 C67H108N14O15S ACDEHNPQRTWY GL 8.75 1 0 1 4 7 166.92 2590 1.1 hour 3 min 2 min 142.31 0 0 30669255 Viruses. 2019 Jan 18;11(1):77. "Roy M, Lebeau L, Chessa C, Damour A, Ladram A, Oury B, Boutolleau D, Bodet C, Lévêque N. " Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1. 10.3390/v11010077 Anti-HSV DRAVPe01528 FLKGIVGMLGKLF 13 Temporin-Sha[K3] Synthetic construct(derived from Temporin-SHa) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae "[Ref.30669255]HSV-1:inhibition of HSV-1 replication in human keratinocytes(48% inhibition at 2.5 µM,57% inhibition at 5 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30669255]Significant cytotoxicity was observed on Keratinocyte at the concentration of 10 μM with a cell viability of 74%. DRAVPe01528 DRAVPe01528.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1422.84 C70H115N15O14S ACDEHNPQRSTWY GL 10 2 0 2 3 7 143.08 2375 1.1 hour 3 min 2 min 142.31 0 0 30669255 Viruses. 2019 Jan 18;11(1):77. "Roy M, Lebeau L, Chessa C, Damour A, Ladram A, Oury B, Boutolleau D, Bodet C, Lévêque N. " Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1. 10.3390/v11010077 Anti-HSV DRAVPe01529 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 LL-37 (human cathelicidin LL-37) "neutrophils, monocytes; mast cells; lymphocytes, Mesenchymal Stem Cells; islets; skin, sweat; airway surface liquid, saliva; Homo sapiens; Also Pan troglodytes" P49913 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available 2K6O "HSV, EBOV" "Herpesviridae, Filoviridae" Plaque assay "[Ref.30669255]HSV-1:inhibition of HSV-1 replication in human keratinocytes(75% inhibition at 1.25 µM,94% inhibition at 2.5 µM).##[Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=4.03 µM);inhibition of viral infection in primary macrophages(IC50>20 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30669255]Significant cytotoxicity was observed on Keratinocyte at the concentration of 5 μM with a cell viability of 80%. DRAVPe01529 DRAVPe01529.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) None L Not found "Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry." 4493.32 C205H340N60O53 ACHMWY K 10.61 11 5 6 6 13 -72.43 -11100 5.5 hour 3 min 2 min 89.46 0 0 30669255##32252021 Viruses. 2019 Jan 18;11(1):77.##iScience. 2020 Apr 24;23(4):100999. "Roy M, Lebeau L, Chessa C, Damour A, Ladram A, Oury B, Boutolleau D, Bodet C, Lévêque N. ##Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K." Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1.##Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. 10.3390/v11010077##10.1016/j.isci.2020.100999 "Anti-HSV, Anti-EBOV" DRAVPe01530 LLGDLLRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 "LL-37[F5,6L]" Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=18.4 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01530 DRAVPe01530.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 4425.29 C199H344N60O53 ACHMWY KL 10.61 11 5 6 6 13 -67.03 -10712 5.5 hour 3 min 2 min 110.54 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01531 LLGDLLRKSKEKIGKEFKRIVQR 23 LL-23 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>35.4 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50>35.4 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01531 DRAVPe01531.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2755.35 C124H220N38O32 ACHMNPTWY K 10.55 8 3 5 3 8 -75.65 -6537 5.5 hour 3 min 2 min 114.35 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01532 KRIVQRIKDFLRNLVPRTES 20 KR-20 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>40.5 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50>40.5 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01532 DRAVPe01532.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2468.93 C109H190N36O29 ACGHMWY R 11.55 6 2 4 3 7 -75.5 -7372 1.3 hour 3 min 2 min 107 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01533 SKEKIGKEFKRIVQRIKDFLR 21 SK-21 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=10.8 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=22.5 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01533 DRAVPe01533.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2619.15 C119H204N36O30 ACHMNPTWY K 10.55 8 3 5 2 7 -100.48 -7317 1.9 hour >20 hour >10 hour 88.1 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01534 FKRIVQRIKDFLR 13 FK-13 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=3.4 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=10.4 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01534 DRAVPe01534.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1719.11 C80H135N25O17 ACEGHMNPSTWY R 11.72 5 1 4 0 6 -43.85 -4536 1.1 hour 3 min 2 min 112.31 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01535 RLFDKIRQVIRKF 13 Retro-FK-13 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>58.1 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=33.7 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01535 DRAVPe01535.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1719.11 C80H135N25O17 ACEGHMNPSTWY R 11.72 5 1 4 0 6 -43.85 -4536 1 hour 2 min 2 min 112.31 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01536 KRIVQRIKDFLR 12 KR-12 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>63.5 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50>63.5 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01536 DRAVPe01536.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1571.93 C71H126N24O16 ACEGHMNPSTWY R 11.72 5 1 4 0 5 -70.83 -4834 1.3 hour 3 min 2 min 121.67 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01537 SKVNGQSGRMEFFWTILK 18 HA-pep25 Synthetic construct(derived from influenza viral HA) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Infection assay [Ref.27623031]Influenza A Virus(A/PuertoRico/8/1934):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=34.0 ± 11.5μM);##AInfluenza A Virus(/Vietnam/1203/2004):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=12.0 ± 2.1μM);##influenza A virus(A/Goose/Qinghai/59/2005):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=34.8 ± 1.5μM);##influenza A virus(A/Duck/Anhui/SC702/2013):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=51.0 ± 0.6μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01537.cif Linear Free Free None L HA receptor binding domain (RBD) Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. 2128.48 C97H150N26O26S ACDHPY FGKS 9.99 3 1 2 6 6 -37.78 -2798 1.9 hour >20 hour >10 hour 59.44 5500 323.53 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 "Chen Q, Guo Y" Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor 10.1021/acsinfecdis.5b00139 Anti-Influenza A virus DRAVPe01538 GFKRIVQRiKDFLRNLV 17 GF-17d1 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>47.5 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=22.7 μM.(TC50:the concentration that reduced cell viability by 50%) No predicted structure available DRAVPe01538.cif Linear Free Free None Mixed(D-Ile9) Not found No machanism information found in the reference(s) presented in this entry 2102.56 C91H151N29O20 ACEHMPSTWY R 11.72 5 1 4 2 7 -35.88 -4702 30 hour >20 hour >10 hour 102.94 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01539 GFKRIVQRiKDFlRNLV 17 GF-17d2 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>47.5μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50>47.5 μM.(TC50:the concentration that reduced cell viability by 50%) No predicted structure available DRAVPe01539.cif Linear Free Free None "Mixed(D-Ile9,D-Leu13)" Not found No machanism information found in the reference(s) presented in this entry 2102.56 C85H138N28O18 ACEHMPSTWY R 11.72 5 1 4 2 6 -58.24 -5194 30 hour >20 hour >10 hour 80 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01540 GIKEFKRIVQRIKDFLRNLV 20 GI-20 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.08 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=22.7 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01540 DRAVPe01540.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2473.01 C114H194N34O27 ACHMPSTWY IKR 11 6 2 4 2 9 -22.5 -4954 30 hour >20 hour >10 hour 126.5 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01541 GIKEXKRIVQRIKDFLRNLV 20 GI-20X17 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>40.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=7.3 μM.(TC50:the concentration that reduced cell viability by 50%) No predicted structure available DRAVPe01541.cif Linear Free Free The 'X' at position 5 is phenylglycine L Not found No machanism information found in the reference(s) presented in this entry 2437.16 C105H183N33O25 ACHMPSTWY IKR 11 6 2 4 2 8 -36.5 -5252 30 hour >20 hour >10 hour 126.5 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01542 GIKEWKRIVQRIKDFLRNLV 20 GI-20W17 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=7.4 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=23.6 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01542 DRAVPe01542.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2512.04 C116H195N35O27 ACHMPSTY IKR 11 6 2 4 2 9 -41 -5019 30 hour >20 hour >10 hour 126.5 5500 289.47 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01543 GIKQFKRIVQRIKDFLRNLV 20 GI-20Q16 Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.91 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=13.7 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01543 DRAVPe01543.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2472.02 C114H195N35O26 ACEHMPSTWY IKR 11.73 6 1 5 2 9 -22.5 -4827 30 hour >20 hour >10 hour 126.5 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01544 GIKEFKREFQRIKDFLRNLV 20 GI-20EF Synthetic construct(derived from human cathelicidin LL-37) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=9.9 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01544 DRAVPe01544.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2537.01 C117H190N34O29 ACHMPSTWY FKR 10.27 6 3 3 2 8 -69.5 -6233 30 hour >20 hour >10 hour 92.5 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01545 GRFKRFRKKFKKLFKKIS 18 BMAP-18 Synthetic construct(derived from BMAP-27) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.35 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=8.45 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01545 DRAVPe01545.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2342.95 C113H188N34O20 ACDEHMNPQTVWY K 12.32 10 0 10 2 6 -125 -6431 30 hour >20 hour >10 hour 43.33 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01546 GRFKRFRKPFKKLFKKIS 18 BMAP-18P9 Synthetic construct(derived from BMAP-27) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=3.20 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=18.9 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01546 DRAVPe01546.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2311.89 C112H183N33O20 ACDEHMNQTVWY K 12.32 9 0 9 2 6 -112.22 -5876 30 hour >20 hour >10 hour 43.33 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01547 GRFKRXRKKXKKLFKKIS 18 BMAP-18X6X10 Synthetic construct(derived from BMAP-27) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.68 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=10.2 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01547 DRAVPe01547.cif Linear Free Free The 'X' at position 6 and 10 are phenylglycine L Not found No machanism information found in the reference(s) presented in this entry 2271.26 C95H166N32O16 ACDEHMNPQTVWY K 12.32 10 0 10 2 4 -156.11 -7027 30 hour >20 hour >10 hour 43.33 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01548 GRFKRIRKKLKKLFKKIS 18 BMAP-18I6L10 Synthetic construct(derived from BMAP-27) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>44.0 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50=2.79 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01548 DRAVPe01548.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2274.92 C107H192N34O20 ACDEHMNPQTVWY K 12.32 10 0 10 2 6 -110 -6043 30 hour >20 hour >10 hour 86.67 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01549 GRFKRFRKKFKKLFK 15 BMAP-15 Synthetic construct(derived from BMAP-27) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>49.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry [Ref.18591279]CEM-SS cells:TC50>49.6 μM.(TC50:the concentration that reduced cell viability by 50%) DRAVPe01549 DRAVPe01549.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 2014.54 C98H160N30O16 ACDEHIMNPQSTVWY K 12.32 9 0 9 1 5 -148.67 -6028 30 hour >20 hour >10 hour 26 0 0 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  "Wang G, Watson KM, Buckheit RW Jr. " Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. 10.1128/AAC.00452-08 Anti-HIV DRAVPe01550 GGLRSLGRKILRAWKKYGPIIVPIIRIG 28 "BMAP-28 (BMAP28, bovine myeloid antimicrobial peptide 28; natural AMPs; cathelicidin-5, cattle, ruminant, mammals, animals; BBMm;ZZP; UCLL1; Derivatives: mBMAP-28" Cow Bos taurus P54229 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2NDC "HSV,PRCV" "Herpesviridae, Coronaviridae" [Ref.15019203]Herpes simplex virus type 1(HSV-1):72% protection from HSV-1 and 72% inhibited of viral replication in Vero cells at 5 μM;##porcine respiratory corona virus(PRCV):did not prove active against PRCV at 0.5–50 μM in Swine Testicular (ST) cells. No hemolysis information or data found in the reference(s) presented in this entry [Ref.15019203]17% cytotoxic against Vero76 cells at 5 μM;95% cytotoxic against Vero76 cells at 50 μM. DRAVPe01550 DRAVPe01550.cif Linear Free Amidation None L Not found No machanism information found in the reference(s) presented in this entry 3131.89 C147H252N44O31 CDEFHMNQT I 12.02 7 0 7 7 12 23.21 -2271 30 hour >20 hour >10 hour 139.29 6990 258.89 15019203 Peptides. 2003 Nov;24(11):1723-31. "Benincasa M, Skerlavaj B, Gennaro R, Pellegrini A, Zanetti M. " In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs. 10.1016/j.peptides.2003.07.025 "Anti-HSV,Anti-PRCV" DRAVPe01551 FFPVIGRILNGIL 13 Temporin G "European common frog, Rana temporaria" P79875 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "influenza virus,Sendai virus" "Orthomyxoviridae, Paramyxoviridae" [Ref.33538061]influenza virus:inhibition of replication in A549 cells(IC50=13 μM);##Sendai virus:inhibit the replication of Sendai virus in A549 cells. No hemolysis information or data found in the reference(s) presented in this entry [Ref.33538061]A549 cells:CC50=73 μM; DRAVPe01551 DRAVPe01551.cif Linear Free Amidation None L Not found "Temporin G block the conformational rearrangements of HA2 subunit, which are essential for the viral envelope fusion with intracellular endocytic vesicles, thereby neutralizing the virus entry into the host cell. " 1458.81 C72H115N17O15 ACDEHKMQSTWY I 9.75 1 0 1 3 8 157.69 1492 1.1 hour 3 min 2 min 172.31 0 0 33538061 FASEB J. 2021 Feb;35(2):e21358.  "De Angelis M, Casciaro B, Genovese A, Brancaccio D, Marcocci ME, Novellino E, Carotenuto A, Palamara AT, Mangoni ML, Nencioni L. " "Temporin G, an amphibian antimicrobial peptide against influenza and parainfluenza respiratory viruses: Insights into biological activity and mechanism of action. " 10.1096/fj.202001885RR "Anti-Influenza virus,Anti-Sendai virus" DRAVPe01552 MKTFSVAVAVAIVLAFICTQESSALPVTGVEELVELVSSDDPVADHQELPVELGERLFNIRKKRASPKCTPYCYPTRDGVFCGVRCDF 88 EC-hepcidin1 Epinephelus coioides No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None SGIV Iridoviridae [Ref.21145974]Singapore grouper iridovirus (SGIV):strongly inhibit the replication of SGIV.(EC-hepcidin1 is more active than EC-hepcidin2) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01552 DRAVPe01552.cif Cyclic Free Free There are two pairs of disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 9665.17 C429H682N112O129S6 W V 4.99 10 12 -2 23 34 17.73 -10622 30 hour >20 hour >10 hour 91.82 3230 37.13 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-68.  "Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW." "Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides. " 10.1016/j.fsi.2010.11.021 Anti-SGIV DRAVPe01553 MKTFSVAVAVAVVLAFICTQESSALPVTGIEELVEPVSSDNNDNHQGLPVELRERLVNIRKKRAPTDCIPYCYPTGDGFHCGVTCRF 87 EC-hepcidin2 Epinephelus coioides No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SGIV Iridoviridae [Ref.21145974]Singapore grouper iridovirus (SGIV):strongly inhibit the replication of SGIV.(EC-hepcidin1 is more active than EC-hepcidin2) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01553 DRAVPe01553.cif Cyclic Free Free There are two pairs of disulfide bonds. L Not found No machanism information found in the reference(s) presented in this entry 9525.93 C418H665N115O127S6 W V 5.55 10 10 0 27 31 5.06 -11678 30 hour >20 hour >10 hour 88.39 3230 37.56 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-68.  "Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW." "Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides. " 10.1016/j.fsi.2010.11.021 Anti-SGIV DRAVPe01554 ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ 34 Dermaseptin-1 Phyllomedusa sauvagei (Sauvage's leaf frog) P24302##P80277 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "CCV,FV3" "Herpesviridae, Iridoviridae" [Ref.15193922]Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(reduce viral infectivity by 50% at 3 μM);##Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(reduce viral infectivity by 50% at 12 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.11601906]No cytotoxicity against catfish ovary(CCO) cells at 0.1-11.4 μM. DRAVPe01554 DRAVPe01554.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 3455.09 C152H257N43O44S2 CEFNPRVY A 10 5 1 4 9 15 18.53 -555 4.4 hour >20 hour >10 hour 92.35 5500 166.67 15193922 Virology. 2004 Jun 1;323(2):268-75. "Chinchar VG, Bryan L, Silphadaung U, Noga E, Wade D, Rollins-Smith L." Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. 10.1016/j.virol.2004.02.029 "Anti-CCV,Anti-FV3" DRAVPe01555 ALWMTLLKKVLKAAAKAALNAVLVGANA 28 "Dermaseptin-4 (DS IV; Dermaseptin-S4, DS4; Frogs, amphibians, animals)" Phyllomedusa sauvagei (Sauvage's leaf frog) P80280 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV,HIV" "Herpesviridae, Retroviridae" Chemiluminescence Reporter Gene Assay [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=2.10 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=6 μM). ##[Ref.15780876]human immunodeficiency virus type 1 (HIV-1):Inhibition of viral infection in Vero P4-CCR5 cells(IC50=2 µM). [Ref:11850249]IC50=20 μM against human erythrocytes [Ref.23161023]Vero cells:CC50=7.50 μM.##[Ref.15780876]P4-CCR5 cells:CC50=4.5 μM. DRAVPe01555 DRAVPe01555.cif Linear Free Free None L viral membrane "exerts a selective activity on viral particles and disturbs their organization by breaking the viral membrane, leading to the exposure of HIV-1 core and its dissociation. " 2850.55 C132H229N35O32S CDEFHIPQRSY A 10.48 4 0 4 4 19 103.21 2550 4.4 hour >20 hour >10 hour 146.79 5500 203.7 11850249##23161023##15780876 Antimicrob Agents Chemother. 2002 Mar;46(3):689-694.##J Med Virol. 2013 Feb;85(2):272-81.##Virology. 2005 Apr 10;334(2):264-75. "Navon-Venezia S, Feder R, Gaidukov L, Carmeli Y, Mor A.##Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. ##Lorin C, Saidi H, Belaid A, Zairi A, Baleux F, Hocini H, Bélec L, Hani K, Tangy F." Antibacterial properties of dermaseptin S4 derivatives with in vivo activity.## In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2.##The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro. 10.1128/AAC.46.3.689-694.2002##10.1002/jmv.23450##10.1016/j.virol.2005.02.002 "Anti-HSV,Anti-HIV" DRAVPe01556 GFCRCLCRRGVCRCICTR 18 RTD-1(Rhesus theta-defensin 1) Macaca mulatta (Rhesus macaque) P82271##P82270##Q9TU01 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1HVZ HIV Retroviridae [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=3.63 ± 0.85 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=0.94 ± 0.59 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=3.98 ± 0.70 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=2.55 ± 1.92 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=0.94 ± 0.42 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=1.15 ± 0.59 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=2.38 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01556 DRAVPe01556.cif Cyclization (N termini to C termini) Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2105.62 C82H145N33O20S6 ADEHKMNPQSWY C 9.3 5 0 5 9 4 35 -5075 30 hour >20 hour >10 hour 59.44 375 22.06 15210812 J Immunol. 2004 Jul 1;173(1):515-20. "Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI." Activity of alpha- and theta-defensins against primary isolates of HIV-1.  10.4049/jimmunol.173.1.515 Anti-HIV DRAVPe01557 GVCRCLCRRGVCRCLCRR 18 "RTD-2 (RTD 2, rhesus theta-defensin 2)" Macaca mulatta (Rhesus macaque) P82271 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=5.20 ± 1.58 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=1.78± 0.57 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=6.74 ± 1.27 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=3.66 ± 0.69 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=3.02 ± 0.10 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=3.08 ± 1.35 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=5.16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01557 DRAVPe01557.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2112.66 C80H150N36O19S6 ADEFHIKMNPQSTWY CR 9.69 6 0 6 8 4 17.78 -6204 30 hour >20 hour >10 hour 75.56 375 22.06 15210812 J Immunol. 2004 Jul 1;173(1):515-20. "Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI." Activity of alpha- and theta-defensins against primary isolates of HIV-1.  10.4049/jimmunol.173.1.515 Anti-HIV DRAVPe01558 GFCRCICTRGFCRCICTR 18 RTD-3 (rhesus theta defensin 3) Macaca mulatta (Rhesus macaque) "P82270,Q9TU01" Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=3.26 ± 0.58 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=1.74± 0.40 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=4.31 ± 0.90 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=2.09 ± 0.60 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=2.31 ± 0.21 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=3.04 ± 0.64 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=0.89 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01558 DRAVPe01558.cif Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2098.58 C84H140N30O21S6 ADEHKLMNPQSVWY C 9.01 4 0 4 10 4 52.22 -3946 30 hour >20 hour >10 hour 43.33 375 22.06 15210812 J Immunol. 2004 Jul 1;173(1):515-20. "Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI." Activity of alpha- and theta-defensins against primary isolates of HIV-1.  10.4049/jimmunol.173.1.515 Anti-HIV DRAVPe01559 GICRCICGRGICRCICGR 18 Retrocyclin-1 (RC1) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=5.51 ± 1.13 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=4.15± 0.99 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=5.33± 0.80 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=4.57 ± 0.53 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=5.86 ± 0.95 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=7.24 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01559 DRAVPe01559.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 1942.44 C74H136N30O19S6 ADEFHKLMNPQSTVWY C 9.01 4 0 4 10 4 74.44 -2856 30 hour >20 hour >10 hour 86.67 375 22.06 15210812 J Immunol. 2004 Jul 1;173(1):515-20. "Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI." Retrocyclin: a primate peptide that protects cells from infection by T- and M-tropic strains of HIV-1 10.4049/jimmunol.173.1.515 DRAVPa0039 Anti-HIV DRAVPe01560 GICRCICGRRICRCICGR 18 Retrocyclin-2 (RC2; HTD-2) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 2LZI HIV Retroviridae [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=2.30 ± 1.41 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=1.05± 0.28 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=3.32 ± 0.76 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=1.14 ± 0.29 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=3.17 ± 1.53 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=3.06 ± 0.43 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=0.18 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01560 DRAVPe01560.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2041.58 C78H145N33O19S6 ADEFHKLMNPQSTVWY C 9.3 5 0 5 9 4 51.67 -4442 30 hour >20 hour >10 hour 86.67 375 22.06 15210812 J Immunol. 2004 Jul 1;173(1):515-20. "Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI." Activity of alpha- and theta-defensins against primary isolates of HIV-1. 10.4049/jimmunol.173.1.515 DRAVPa0166 Anti-HIV DRAVPe01561 GICRCICGKGICRCICGR 18 RC-101 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.15588337]HIV-1 92US714:inhibition of virus replication in JC53-BL cells(IC50=2.3 µg/ml);##HIV-1 93US151:inhibition of virus replication in JC53-BL cells(IC50=0.5 µg/ml);##HIV-1 92HT593:inhibition of virus replication in JC53-BL cells(IC50=0.8 µg/ml);##HIV-1 92US727:inhibition of virus replication in JC53-BL cells(IC50=1.7 µg/ml);##HIV-1 5148-1382:inhibition of virus replication in JC53-BL cells(IC50=4.1 µg/ml);##HIV-1 5157-1326:inhibition of virus replication in JC53-BL cells(IC50=3.6 µg/ml);##HIV-1 5157-35097:inhibition of virus replication in JC53-BL cells(IC50=4.0 µg/ml);##HIV-1 193317:inhibition of virus replication in JC53-BL cells(IC50=2.7 µg/ml);##HIV-1 196554:inhibition of virus replication in JC53-BL cells(IC50=0.5 µg/ml);##HIV-1 196531:inhibition of virus replication in JC53-BL cells(IC50=2.7 µg/ml);##HIV-1 92UG037:inhibition of virus replication in JC53-BL cells(IC50=0.9 µg/ml);##HIV-1 192431:inhibition of virus replication in JC53-BL cells(IC50=0.5 µg/ml);##HIV-1 193358:inhibition of virus replication in JC53-BL cells(IC50=2.8 µg/ml);##HIV-1 98CN009:inhibition of virus replication in JC53-BL cells(IC50=8.5 µg/ml);##HIV-1 98TZ017:inhibition of virus replication in JC53-BL cells(IC50=4.9 µg/ml);##HIV-1 93UG053:inhibition of virus replication in JC53-BL cells(IC50=1.5 µg/ml);##HIV-1 92UG005:inhibition of virus replication in JC53-BL cells(IC50=1.0 µg/ml);##HIV-1 HM14:inhibition of virus replication in JC53-BL cells(IC50=0.8 µg/ml);##HIV-1 93TH060:inhibition of virus replication in JC53-BL cells(IC50=2.2 µg/ml);##HIV-1 HM16:inhibition of virus replication in JC53-BL cells(IC50=0.6µg/ml);##HIV-1 92BR023:inhibition of virus replication in JC53-BL cells(IC50=3.0 µg/ml);##HIV-1 92RW009:inhibition of virus replication in JC53-BL cells(IC50=2.7 µg/ml);##HIV-1 92RW024:inhibition of virus replication in JC53-BL cells(IC50=2.9 µg/ml);##HIV-1 93UG059:inhibition of virus replication in JC53-BL cells(IC50=). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01561 DRAVPe01561.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 1914.43 C74H136N28O19S6 ADEFHLMNPQSTVWY C 8.98 4 0 4 10 4 77.78 -1919 30 hour >20 hour >10 hour 86.67 375 22.06 15588337 AIDS Res Hum Retroviruses. 2004 Nov;20(11):1157-65. "Owen SM, Rudolph DL, Wang W, Cole AM, Waring AJ, Lal RB, Lehrer RI. " "RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates." 10.1089/aid.2004.20.1157 DRAVPa0040 Anti-HIV DRAVPe01562 GICRCICGRYICRCICGR 18 RC-115 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.15588337]HIV-1 92US714:inhibition of virus replication in JC53-BL cells(IC50>10 µg/ml);##HIV-1 93US151:inhibition of virus replication in JC53-BL cells(IC50=2.1 µg/ml);##HIV-1 92HT593:inhibition of virus replication in JC53-BL cells(IC50=4.2 µg/ml);##HIV-1 92US727:inhibition of virus replication in JC53-BL cells(IC50=5.4 µg/ml);##HIV-1 5148-1382:inhibition of virus replication in JC53-BL cells(IC50=4.1 µg/ml);##HIV-1 5157-1326:inhibition of virus replication in JC53-BL cells(IC50=4.2 µg/ml);##HIV-1 5157-35097:inhibition of virus replication in JC53-BL cells(IC50=4.53 µg/ml);##HIV-1 193317:inhibition of virus replication in JC53-BL cells(IC50=7.1 µg/ml);##HIV-1 196554:inhibition of virus replication in JC53-BL cells(IC50=4.5 µg/ml);##HIV-1 196531:inhibition of virus replication in JC53-BL cells(IC50=2.7 µg/ml);##HIV-1 92UG037:inhibition of virus replication in JC53-BL cells(IC50=1.9 µg/ml);##HIV-1 192431:inhibition of virus replication in JC53-BL cells(IC50=5.4 µg/ml);##HIV-1 193358:inhibition of virus replication in JC53-BL cells(IC50=>10 µg/ml);##HIV-1 98CN009:inhibition of virus replication in JC53-BL cells(IC50>10 µg/ml);##HIV-1 98TZ017:inhibition of virus replication in JC53-BL cells(IC50=7.1 µg/ml);##HIV-1 93UG053:inhibition of virus replication in JC53-BL cells(IC50=3.9 µg/ml);##HIV-1 92UG005:inhibition of virus replication in JC53-BL cells(IC50=4.1 µg/ml);##HIV-1 94UG114:inhibition of virus replication in JC53-BL cells(IC50=3.5 µg/ml);##HIV-1 HM14:inhibition of virus replication in JC53-BL cells(IC50=3.4 µg/ml);##HIV-1 93TH060:inhibition of virus replication in JC53-BL cells(IC50=5.0 µg/ml);##HIV-1 HM16:inhibition of virus replication in JC53-BL cells(IC50=3.3µg/ml);##HIV-1 RU132:inhibition of virus replication in JC53-BL cells(IC50=3.0µg/ml);##HIV-1 RU570:inhibition of virus replication in JC53-BL cells(IC50= 5.8µg/ml);##HIV-1 92BR023:inhibition of virus replication in JC53-BL cells(IC50=2.4 µg/ml);##HIV-1 92RW009:inhibition of virus replication in JC53-BL cells(IC50=4.7 µg/ml);##HIV-1 92RW024:inhibition of virus replication in JC53-BL cells(IC50=4.5 µg/ml);##HIV-1 93UG059:inhibition of virus replication in JC53-BL cells(IC50=4.6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01562 DRAVPe01562.cif Cyclic Free Free "Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2048.57 C81H142N30O20S6 ADEFHKLMNPQSTVW C 8.98 4 0 4 10 4 69.44 -2964 30 hour >20 hour >10 hour 86.67 1865 109.71 15588337 AIDS Res Hum Retroviruses. 2004 Nov;20(11):1157-65. "Owen SM, Rudolph DL, Wang W, Cole AM, Waring AJ, Lal RB, Lehrer RI. " "RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates." 10.1089/aid.2004.20.1157 DRAVPa0164 Anti-HIV DRAVPe01563 RYICRCICGRGICRCICG 18 RC-116 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae [Ref.15588337]HIV-1 92US714:inhibition of virus replication in JC53-BL cells(IC50=9.5 µg/ml);##HIV-1 93US151:inhibition of virus replication in JC53-BL cells(IC50=1.3 µg/ml);##HIV-1 92HT593:inhibition of virus replication in JC53-BL cells(IC50=3.7 µg/ml);##HIV-1 92US727:inhibition of virus replication in JC53-BL cells(IC50=4.6µg/ml);##HIV-1 5148-1382:inhibition of virus replication in JC53-BL cells(IC50=5.2 µg/ml);##HIV-1 5157-1326:inhibition of virus replication in JC53-BL cells(IC50=4.8 µg/ml);##HIV-1 5157-35097:inhibition of virus replication in JC53-BL cells(IC50=5.2 µg/ml);##HIV-1 193317:inhibition of virus replication in JC53-BL cells(IC50=7.1 µg/ml);##HIV-1 196554:inhibition of virus replication in JC53-BL cells(IC50=2.4 µg/ml);##HIV-1 196531:inhibition of virus replication in JC53-BL cells(IC50=7.8 µg/ml);##HIV-1 92UG037:inhibition of virus replication in JC53-BL cells(IC50=3.1 µg/ml);##HIV-1 192431:inhibition of virus replication in JC53-BL cells(IC50=2.4 µg/ml);##HIV-1 193358:inhibition of virus replication in JC53-BL cells(IC50=7.8 µg/ml);##HIV-1 98CN009:inhibition of virus replication in JC53-BL cells(IC50>10 µg/ml);##HIV-1 98TZ017:inhibition of virus replication in JC53-BL cells(IC50>10 µg/ml);##HIV-1 93UG053:inhibition of virus replication in JC53-BL cells(IC50=6.6 µg/ml);##HIV-1 92UG005:inhibition of virus replication in JC53-BL cells(IC50=5.2 µg/ml);##HIV-1 94UG114:inhibition of virus replication in JC53-BL cells(IC50=4.2 µg/ml);##HIV-1 HM14:inhibition of virus replication in JC53-BL cells(IC50=3.3 µg/ml);##HIV-1 93TH060:inhibition of virus replication in JC53-BL cells(IC50=6.5 µg/ml);##HIV-1 HM16:inhibition of virus replication in JC53-BL cells(IC50=2.9 µg/ml);##HIV-1 RU132:inhibition of virus replication in JC53-BL cells(IC50=4.9 µg/ml);##HIV-1 RU570:inhibition of virus replication in JC53-BL cells(IC50=9.6 µg/ml);##HIV-1 92BR023:inhibition of virus replication in JC53-BL cells(IC50=2.9 µg/ml);##HIV-1 92RW009:inhibition of virus replication in JC53-BL cells(IC50=7.8 µg/ml);##HIV-1 92RW024:inhibition of virus replication in JC53-BL cells(IC50=6.6 µg/ml);##HIV-1 93UG059:inhibition of virus replication in JC53-BL cells(IC50=5.7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented DRAVPe01563 DRAVPe01563.cif Cyclic Free Free "Disulfide bonds between Cys4 and Cys17,Cys6 and Cys15,Cys8 and Cys13." L "gp120,CD4" "The peptide binds to gp120 and CD4, thereby inhibiting HIV entry." 2048.57 C81H142N30O20S6 ADEFHKLMNPQSTVW C 8.98 4 0 4 10 4 69.44 -2964 1 hour 2 min 2 min 86.67 1865 109.71 15588337 AIDS Res Hum Retroviruses. 2004 Nov;20(11):1157-65. "Owen SM, Rudolph DL, Wang W, Cole AM, Waring AJ, Lal RB, Lehrer RI. " "RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates." 10.1089/aid.2004.20.1157 DRAVPa0165 Anti-HIV DRAVPe01564 RPRLSHKGPMPF 12 Apelin-12 Synthetic construct Q9TUI9##K7GLR4 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=63.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01564 DRAVPe01564.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1422.71 C64H103N21O14S ACDEINQTVWY P 12.01 4 0 4 2 2 -113.33 -3226 1 hour 2 min 2 min 32.5 0 0 10802050 FEBS Lett. 2000 May 4;473(1):15-8. "Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H." Apelin peptides block the entry of human immunodeficiency virus (HIV). 10.1016/s0014-5793(00)01487-3 Anti-HIV DRAVPe01565 QRPRLSHKGPMPF 13 Apelin-13 Bos taurus (Bovine) Q9TUI9##A0A484GMR2##A0A5N3XG03##A0A2Y9M6A9##A0A5G2R3Z5##A0A2Y9SZ03##A0A2U4A1K6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=26.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01565 DRAVPe01565.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1550.84 C69H111N23O16S ACDEINTVWY P 12.01 4 0 4 2 2 -131.54 -3780 0.8 hour 10 min >10 hour 30 0 0 10802050 FEBS Lett. 2000 May 4;473(1):15-8. "Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H." Apelin peptides block the entry of human immunodeficiency virus (HIV). 10.1016/s0014-5793(00)01487-3 Anti-HIV DRAVPe01566 KFRRQRPRLSHKGPMPF 17 Apelin-17 Synthetic construct Q9TUI9##K7GLR4 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=4.8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01566 DRAVPe01566.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 2138.57 C96H156N34O20S ACDEINTVWY R 12.48 7 0 7 2 3 -160 -7021 1.3 hour 3 min 2 min 22.94 0 0 10802050 FEBS Lett. 2000 May 4;473(1):15-8. "Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H." Apelin peptides block the entry of human immunodeficiency virus (HIV). 10.1016/s0014-5793(00)01487-3 Anti-HIV DRAVPe01567 LVQPRGPRSGPGPWQGGRRKFRRQRPRLSHKGPMPF 36 Apelin-36 Bos taurus (Bovine) Q9TUI9##A0A484GMR2##A0A5N3XG03##A0A2Y9M6A9##A0A5G2R3Z5##A0A2Y9SZ03##A0A2U4A1K6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=0.3 μg/ml).##[Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01567 DRAVPe01567.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 4178.89 C185H298N68O42S ACDEINTY R 12.85 11 0 11 8 6 -150.83 -12838 5.5 hour 3 min 2 min 29.72 5500 157.14 10802050##11090199 FEBS Lett. 2000 May 4;473(1):15-8.##J Virol. 2000 Dec;74(24):11972-6. "Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H.##Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin peptides block the entry of human immunodeficiency virus (HIV).##Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1016/s0014-5793(00)01487-3##10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01568 RRQRPRLSHKGPMPF 15 Apelin-15 Synthetic construct Q9TUI9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=12μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01568 DRAVPe01568.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1863.22 C81H135N31O18S ACDEINTVWY R 12.48 6 0 6 2 2 -174 -6764 1 hour 2 min 2 min 26 0 0 11090199 J Virol. 2000 Dec;74(24):11972-6. "Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01569 RRKFRRQRPRLSHKGPMPF 19 Apelin-19 Synthetic construct Q9TUI9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01569 DRAVPe01569.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 2450.95 C108H180N42O22S ACDEINTVWY R 12.7 9 0 9 2 3 -190.53 -10005 1 hour 2 min 2 min 20.53 0 0 11090199 J Virol. 2000 Dec;74(24):11972-6. "Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01570 RRQRPRLSHKGPM 13 Apelin-15-(63-75)-peptide Synthetic construct Q9TUI9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01570 DRAVPe01570.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1618.93 C67H119N29O16S ACDEFINTVWY R 12.48 6 0 6 2 1 -210 -7062 1 hour 2 min 2 min 30 0 0 11090199 J Virol. 2000 Dec;74(24):11972-6. "Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01571 RRQRPRLSHKGPX 13 [Met(O)75]apelin-15-(63-75)-peptide Synthetic construct Q9TUI9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=45 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free The 'X' at position 13 indicates oxidized methionine. L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1599.06 C62H108N28O14 ACDEFIMNTVWY R 12.48 6 0 6 2 1 -224.62 -7297 1 hour 2 min 2 min 30 0 0 11090199 J Virol. 2000 Dec;74(24):11972-6. "Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01572 RRQRPRLSHKGP 12 Apelin-15-(63-74)-peptide Synthetic construct Q9TUI9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Reverse transcriptase assay [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=37 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01572 DRAVPe01572.cif Linear Free Free None L APJ receptor "APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection." 1487.73 C62H110N28O15 ACDEFIMNTVWY R 12.48 6 0 6 2 1 -243.33 -7297 1 hour 2 min 2 min 32.5 0 0 11090199 J Virol. 2000 Dec;74(24):11972-6. "Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J." "Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. " 10.1128/jvi.74.24.11972-11976.2000 Anti-HIV DRAVPe01573 GRKKRRQRRR 10 TAT(48-57) Synthetic construct P04610 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae infection inhibition assay [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.094 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22319541]No cytotoxicity against P4-R5 MAGI cells up to 100 μM. DRAVPe01573 DRAVPe01573.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1396.67 C55H109N31O12 ACDEFHILMNPSTVWY R 12.7 8 0 8 1 0 -387 -10522 30 hour >20 hour >10 hour 0 0 0 22319541 Int J Pept. 2012;2012:349427. "Keogan S, Passic S, Krebs FC." Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. 10.1155/2012/349427 DRAVPa1019 Anti-HIV DRAVPe01574 RRKKRRQRRR 10 TAT(48-57)[G1R] Synthetic construct P04610 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae infection inhibition assay [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.065 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01574 DRAVPe01574.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1495.81 C59H118N34O12 ACDEFGHILMNPSTVWY R 12.78 9 0 9 0 0 -428 -12108 1 hour 2 min 2 min 0 0 0 22319541 Int J Pept. 2012;2012:349427. "Keogan S, Passic S, Krebs FC." Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. 10.1155/2012/349427 Anti-HIV DRAVPe01575 GRKKRRRRRR 10 TAT(48-57)[Q7R] Synthetic construct P04610 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae infection inhibition assay [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.071 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01575 DRAVPe01575.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1424.73 C56H113N33O11 ACDEFHILMNPQSTVWY R 12.78 9 0 9 1 0 -397 -11460 30 hour >20 hour >10 hour 0 0 0 22319541 Int J Pept. 2012;2012:349427. "Keogan S, Passic S, Krebs FC." Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. 10.1155/2012/349427 Anti-HIV DRAVPe01576 RRKKRRRRRR 10 "TAT(48-57)[G1R,Q7R]" Synthetic construct P04610 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae infection inhibition assay [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.025 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01576 DRAVPe01576.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1523.86 C60H122N36O11 ACDEFGHILMNPQSTVWY R 12.85 10 0 10 0 0 -438 -13046 1 hour 2 min 2 min 0 0 0 22319541 Int J Pept. 2012;2012:349427. "Keogan S, Passic S, Krebs FC." Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. 10.1155/2012/349427 Anti-HIV DRAVPe01577 RRRRRRRRRR 10 R-10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae infection inhibition assay [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.014 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01577 DRAVPe01577.cif Linear Free Free None L Not found No machanism information found in the reference(s) presented in this entry 1579.89 C60H122N40O11 ACDEFGHIKLMNPQSTVWY R 12.95 10 0 10 0 0 -450 -14920 1 hour 2 min 2 min 0 0 0 22319541 Int J Pept. 2012;2012:349427. "Keogan S, Passic S, Krebs FC." Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. 10.1155/2012/349427 Anti-HIV DRAVPe01578 KGEAMHGQVDCSPGIWQLDC 20 #4330 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1:inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(IC50=4 μM);inhibition of reverse transcriptase(DNA-dependent DNA polymerase) activity(IC50=6.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01578 DRAVPe01578.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 2174.45 C91H140N26O30S3 FNRTY G 4.54 2 3 -1 6 5 -39.5 -2319 1.3 hour 3 min 2 min 58.5 5625 296.05 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01579 ASCDKCQLKGEAMHG 15 #5649 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(91.5 ± 2.5% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01579 DRAVPe01579.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1577.81 C62H104N20O22S3 FINPRTVWY ACGK 6.77 3 2 1 5 3 -58.67 -2490 4.4 hour >20 hour >10 hour 39.33 125 8.93 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01580 KCQLKGEAMHGQVDC 15 #5650 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(63± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01580 DRAVPe01580.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1646.91 C66H111N21O22S3 FINPRSTWY CGKQ 6.73 3 2 1 4 3 -60.67 -2481 1.3 hour 3 min 2 min 52 125 8.93 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01581 KGEAMHGQVDCSPGI 15 #5651 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(99 ± 6% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01581 DRAVPe01581.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1528.72 C62H101N19O22S2 FLNRTWY G 5.32 2 2 0 5 3 -42 -1746 1.3 hour 3 min 2 min 52 0 0 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01582 MHGQVDCSPGIWQLD 15 #5652 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(79 ± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01582 DRAVPe01582.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1685.89 C72H108N20O23S2 AEFKNRTY DGQ 4.2 1 2 -1 4 4 -29.33 -1486 30 hour >20 hour >10 hour 71.33 5500 392.86 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01583 VDCSPGIWQLDCTHL 15 #5653 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(58 ± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01583 DRAVPe01583.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1686.92 C73H111N19O23S2 AEFKMNRY CDL 4.2 1 2 -1 5 5 21.33 -898 100 hour >20 hour >10 hour 97.33 5625 401.79 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01584 PGIWQLDCTHLEGKI 15 #5654 derived from HIV-1 integrase Synthetic construct P04587 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae Assay for the enzymatic activities of RT [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(62.5 ± 0.5% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01584 DRAVPe01584.cif Linear Free Free None L Reverse Transcriptase The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. 1709.98 C77H120N20O22S AFMNRSVY GIL 5.33 2 2 0 4 5 -16.67 -868 >20 hour >20 hour ? 104 5500 392.86 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. "Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A." Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. 10.1016/j.abb.2006.12.007 Anti-HIV DRAVPe01585 SWLRDLWDWICEVLSDFK 18 NS5A-derived peptide C5A [I6L] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.13 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=13.84 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01585 DRAVPe01585.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2311.64 C109H155N25O29S AGHMNPQTY DLW 4.23 2 4 -2 3 9 -7.22 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01586 SWLRDIWDWLCEVLSDFK 18 NS5A-derived peptide C5A [I10L] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.09 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=1.84±0.16 μM). [Ref.21801309]Human erythrocytes:MHC=6.92 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01586 DRAVPe01586.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2311.64 C109H155N25O29S AGHMNPQTY DLW 4.23 2 4 -2 3 9 -7.22 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01587 SWLRDIWDWICELLSDFK 18 NS5A-derived peptide C5A [V13L] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.11 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.76±0.19 μM). [Ref.21801309]Human erythrocytes:MHC=3.44 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01587 DRAVPe01587.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2325.67 C110H157N25O29S AGHMNPQTVY DLW 4.23 2 4 -2 3 9 -5.56 -2439 1.9 hour >20 hour >10 hour 108.33 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01588 SWLRDLWDWLCEVLSDFK 18 "NS5A-derived peptide C5A [I6L,I10L]" Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.15 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=6.92 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01588 DRAVPe01588.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2311.64 C109H155N25O29S AGHIMNPQTY L 4.23 2 4 -2 3 9 -11.11 -2527 1.9 hour >20 hour >10 hour 102.78 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01589 SWLRDLWDWICELLSDFK 18 "NS5A-derived peptide C5A [I6L,V13L]" Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=0.78±0.07 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=3.31±0.31 μM). [Ref.21801309]Human erythrocytes:MHC=53.75 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01589 DRAVPe01589.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2325.67 C110H157N25O29S AGHMNPQTVY L 4.23 2 4 -2 3 9 -9.44 -2439 1.9 hour >20 hour >10 hour 108.33 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01590 SWLRDIWDWLCELLSDFK 18 "NS5A-derived peptide C5A [I10L,V13L]" Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=0.82±0.10 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.58±0.22 μM). [Ref.21801309]Human erythrocytes:MHC=3.44 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01590 DRAVPe01590.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2325.67 C110H157N25O29S AGHMNPQTVY L 4.23 2 4 -2 3 9 -9.44 -2439 1.9 hour >20 hour >10 hour 108.33 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01591 SWLRDLWDWLCELLSDFK 18 "NS5A-derived peptide C5A [I6L,I10L,V13L]" Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.14 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=0.59±0.03 μM). [Ref.21801309]Human erythrocytes:MHC=107.50 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01591 DRAVPe01591.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2325.67 C110H157N25O29S AGHIMNPQTVY L 4.23 2 4 -2 3 9 -13.33 -2439 1.9 hour >20 hour >10 hour 108.33 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01592 SWLRDIWDWVCEVLSDFK 18 NS5A-derived peptide C5A [I10V] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.117 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=1.86±0.25 μM). [Ref.21801309]Human erythrocytes:MHC=13.93 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01592 DRAVPe01592.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2297.61 C108H153N25O29S AGHMNPQTY DW 4.23 2 4 -2 3 9 -5 -2615 1.9 hour >20 hour >10 hour 97.22 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01593 SWLRDIWDWACEVLSDFK 18 NS5A-derived peptide C5A [I10A] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=4.00±0.36 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.21±0.28 μM). [Ref.21801309]Human erythrocytes:MHC=14.10 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01593 DRAVPe01593.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2269.56 C106H149N25O29S GHMNPQTY DW 4.23 2 4 -2 3 9 -18.33 -2838 1.9 hour >20 hour >10 hour 86.67 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01594 SWLRDIWDWGCEVLSDFK 18 NS5A-derived peptide C5A [I10G] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=3.50±0.36 μM). [Ref.21801309]Human erythrocytes:MHC=28.38 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01594 DRAVPe01594.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2255.53 C105H147N25O29S AHMNPQTY DW 4.23 2 4 -2 4 8 -30.56 -2925 1.9 hour >20 hour >10 hour 81.11 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01595 SWLRDIWDWSCEVLSDFK 18 NS5A-derived peptide C5A [I10S] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=28.00 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01595 DRAVPe01595.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2285.56 C106H149N25O30S AGHMNPQTY DSW 4.23 2 4 -2 4 8 -32.78 -3359 1.9 hour >20 hour >10 hour 81.11 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01596 SWLRDIWDWECEVLSDFK 18 NS5A-derived peptide C5A [I10E] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=214.91 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01596 DRAVPe01596.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2327.6 C108H151N25O31S AGHMNPQTY DW 4.1 2 5 -3 3 8 -47.78 -3700 1.9 hour >20 hour >10 hour 81.11 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01597 SWLRDIWDWKCEVLSDFK 18 NS5A-derived peptide C5A [I10K] Synthetic construct V5RF15 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCV,HIV" "Flaviviridae, Retroviridae" "Pseudotyped HIV (HIVpp) and antiviral assay,HCV production and infection assay" [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=214.81 μM. No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01597 DRAVPe01597.cif Linear Free Free None L membrane "The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes." 2326.65 C109H156N26O29S AGHMNPQTY DW 4.68 3 4 -1 3 8 -50 -3574 1.9 hour >20 hour >10 hour 81.11 16500 970.59 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. "Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX." Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. 10.1111/j.1747-0285.2011.01201.x "Anti-HCV,Anti-HIV" DRAVPe01598 TRQARRNRRRRWRERQR 17 Rev (34-50) Synthetic construct P05866 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ULL HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=1.7±0.25 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01598 DRAVPe01598.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  2437.77 C97H173N51O24 CDFGHIKLMPSVY R 12.6 10 1 9 2 2 -345.88 -17216 7.2 hour >20 hour >10 hour 5.88 5500 343.75 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01599 TRQARRNRRRRWRERQRAAAAC 22 Rev (34-50) -A4C Synthetic construct P05866 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=0.35±0.07 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01599 DRAVPe01599.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  2825.22 C112H198N56O29S DFGHIKLMPSVY R 12.37 10 1 9 3 6 -223.18 -16364 7.2 hour >20 hour >10 hour 22.73 5500 261.9 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01600 TRQARRNRRRRWRERQRAAAACYGRKKRRQRRR 33 Rev (34-50) -A4C-RTD Synthetic construct P05866##P04612 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=0.37±0.09 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01600 DRAVPe01600.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  4367.05 C176H314N88O42S DFHILMPSV R 12.48 18 1 17 5 6 -270 -26900 7.2 hour >20 hour >10 hour 15.15 6990 218.44 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01601 MPKTRRRPRRSQRKRPPTPWP 21 Rex (1-21) Synthetic construct P0C207 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01601 DRAVPe01601.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  2685.2 C116H198N46O26S ACDEFGHILNVY R 12.78 9 0 9 3 1 -255.24 -12494 30 hour >20 hour >10 hour 0 5500 275 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01602 MPKTRRRPRRSQRKRPPTPWPYGRKKRRQRRR 32 Rex (1-21) -RTD Synthetic construct P0C207##P04612 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=2.5±0.76 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01602 DRAVPe01602.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  4227.03 C180H314N78O39S ACDEFHILNV R 12.74 17 0 17 5 1 -292.5 -23030 30 hour >20 hour >10 hour 0 6990 225.48 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01603 RPRGRRGSRPSGAERRRRRAAAA 23 RSG-P2G4 Synthetic construct None Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae MAGI assay [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=2.2±0.51 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01603 DRAVPe01603.cif Linear Free Free None L Not found Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  2603.95 C102H187N53O28 CDFHIKLMNQTVWY R 12.6 10 1 9 5 5 -197.83 -15094 1 hour 2 min 2 min 21.74 0 0 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. "Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M." "Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4." 10.1016/j.biocel.2010.05.005 Anti-HIV DRAVPe01604 RSQKEGLHYTCSSHFPYSQYQFWK 24 CCR5 ECL2 (168-191) Synthetic construct P51681 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV neutralization assay [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=136 ± 49 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=138± 36 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=89±31 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=103±37 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01604 DRAVPe01604.cif Linear Free Free None L gp120 The peptide binds gp120 and inhibits virus entry. 3008.32 C138H191N37O38S ADIMNV S 9.05 5 1 4 10 4 -131.25 -5993 1 hour 2 min 2 min 16.25 9970 433.48 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. "Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA." Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. 10.1074/jbc.M111.332361 Anti-HIV DRAVPe01605 CSSHFPYSQYQFWK 14 CCR5 ECL2 (178-191) Synthetic construct P51681 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV neutralization assay [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=28 ±7 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=65± 3 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=54±2 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=53±2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01605 DRAVPe01605.cif Linear Free Free None L gp120 The peptide binds gp120 and inhibits virus entry. 1808 C86H110N20O22S ADEGILMNRTV S 8.18 2 0 2 6 3 -96.43 -2220 1.2 hour >20 hour >10 hour 0 8480 652.31 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. "Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA." Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. 10.1074/jbc.M111.332361 Anti-HIV DRAVPe01606 QKEGLHYTCSSHFPYSQYQF 20 CCR5 ECL2 (170-189) Synthetic construct P51681 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV neutralization assay [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=237 ± 31 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=612± 21 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=374±28 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=600±24 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01606 DRAVPe01606.cif Linear Free Free None L gp120 The peptide binds gp120 and inhibits virus entry. 2450.67 C112H152N28O33S ADIMNRVW QSY 6.91 3 1 2 9 3 -107 -3839 0.8 hour 10 min >10 hour 19.5 4470 235.26 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. "Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA." Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. 10.1074/jbc.M111.332361 Anti-HIV DRAVPe01607 RRWYRWW 7 Octa 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01607 DRAVPe01607.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 1208.39 C60H77N19O9 ACDEFGHIKLMNPQSTV RW 11.71 3 0 3 1 3 -250 -3791 1 hour 2 min 2 min 0 17990 2998.33 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01608 RRWYRWWRRRWYRWWR 16 MU89 (Octa 1 dp) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=8.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01608 DRAVPe01608.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2711.15 C132H176N46O19 ACDEFGHIKLMNPQSTV R 12.22 8 0 8 2 6 -275 -10566 1 hour 2 min 2 min 0 35980 2398.67 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01609 RWWRWWR 7 Hepta 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01609 DRAVPe01609.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 1231.43 C62H78N20O8 ACDEFGHIKLMNPQSTVY W 12.3 3 0 3 0 4 -244.29 -3544 1 hour 2 min 2 min 0 22000 3666.67 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01610 RWWRWWRRWWRWWR 14 MU92 (Hepta 1 dp) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=3.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01610 DRAVPe01610.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2444.85 C124H154N40O15 ACDEFGHIKLMNPQSTVY W 12.7 6 0 6 0 8 -244.29 -7088 1 hour 2 min 2 min 0 44000 3384.62 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01611 YRWWRWARRW 10 Deca 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01611 DRAVPe01611.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 1621.87 C80H104N26O12 CDEFGHIKLMNPQSTV RW 12 4 0 4 1 5 -211 -4869 2.8 hour 10 min 2 min 10 23490 2610 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01612 YRWWRWARRWYRWWRWARRW 20 MU94 (Deca 1 dp) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=5 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01612 DRAVPe01612.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 3225.73 C160H206N52O23 CDEFGHIKLMNPQSTV RW 12.22 8 0 8 2 10 -211 -9738 2.8 hour 10 min 2 min 10 46980 2472.63 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01613 APKAMRLLRRLLRRLLR 17 N-[RLLR]3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=7.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01613 DRAVPe01613.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2132.74 C94H178N36O18S CDEFGHINQSTVWY LR 12.7 7 0 7 0 8 -24.71 -5958 4.4 hour >20 hour >10 hour 149.41 0 0 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01614 RLLRRLLRRLLRRLLRRLLR 20 RLLR5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50<3.3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01614 DRAVPe01614.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2711.48 C120H232N50O21 ACDEFGHIKMNPQSTVWY LR 12.95 10 0 10 0 10 -35 -10000 1 hour 2 min 2 min 195 0 0 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01615 RRRRRRRWWWRRRRRRRR 18 MU103 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01615 DRAVPe01615.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2919.47 C123H212N66O19 ACDEFGHIKLMNPQSTVY R 13.15 15 0 15 0 3 -390 -21681 1 hour 2 min 2 min 0 16500 970.59 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01616 RRRRRRRRRRRRRRRWWW 18 MU104 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=9.25 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01616 DRAVPe01616.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2919.47 C123H212N66O19 ACDEFGHIKLMNPQSTVY R 13.15 15 0 15 0 3 -390 -21681 1 hour 2 min 2 min 0 16500 970.59 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x Anti-HSV DRAVPe01617 WRKWRKRWWWRKWRKRWW 18 ApoEdpL-W Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV,HIV,VSV" "Herpesviridae, Retroviridae, Rhabdoviridae" plaque reduction assay [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=3.1 µM);##HIV-1:inhibition of virus replication(>80% inhibition at 10 µM). [Ref.17681018]15% hemolysis against human red blood cells at 35 μM. [Ref.17681018]No significant cytotoxicity against Vero cells up to 40 μM. DRAVPe01617 DRAVPe01617.cif Linear Free Free None L Not found "The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region." 2957.54 C148H202N48O19 ACDEFGHILMNPQSTVY W 12.7 10 0 10 0 8 -276.67 -9308 2.8 hour 3 min 2 min 0 44000 2588.24 17681018 FEBS J. 2007 Sep;274(17):4511-25. "Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB." Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. 10.1111/j.1742-4658.2007.05981.x "Anti-HSV,Anti-HIV,Anti-VSV" DRAVPe01618 HCKFWW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01618 DRAVPe01618.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 906.07 C46H55N11O7S ADEGILMNPQRSTVY W 8.23 2 0 2 1 3 -60 -129 3.5 hour 10 min >10 hour 0 11000 2200 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01619 HCKFWI 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01619 DRAVPe01619.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 833.02 C41H56N10O7S ADEGLMNPQRSTVY CFHIKW 8.23 2 0 2 1 3 30 130 3.5 hour 10 min >10 hour 65 5500 1100 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01620 HCKFWF 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01620 DRAVPe01620.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 867.04 C44H54N10O7S ADEGILMNPQRSTVY F 8.23 2 0 2 1 3 1.67 -64 3.5 hour 10 min >10 hour 0 5500 1100 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01621 HCKFAW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=150 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01621 DRAVPe01621.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 790.94 C38H50N10O7S DEGILMNPQRSTVY ACFHKW 8.23 2 0 2 1 3 -15 -181 3.5 hour 10 min >10 hour 16.67 5500 1100 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01622 HCKFWA 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=210 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01622 DRAVPe01622.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 790.94 C38H50N10O7S DEGILMNPQRSTVY ACFHKW 8.23 2 0 2 1 3 -15 -181 3.5 hour 10 min >10 hour 16.67 5500 1100 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01623 HCKAWW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01623 DRAVPe01623.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 829.97 C40H51N11O7S DEFGILMNPQRSTVY W 8.23 2 0 2 1 3 -76.67 -246 3.5 hour 10 min >10 hour 16.67 11000 2200 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01624 ACKFWW 6 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae integrase assay [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=51 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01624 DRAVPe01624.cif Linear Free Amidation None L integrase "The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication." 840.01 C43H53N9O7S DEGHILMNPQRSTVY W 8.27 1 0 1 1 4 23.33 518 4.4 hour >20 hour >10 hour 16.67 11000 2200 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. "Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH." Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. 10.1073/pnas.92.25.11456 Anti-HIV DRAVPe01812 GWINEKKMQQKIDEKIGKNIIGGMAKAVIHKMAKNEFQCVANVDTLGNCKKHCAKTTGEKGYCHGTKCKCGIELSY 76 Smp76 Scorpio maurus palmatu No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Plaque assay [Ref.32435168]Dengue Virus(DENV):inhibition of viral infection in Vero/SLAM cells(IC50= 0.01 μg/ml). [Ref.32435168]human red blood cells:HC50>10 μg/ml. [Ref.32435168]Huh7it-1 cells:CC50>10 μg/ml. No predicted structure available DRAVPe01812.cif Cyclic Free Free "Disulfide bonds between Cys39 and Cys63, Cys49 and Cys68, Cys53 and Cys70." L Not found No mechanism information found in the reference(s). 8402.89 C362H595N105O106S9 PR K 9.22 17 7 10 27 19 -56.84 -11300 30 hour >20 hour >10 hour 64.21 8855 118.07 32435168 Int J Pept Res Ther. 2020;26(2):811-821. "El-Bitar AMH, Sarhan M, Abdel-Rahman MA, Quintero-Hernandez V, Aoki-Utsubo C, Moustafa MA, Possani LD, Hotta H." "Smp76, a Scorpine-Like Peptide Isolated from the Venom of the Scorpion Scorpio maurus palmatus, with a Potent Antiviral Activity Against Hepatitis C Virus and Dengue Virus." 10.1007/s10989-019-09888-2 Anti-DENV DRAVPe01813 GFGCPFNQGQCHKHCQSIRRRGGYCDGFLKTRCVCYR 37 BmKDfsin4 Mesobuthus martensii No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae ELISA "[Ref.27128943]hepatitic B Virus (HBV): Pharmacological profiles of BmKDfsin4 against HBeAg, HBsAg and HBV DNA on HepG2.2.15 cells(HBeAg: IC50= 3.95 μM; HBsAg: IC50= 2.28 μM; HBV DNA: IC50= 1.26 μM)." [Ref.27128943]Human erythrocytes: 50% hemolysis concentration was 66.85 μM. [Ref.27128943]HepG2.2.15 cells: CC50= 167.82 μM;##HepG2 cells: CC50= 154.24 μM;##L-02 cells: CC50= 103.77 μM. No predicted structure available DRAVPe01813.cif Cyclic Free Free "Disulfide bonds between Cys4 and Cys25, Cys11 and Cys33, Cys15 and Cys35." L Not found "BmKDfsin4 had been shown to exhibit powerful inhibitory activity against HBV replication by reducing the production of HBeAg, HBsAg, and HBV DNAin cell culture medium and the production of intracellular HBsAg, HBV core protein, HBx protein, and HBV RT." 4282.95 C181H278N62O48S6 AEMW CG 9.38 9 1 8 17 6 -71.35 -9711 30 hour >20 hour >10 hour 28.92 3355 93.19 27128943 Toxins (Basel). 2016 Apr 27;8(5):124. "Zeng Z, Zhang Q, Hong W, Xie Y, Liu Y, Li W, Wu Y, Cao Z. " A Scorpion Defensin BmKDfsin4 Inhibits Hepatitis B Virus Replication in Vitro. 10.3390/toxins8050124 Anti-HBV DRAVPe01814 ILGKIWEGIKSIF 13 Hp1036 Heterometrus petersii P0DME6 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque forming assay [Ref.24315793]Herpes simplex virus type 1(HSV-1):inhibition of viral inactivation in Vero cells(EC50=0.43 ± 0.09 μM);inhibition of viral attachment in Vero cells(EC50=2.87 ± 0.16 μM);inhibition of viral entry in Vero cells(EC50=4.29 ± 0.35 μM);inhibition of postentry in Vero cells(EC50=7.86 ± 0.80 μM). [Ref.24315793]Human erythrocytes: HC50 = 34.91 ± 0.47 μM. [Ref.24315793]Vero cells: CC50 = 46.71 ± 3.80 μM. No predicted structure available DRAVPe01814.cif Linear Free Amidation None L Not found inhibit HSV-1 when it attaches to the cell surface and when it has already bound to the cells but not entered yet and also exhibited potent inhibitory effects against viral particles proliferation in postentry stage. 1503.85 C74H118N16O17 ACDHMNPQRTVY I 8.59 2 1 1 3 7 83.08 1048 20 hour 30 min >10 hour 150 5500 458.33 24315793 Antiviral Res. 2014 Feb;102:1-10. "Hong W, Li T, Song Y, Zhang R, Zeng Z, Han S, Zhang X, Wu Y, Li W, Cao Z." Inhibitory activity and mechanism of two scorpion venom peptides against herpes simplex virus type 1. 10.1016/j.antiviral.2013.11.013 Anti-HSV-1 DRAVPe01815 ILSYLWNGIKSIF 13 Hp1239 Heterometrus petersii P0DME8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV-1 Herpesviridae Plaque forming assay [Ref.24315793]Herpes simplex virus type 1(HSV-1):inhibition of viral inactivation in Vero cells(EC50=0.41 ± 0.06 μM);inhibition of viral attachment in Vero cells(EC50=5.73 ± 0.61 μM);inhibition of viral entry in Vero cells(EC50=4.32 ± 0.47 μM);inhibition of postentry in Vero cells(EC50=8.41 ± 0.73 μM). [Ref.24315793]Human erythrocytes: HC50 = 33.32 ± 0.96 μM. [Ref.24315793]Vero cells: CC50 = 26.15 ± 1.91 μM. No predicted structure available DRAVPe01815.cif Linear Free Amidation None L Not found inhibit HSV-1 when it attaches to the cell surface and when it has already bound to the cells but not entered yet and also exhibited potent inhibitory effects against viral particles proliferation in postentry stage. 1553.86 C77H116N16O18 ACDEHMPQRTV I 8.59 1 0 1 5 7 94.62 1172 20 hour 30 min >10 hour 150 6990 582.5 24315793 Antiviral Res. 2014 Feb;102:1-10. "Hong W, Li T, Song Y, Zhang R, Zeng Z, Han S, Zhang X, Wu Y, Li W, Cao Z." Inhibitory activity and mechanism of two scorpion venom peptides against herpes simplex virus type 1. 10.1016/j.antiviral.2013.11.013 Anti-HSV-1 DRAVPe01816 LWGEIWNTVKGLI 13 Eval418 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HSV-1 Herpesviridae Plaque reduction assay [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=2.48 µg/mL); inhibition of viral attachment in Vero cells(IC50=3.70 µg/mL); inhibition of viral entry in Vero cells(IC50=31.71 µg/mL). [Ref.29290802]The hemolysis rate of human erythrocytes was less than 50% when the concentration of Eval418 was as high as 200 μg/mL. [Ref.29290802]Vero cells: CC50 = 68.50 µg/mL. No predicted structure available DRAVPe01816.cif Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1528.81 C74H113N17O18 ACDFHMPQRSY GILW 6 1 1 0 4 7 50.77 869 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV-1 DRAVPe01817 LWGHIWNFVHGLI 13 Eval418-FH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque reduction assay [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=1.50 µg/mL); inhibition of viral attachment in Vero cells(IC50=1.43 µg/mL); inhibition of viral entry in Vero cells(IC50=8.63 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cells: CC50 = 27.60 µg/mL. No predicted structure available DRAVPe01817.cif Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1591.88 C80H110N20O15 ACDEKMPQRSTY GHILW 6.92 2 0 2 3 8 85.38 1728 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV-1 DRAVPe01818 LWHHIWNFVHGLI 13 Eval418-FH3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque reduction assay [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=1.01 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.86 µg/mL); inhibition of viral entry in Vero cells(IC50=4.23 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cells: CC50 = 26.83 µg/mL. No predicted structure available DRAVPe01818.cif Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1671.97 C84H114N22O15 ACDEKMPQRSTY H 7.02 3 0 3 2 8 63.85 1168 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV-1 DRAVPe01819 LWHHIWNTVHHLI 13 Eval418-FH4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque reduction assay [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=0.87 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.63 µg/mL); inhibition of viral entry in Vero cells(IC50=4.37 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cells: CC50 = 27.58 µg/mL. No predicted structure available DRAVPe01819.cif Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1705.99 C83H116N24O16 ACDEFGKMPQRSY H 7.1 4 0 4 2 7 15.38 53 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV-1 DRAVPe01820 LWHHIWHTVHHLI 13 Eval418-FH5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque reduction assay [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=0.86 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.67 µg/mL); inhibition of viral entry in Vero cells(IC50=2.88 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry [Ref.29290802]Vero cells: CC50 = 106.68 µg/mL. No predicted structure available DRAVPe01820.cif Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1729.02 C85H117N25O15 ACDEFGKMNPQRSY H 7.16 5 0 5 1 7 17.69 251 5.5 hour 3 min 2 min 142.31 11000 916.67 29290802 Theranostics. 2018 Jan 1;8(1):199-211. "Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z." Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. 10.7150/thno.21425 Anti-HSV-1 DRAVPe01821 LLMVNEATRFQTVSGFV 17 BPIP Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae MBP-tagged (SARS-CoV-2) assay [Ref.35896605]SARS-CoV-2: inhibition of Mpro (IC50= 0.52 nM). [Ref.35896605]BRIP is not hemolytic at 500 nM and slightly hemolytic at 50 µM. No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available DRAVPe01821.cif Linear Free Free None L Mpro "The peptide inhibits Mpro, a protein crucial for viral replication." 1912.23 C86H138N22O25S CDHIKPWY V 6 1 1 0 5 8 70 -943 5.5 hour 3 min 2 min 102.94 0 0 35896605 Sci Rep. 2022 Jul 27;12(1):12802 "Kashyap P, Bhardwaj VK, Chauhan M, Chauhan V, Kumar A, Purohit R, Kumar A, Kumar S" A ricin-based peptide BRIP from Hordeum vulgare inhibits Mpro of SARS-CoV-2 10.1038/s41598-022-15977-y Anti-SARS-CoV-2 DRAVPe01822 KFFRKKSVKK 10 BF-30 Bungarus fasciatus No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Cytopathic effect (CPE) reduction assay [Ref.30447229]Influenza A virus H1N1:inhibition of viral replication in MDCK cells(EC50=5.20±0.9 μM);##influenza A virus H3N2: inhibition of viral replication in MDCK cells(EC50=7.36 ± 1.2 μM);##influenza A virus(oseltamivir-resistant strain): inhibition of viral replication in MDCK cells(EC50=18.91 ± 7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30447229]MDCK cells:CC50=67.7μM. No predicted structure available DRAVPe01822.cif Linear Free Free None L Not found BF-30 could inhibit the replication of various influenza subtypes by fusing virion membranes and reducing infectivity. 1295.64 C62H106N18O12 ACDEGHILMNPQTWY K 11.39 6 0 6 1 3 -150 -3607 1.3 hour 3 min 2 min 29 0 0 30447229 Peptides. 2019 Feb;112:14-22. "Xu J, Chen S, Jin J, Ma L, Guo M, Zhou C, Dou J." Inhibition of peptide BF-30 on influenza A virus infection in vitro/vivo by causing virion membrane fusion. 10.1016/j.peptides.2018.10.004 Anti-Anti-Influenza A virus DRAVPe01823 FLGAILKIGHALAKTVLPMVTNAFKPKQ 28 Figainin 2 Boana raniceps (Hypsiboas raniceps) A0A2L2DDD0 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "CHIKV,DENV,YFV" immunofluorescence assay [Ref.32443921]chikungunya virus (CHIKV):inhibition of viral infection in Huh7 cells(EC50=17 μM);##Dengue Serotype 4 Virus(DENV4):inhibition of viral infection in Huh7 cells(EC50=20.8 μM);##Yellow Fever viral (YFV):inhibition of viral infection in Huh7 cells(EC50=21.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.32443921]No cytotoxicity against noninfected Huh7 cells at concentrations as high as 25 µM. No predicted structure available DRAVPe01823.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 3007.72 C142H236N36O33S CDERSWY AKL 10.48 5 0 5 5 14 57.5 1085 1.1 hour 3 min 2 min 118.57 0 0 32443921 Biomolecules. 2020 May 20;10(5):790. "Santana CJC, Magalhães ACM, Prías-Márquez CA, Falico DA, Dos Santos Júnior ACM, Lima BD, Ricart CAO, de Pilger DRB, Bonotto RM, Moraes CB, Freitas-Júnior LH, Álvares ADCM, Freitas SM, Luz IS, Pires OR Jr, Fontes W, Castro MS." "Biological Properties of a Novel Multifunctional Host Defense Peptide from the Skin Secretion of the Chaco Tree Frog, Boana raniceps." 10.3390/biom10050790 "Anti-CHIKV,Anti-DENV,Anti-YFV" DRAVPe01824 QMRRKVELFTYMRFD 15 SP40 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EV-A71 Picornaviridae cell protection assay [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=18 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34314773]RD cells: CC50=228.7 μM. No predicted structure available DRAVPe01824.cif Linear Acetylation Amidation Free L Not found SP40 peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors 2020.4 C90H142N26O23S2 ACGHINPSW R 9.98 4 2 2 2 4 -83.33 -5447 0.8 hour 10 min >10 hour 45.33 1490 106.43 34314773 Virus Res. 2021 Oct 2;303:198456. "Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL." Stability and antiviral activity of SP40 peptide in human serum. 10.1016/j.virusres.2021.198456. Anti-EV-A71 DRAVPe01825 MRRKVELFTYMRFD 14 TP1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EV-A71 Picornaviridae cell protection assay [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34314773]RD cells: CC50=683.6 μM. No predicted structure available DRAVPe01825.cif Linear Acetylation Amidation Free L Not found The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. 1892.27 C85H134N24O21S2 ACGHINPQSW R 9.98 4 2 2 2 4 -64.29 -4893 30 hour >20 hour >10 hour 48.57 1490 114.62 34314773 Virus Res. 2021 Oct 2;303:198456. "Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL." Stability and antiviral activity of SP41 peptide in human serum. 10.1016/j.virusres.2021.198456. Anti-EV-A71 DRAVPe01826 RRKVELFTYMRFD 13 TP2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None EV-A71 Picornaviridae cell protection assay [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34314773]RD cells: CC50=345 μM. No predicted structure available DRAVPe01826.cif Linear Acetylation Amidation Free L Not found The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. 1761.07 C80H125N23O20S ACGHINPQSW R 9.98 4 2 2 2 4 -83.85 -5128 1 hour 2 min 2 min 52.31 1490 124.17 34314773 Virus Res. 2021 Oct 2;303:198456. "Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL." Stability and antiviral activity of SP42 peptide in human serum. 10.1016/j.virusres.2021.198456. Anti-EV-A71 DRAVPe01827 RKVELFTYMRFD 12 TP3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None EV-A71 Picornaviridae cell protection assay [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34314773]RD cells: CC50=1123 μM. No predicted structure available DRAVPe01827.cif Linear Acetylation Amidation Free L Not found The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. 1604.89 C74H113N19O19S ACGHINPQSW FR 8.59 3 2 1 2 4 -53.33 -3636 1 hour 2 min 2 min 56.67 1490 135.45 34314773 Virus Res. 2021 Oct 2;303:198456. "Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL." Stability and antiviral activity of SP43 peptide in human serum. 10.1016/j.virusres.2021.198456. Anti-EV-A71 DRAVPe01828 QMRRKVELFTYMRF 14 TP10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EV-A71 Picornaviridae cell protection assay [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.34314773]RD cells: CC50=231 μM. No predicted structure available DRAVPe01828.cif Linear Acetylation Amidation Free L Not found The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. 1905.31 C86H137N25O20S2 ACDGHINPSW R 10.9 4 1 3 2 4 -64.29 -4575 0.8 hour 10 min >10 hour 48.57 1490 114.62 34314773 Virus Res. 2021 Oct 2;303:198456. "Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL." Stability and antiviral activity of SP44 peptide in human serum. 10.1016/j.virusres.2021.198456. Anti-EV-A71 DRAVPe01829 AKVTMTCSAS 10 KP Synthetic construct P01680 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque reduction assay [Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (96% inhibition at 50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01829.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 998.18 C39H71N11O15S2 DEFGHILNPQRWY AST 8.27 1 0 1 5 3 53 -620 4.4 hour >20 hour >10 hour 49 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-HSV-1 DRAVPe01830 KKVTMTCSAS 10 K10S Synthetic construct P01680 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV-1, CoxV B5, AdV, VSV" "Herpesviridae, Picornaviridae, Adenoviridae, Rhabdoviridae" Plaque reduction assay "[Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (45% inhibition at 10 µg/ml, 76% inhibition at 50 µg/ml, 89% inhibition at 100 µg/ml);##Coxsackie virus B5:inhibition of viral replication in Vero cells (75% inhibition at 50 µg/ml, 94% inhibition at 100 µg/ml);##Vesicular Stomatitis Virus (VSV):inhibition of viral replication in Vero cells (78% inhibition at 50 µg/ml, 96% inhibition at 100 µg/ml);##Adenovirus:inhibition of viral replication in Vero cells (75% inhibition at 50 µg/ml, 91% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]20% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01830.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1055.27 C42H78N12O15S2 DEFGHILNPQRWY KST 9.31 2 0 2 5 2 -4 -1356 1.3 hour 3 min 2 min 39 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 "Anti-HSV-1, Anti-CoxV B5, Anti-AdV, Anti-VSV" DRAVPe01831 NQVSATCSVK 10 L5A Synthetic construct P0DOX5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None VSV Rhabdoviridae Plaque reduction assay "[Ref.30654366]Vesicular Stomatitis Virus (VSV):inhibition of viral replication in Vero cells (45% inhibition at 50 µg/ml, 50% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]20% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01831.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1036.17 C41H73N13O16S DEFGHILMPRWY SV 8.22 1 0 1 5 3 -5 -1593 1.4 hour 3 min >10 hour 68 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-VSV DRAVPe01832 KKLVAASQAALGL 13 K13L Synthetic construct P02768-2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None CoxV B5 Picornaviridae Plaque reduction assay "[Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 80% inhibition at 50 µg/ml, 87% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]30% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01832.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1269.55 C57H104N16O16 CDEFHIMNPRTWY A 10 2 0 2 2 8 79.23 694 1.3 hour 3 min 2 min 143.08 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-CoxV B5 DRAVPe01833 DSGEGDFLAEGGGVR 15 D15R Synthetic construct P02671 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None CoxV B5 Picornaviridae Plaque reduction assay "[Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (82% inhibition at 10 µg/ml, 85% inhibition at 50 µg/ml, 93% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01833.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1465.5 C60H92N18O25 CHIKMNPQTWY G 3.92 1 4 -3 6 4 -58 -3093 1.1 hour 3 min >10 hour 52 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-CoxV B5 DRAVPe01834 GLEEELQFSLGSKINVK 17 G17K Synthetic construct P0C0L5 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None CoxV B5 Picornaviridae Plaque reduction assay "[Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 75% inhibition at 50 µg/ml, 88% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01834.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1891.15 C84H139N21O28 ACDHMPRTWY EL 4.79 2 3 -1 5 6 -28.24 -2193 30 hour >20 hour >10 hour 108.82 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-CoxV B5 DRAVPe01835 SEETKENEGFTVTAEGK 17 S17K Synthetic construct P01024 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None AdV Adenoviridae Plaque reduction assay "[Ref.30654366]Adenovirus:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 65% inhibition at 50 µg/ml, 80% inhibition at 100 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01835.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1855.93 C77H122N20O33 CDHILMPQRWY E 4.32 2 5 -3 7 3 -139.41 -5219 1.9 hour >20 hour >10 hour 22.94 0 0 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 Anti-AdV DRAVPe01836 LCLRNWDQGHRP 12 L12P Synthetic construct A0M8Q8 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV-1, CoxV B5" "Herpesviridae, Picornaviridae" Plaque reduction assay "[Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (78% inhibition at 10 µg/ml, 84% inhibition at 50 µg/ml);##Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 42% inhibition at 50 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. No predicted structure available DRAVPe01836.cif Linear Free Free None L Not found No mechanism information found in the reference(s). 1494.69 C64H99N23O17S AEFIKMSTVY LR 8.26 3 1 2 3 3 -129.17 -4101 5.5 hour 3 min 2 min 65 5500 500 30654366 Intervirology. 2018;61(4):166-173. "Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C" Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. 10.1159/000494354 "Anti-HSV-1, Anti-CoxV B5" DRAVPe01837 GKRKSGCA 8 Entry 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 114.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 805.95 C31H59N13O10S DEFHILMNPQTVWY GK 10.06 3 0 3 4 1 -120 -2445 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01838 GKRKSGAA 8 Entry 6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 57.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 773.89 C31H59N13O10 CDEFHILMNPQTVWY AGK 11.17 3 0 3 3 2 -128.75 -2392 30 hour >20 hour >10 hour 25 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01839 GKRKSXCA 8 Entry 7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 22.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates phenylglycine(Phg). The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 860.23 C29H54N12O8S DEFHILMNPQTVWY K 10.06 3 0 3 3 1 -115 -2539 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01840 GKRKSFCA 8 Entry 8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 39.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 896.08 C38H65N13O10S DEHILMNPQTVWY K 10.06 3 0 3 3 2 -80 -2241 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01841 GKRKSXCA 8 Entry 9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 9.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 860.23 C29H54N12O8S DEFHILMNPQTVWY K 10.06 3 0 3 3 1 -115 -2539 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01842 GKRKSxCA 8 Entry 10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 38.7 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'x' at position 6 indicates D-homophenylalanine(D-hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-hPhe6) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 860.23 C29H54N12O8S DEFHILMNPQTVWY K 10.06 3 0 3 3 1 -115 -2539 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01843 GKRKSXAA 8 Entry 11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 18.4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 828.17 C29H54N12O8 CDEFHILMNPQTVWY AK 11.17 3 0 3 2 2 -123.75 -2486 30 hour >20 hour >10 hour 25 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01844 GKRKSXAX 8 Entry 12 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 22.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates homophenylalanine(Phg). The N-terminal and C-terminal cyclized by a amide bond." L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 868.42 C26H47N11O6 CDEFHILMNPQTVWY KX 11.17 3 0 3 2 1 -146.25 -2667 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01845 GKRKSXAx 8 Entry 13 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 15.1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates D-homophenylalanine(D-Phg). The N-terminal and C-terminal cyclized by a amide bond." Mixed(D-Phg8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 868.42 C26H47N11O6 CDEFHILMNPQTVWY K 11.17 3 0 3 2 1 -146.25 -2667 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01846 GKRKSXAF 8 Entry 14 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 19.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 904.27 C35H58N12O8 CDEHILMNPQTVWY K 11.17 3 0 3 2 2 -111.25 -2369 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01847 GKRKSXAf 8 Entry 15 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 7.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 904.27 C26H47N11O6 CDEFHILMNPQTVWY K 11.17 3 0 3 2 1 -146.25 -2667 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01848 GKRKSXAX 8 Entry 16 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 25.6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 and 8 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 868.42 C26H47N11O6 CDEFHILMNPQTVWY KX 11.17 3 0 3 2 1 -146.25 -2667 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01849 GKRKSXAx 8 Entry 17 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 16.2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 and 8 indicates homophenylalanine(hPhe/D-hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-hPhe8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 868.42 C26H47N11O6 CDEFHILMNPQTVWY K 11.17 3 0 3 2 1 -146.25 -2667 30 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01850 GKRKSXSf 8 Entry 18 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 5.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 920.27 C26H47N11O7 ACDEFHILMNPQTVWY KS 11.17 3 0 3 3 0 -178.75 -3188 30 hour >20 hour >10 hour 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01851 AKRKSXSf 8 Entry 19 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 28.5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 934.29 C27H49N11O7 CDEFGHILMNPQTVWY KS 11.17 3 0 3 2 1 -151.25 -3101 4.4 hour >20 hour >10 hour 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01852 aKRKSXSf 8 Entry 20 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Ala1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 934.29 C24H42N10O5 ACDEFGHILMNPQTVWY KS 11.17 3 0 3 2 0 -173.75 -3282 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01853 PKRKSXSf 8 Entry 21 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 52.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 960.33 C29H51N11O7 ACDEFGHILMNQTVWY KS 11.17 3 0 3 2 0 -193.75 -3282 >20 hour >20 hour ? 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01854 pKRKSXSf 8 Entry 22 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 0.95 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Pro1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 960.33 C24H42N10O5 ACDEFGHILMNPQTVWY KS 11.17 3 0 3 2 0 -173.75 -3282 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01855 pKRKSXSf 8 Entry 23 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 2.6 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=306.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50>400 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates L-2-naphthylalanine(l-2Nal). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Pro1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 960.33 C24H42N10O5 ACDEFGHILMNPQTVWY KS 11.17 3 0 3 2 0 -173.75 -3282 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01856 pKRKSXSf 8 Entry 24 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.8 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=293.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50>400 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Pro1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 960.33 C24H42N10O5 ACDEFGHILMNPQTVWY KS 11.17 3 0 3 2 0 -173.75 -3282 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01857 pRRKSXSf 8 Entry 25 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.8 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=108.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50>400 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Pro1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 988.34 C24H42N12O5 ACDEFGHILMNPQTVWY RS 12.01 3 0 3 2 0 -181.25 -4219 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01858 rRRKSXSf 8 Entry 26 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=87.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50>400 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Arg1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1047.42 C24H42N12O5 ACDEFGHILMNPQTVWY RS 12.3 3 0 3 2 0 -181.25 -4219 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01859 rRRKSXSr 8 Entry 27 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 2.3 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=141.1 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50>400 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. "Mixed(D-Arg1, 8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1056.43 C24H42N12O5 ACDEFGHILMNPQTVWY RS 12.48 3 0 3 2 0 -181.25 -4219 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01860 rRRKSXXf 8 Entry 28 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.6 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=23.2 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50=233 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-1-naphthylalanine(L-1Nal). The N-terminal and C-terminal cyclized by a amide bond." "Mixed(D-Arg1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1071.67 C21H35N11O2 ACDEFGHILMNPQTVWY RX 12.3 3 0 3 1 0 -171.25 -3879 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01861 rRRKAXXf 8 Entry 29 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=11.8 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50=134.1 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-1-naphthylalanine(L-1Nal). The N-terminal and C-terminal cyclized by a amide bond." "Mixed(D-Arg1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1055.67 C21H35N11O CDEFGHILMNPQSTVWY RX 12.3 3 0 3 0 1 -138.75 -3358 12.5 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01862 rRRKSXXf 8 Entry 30 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.5 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=48.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50=210 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-2-naphthylalanine(L-2Nal). The N-terminal and C-terminal cyclized by a amide bond." "Mixed(D-Arg1, Phe8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1071.67 C21H35N11O2 ACDEFGHILMNPQTVWY RX 12.3 3 0 3 1 0 -171.25 -3879 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01863 rRRKfXFx 8 Entry 31 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=4.6 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50=86 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates D-2-naphthylalanine(D-2Nal). The N-terminal and C-terminal cyclized by a amide bond." "Mixed(D-Arg1, Phe5, 2Nal8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1131.77 C27H39N11O ACDEGHILMNPQSTVWY R 12.3 3 0 3 0 1 -126.25 -3241 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01864 rRRKxXFx 8 Entry 32 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Fluorimetric assay [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.1 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=2.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28539222]BHK-21 cells: CC50=24 μM. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 6 indicates homophenylalanine(hPhe), position 5 and 8 indicates D-2-naphthylalanine(D-2Nal). The N-terminal and C-terminal cyclized by a amide bond." "Mixed(D-Arg1, 2Nal5, 8)" NS2B-NS3 protease "The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus." 1095.92 C27H39N11O ACDEGHILMNPQSTVWY R 12.3 3 0 3 0 1 -126.25 -3241 0 0 0 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. "Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y." Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. 10.1016/j.bmcl.2017.05.027 Anti-DENV DRAVPe01865 CGGGGGSLTEINTELLDLEYEMKKLEEVVKKLEESYIDLKEL 42 PIH Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae [Ref.31099550]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.171 μM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.31099550]PIH displayed no significant cytotoxicity to 293T, Huh-7, and L02 cells even at a high concentration of 100 μM." No predicted structure available Linear Free Free None L membrane "Inhibits MERS-Cov S protein-mediated cell fusion, which is the major pathway of MERS-CoV-induced host infections." 4717.37 C207H340N48O72S2 AFHPQRW E 4.32 5 11 -6 13 12 -40.24 -5973 1.2 hour >20 hour >10 hour 106.67 2980 72.68 31099550 ACS Appl Mater Interfaces. 2019 Jun 5;11(22):19799-19807. "Huang X, Li M, Xu Y, Zhang J, Meng X, An X, Sun L, Guo L, Shan X, Ge J, Chen J, Luo Y, Wu H, Zhang Y, Jiang Q, Ning X. " Novel Gold Nanorod-Based HR1 Peptide Inhibitor for Middle East Respiratory Syndrome Coronavirus. 10.1021/acsami.9b04240 Anti-MERS-CoV DRAVPe01866 PWLKPGDLDL 10 DET2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Plaque formation assay "[Ref.23630436]dengue virus 2(DENV2):inhibition of viral replication in LLC-MK2 cells(41.5±20.0% inhibition at 200 µM, IC50>500 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.23630436]Monkey kidney epithelial cells LLC-MK2: 8% Cell death at 500 µM. No predicted structure available Linear Free Free None L E protein "The peptide caused structural abnormalities and alteration of the arrangement of the viral E protein, which interferes with virus binding and entry. " 1153.34 C55H84N12O15 ACEFHIMNQRSTVY L 4.21 1 2 -1 1 4 -40 -496 >20 hour >20 hour ? 117 5500 611.11 23630436 Int J Med Sci. 2013 Apr 16;10(6):719-29. "Alhoot MA, Rathinam AK, Wang SM, Manikam R, Sekaran SD." Inhibition of dengue virus entry into target cells using synthetic antiviral peptides. 10.7150/ijms.5037 Anti-DENV DRAVPe01867 AGVKDGKLDF 10 DET4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Plaque formation assay "[Ref.23630436]dengue virus 2(DENV2):inhibition of viral replication in LLC-MK2 cells(84.6±5.6% inhibition at 500 µM, IC50=35 µM)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.23630436]Monkey kidney epithelial cells LLC-MK2: 5% Cell death at 500 µM. No predicted structure available Linear Free Free None L E protein "The peptide caused structural abnormalities and alteration of the arrangement of the viral E protein, which interferes with virus binding and entry. " 1049.19 C47H76N12O15 CEHIMNPQRSTWY DGK 6 2 2 0 2 4 -30 -1291 4.4 hour >20 hour >10 hour 78 0 0 23630436 Int J Med Sci. 2013 Apr 16;10(6):719-29. "Alhoot MA, Rathinam AK, Wang SM, Manikam R, Sekaran SD." Inhibition of dengue virus entry into target cells using synthetic antiviral peptides. 10.7150/ijms.5037 Anti-DENV DRAVPe01868 WLVFFVIFYFFR 12 FP1 (Tkip) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.09360 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 1684.06 C93H118N16O14 ACDEGHKMNPQST F 8.75 1 0 1 1 10 200 2009 2.8 hour 3 min 2 min 113.33 6990 635.45 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01869 WLVFFVIAYFAR 12 FP2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00087 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 1531.86 C81H110N16O14 CDEGHKMNPQST F 8.75 1 0 1 1 10 183.33 1775 2.8 hour 3 min 2 min 130 6990 635.45 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01870 WLVFFVIFYFFRRRKK 16 FP3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00003 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 2252.78 C117H166N28O18 ACDEGHMNPQST F 11.73 5 0 5 1 10 45 -2085 2.8 hour 3 min 2 min 85 6990 466 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01871 RRKKWLVFFVIFYFFR 16 FP4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00004 µM);##influenza A virus PR8/Eng09 (H1N1):inhibition of viral replication in MDCK cells(IC50=0.0778 µM);##influenza A virus PR8/Vic (H3N2):inhibition of viral replication in MDCK cells(IC50=0.0535 µM);##influenza A virus PR8/Viet (H5N1):inhibition of viral replication in MDCK cells(IC50=0.1325 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 2252.78 C117H166N28O18 ACDEGHMNPQST F 11.73 5 0 5 1 10 45 -2085 1 hour 2 min 2 min 85 6990 466 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01872 RRKKIFYFFR 10 FP7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.15483 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 1460.79 C72H109N21O12 ACDEGHLMNPQSTVW FR 11.73 5 0 5 1 4 -97 -4214 1 hour 2 min 2 min 39 1490 165.56 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01873 WLVFFVRRKK 10 FP8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.63806 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 1378.73 C69H107N19O11 ACDEGHIMNPQSTY FKRV 12.02 4 0 4 0 6 1 -1965 2.8 hour 3 min 2 min 97 5500 611.11 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01874 FFVIFYRRKK 10 FP9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza virus Orthomyxoviridae Plaque reduction assay [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=1.48175 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L HA the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. 1403.74 C71H106N18O12 ACDEGHLMNPQSTW F 11.1 4 0 4 1 5 -10 -2318 1.1 hour 3 min 2 min 68 1490 165.56 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. "Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. " A novel family of peptides with potent activity against influenza A viruses. 10.1099/vir.0.038679-0 Anti-Influenza virus DRAVPe01875 GYRARPKFKAGKR 13 HPV-31 L1 Cta Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae luminescence assay [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(86±3% inhibition at 10 μg/ml); inhibition of pseudovirions infection(91±4% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1534.83 C69H115N25O15 CDEHILMNQSTVW KR 11.74 6 0 6 3 3 -173.08 -5307 30 hour >20 hour >10 hour 15.38 1490 124.17 15170645 J Med Virol. 2004 Jul;73(3):474-80. "Bousarghin L, Touzé A, Yvonnet B, Coursaget P." Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. 10.1002/jmv.20114 Anti-HPV DRAVPe01876 TTTPAKRKKTKK 12 HPV-31 L1 Ctb Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HPV Papillomaviridae luminescence assay [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(12±10% inhibition at 10 μg/ml); inhibition of pseudovirions infection(15±8% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1387.69 C60H114N20O17 CDEFGHILMNQSVWY K 11.39 6 0 6 4 1 -221.67 -5114 7.2 hour >20 hour >10 hour 8.33 0 0 15170645 J Med Virol. 2004 Jul;73(3):474-80. "Bousarghin L, Touzé A, Yvonnet B, Coursaget P." Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. 10.1002/jmv.20114 Anti-HPV DRAVPe01877 MLRKRRKRL 9 HPV-16 L2 Ct Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae luminescence assay [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(78±6% inhibition at 10 μg/ml); inhibition of pseudovirions infection(96±20% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1256.62 C53H105N23O10S ACDEFGHINPQSTVWY R 12.48 6 0 6 0 2 -181.11 -5859 30 hour >20 hour >10 hour 86.67 0 0 15170645 J Med Virol. 2004 Jul;73(3):474-80. "Bousarghin L, Touzé A, Yvonnet B, Coursaget P." Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. 10.1002/jmv.20114 Anti-HPV DRAVPe01878 GCKKYRRFRWKFKGKFWFWG 20 Pep19-2.5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "HIV, HSV-1, HCV, HBV" "Retroviridae,Herpesviridae, Flaviviridae, Hepadnaviridae" luciferase infection assay [Ref.22457281]HIV-1 BaL:inhibition of viral entry in 293T cells(IC50=8 µg/ml);##HIV-1 NL4-3:inhibition of viral entry in 293T cells(IC50=16 µg/ml);##HSV-1:inhibition of viral entry in Vero cells(IC50=0.42 µg/ml);##Hepatitis C virus (HCV):inhibition of viral entry in 293T cells(IC50=40 µg/ml);##Hepatitis B virus (HBV):inhibition of viral entry in 293T cells(IC50=1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL." No predicted structure available Linear Free Free None L membrane "SALPs block entry of a variety of human pathogenic enveloped viruses, such as HIV-1, HBV, HCV, and HSV 1 and 2 by blocking heparan sulfate on the host cell plasma membrane, which serves as a the docking molecule for these pathogens." 2712.26 C135H187N37O22S ADEHILMNPQSTV K 11.17 8 0 8 5 7 -122.5 -4964 30 hour >20 hour >10 hour 0 17990 946.84 22457281 J Infect Dis. 2012 Jun;205(11):1654-64. "Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U." A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses. 10.1093/infdis/jis273 "Anti-HIV, Anti-HSV-1, Anti-HCV, Anti-HBV" DRAVPe01879 GKKYRRFRWKFKFGKWFWFG 20 Pep19-4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV, HSV-1, HCV" "Retroviridae,Herpesviridae, Flaviviridae" luciferase infection assay [Ref.22457281]HIV-1 BaL:inhibition of viral entry in 293T cells(IC50=22 µg/ml);##HIV-1 NL4-3:inhibition of viral entry in 293T cells(IC50=10 µg/ml);##HSV-1:inhibition of viral entry in Vero cells(IC50=1.8 µg/ml);##Hepatitis C virus (HCV):inhibition of viral entry in 293T cells(IC50=37 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry "[Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL." No predicted structure available Linear Free Free None L membrane "SALPs block entry of a variety of human pathogenic enveloped viruses, such as HIV-1, HBV, HCV, and HSV 1 and 2 by blocking heparan sulfate on the host cell plasma membrane, which serves as a the docking molecule for these pathogens." 2756.3 C141H191N37O22 ACDEHILMNPQSTV FK 11.76 8 0 8 4 8 -121 -4794 30 hour >20 hour >10 hour 0 17990 946.84 22457281 J Infect Dis. 2012 Jun;205(11):1654-64. "Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U." A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses. 10.1093/infdis/jis273 "Anti-HIV, Anti-HSV-1, Anti-HCV" DRAVPe01880 ATSSANSKA 9 Loop3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None JEV Flaviviridae Plaque assay [Ref.22465300]Japanese encephalitis virus(JEV):inhibition of viral replication in BHK-21 cells(IC50=10 ± 1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22465300]Did not stimulate significant cytotoxicity in BHK-21 cells even at 200 μM. No predicted structure available Linear Free Free None L Envelope protein prevent JEV infection by interfering in virus attachment to the cells. 835.87 C32H57N11O15 CDEFGHILMPQRVWY AS 8.8 1 0 1 5 3 -56.67 -1953 4.4 hour >20 hour >10 hour 33.33 0 0 22465300 Antiviral Res. 2012 May;94(2):179-83. "Li C, Zhang LY, Sun MX, Li PP, Huang L, Wei JC, Yao YL, Isahg H, Chen PY, Mao X." Inhibition of Japanese encephalitis virus entry into the cells by the envelope glycoprotein domain III (EDIII) and the loop3 peptide derived from EDIII. 10.1016/j.antiviral.2012.03.002 Anti-JEV DRAVPe01881 SISNALNKLEESNRNLDKVNVKLT 24 C24 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None NDV Paramyxoviridae Plaque reduction assay [Ref.12127571]Newcastle disease virus (NDV):inhibition of syncytium formation between NDV-infected cells(IC50=3.27 μM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L F protein "By binding to the opposite HR region in the F protein, peptides would inhibit fusion from the initial steps (lipid- and contents-mixing), blocking the conformational changes in the fusion protein required for triggering fusion." 2700.04 C114H199N35O40 CFGHMPQWY N 8.22 4 3 1 9 8 -72.5 -6539 1.9 hour >20 hour >10 hour 109.58 0 0 12127571 Int J Biochem Cell Biol. 2002 Oct;34(10):1207-20. "San Román K, Villar E, Muñoz-Barroso I." Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus. 10.1016/s1357-2725(02)00045-6 Anti-NDV DRAVPe01882 KQNAANILRLKESIAATNEAVHEV 24 N24 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None NDV Paramyxoviridae Plaque reduction assay [Ref.12127571]Newcastle disease virus (NDV):inhibition of syncytium formation between NDV-infected cells(IC50=22.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L F protein "By binding to the opposite HR region in the F protein, peptides would inhibit fusion from the initial steps (lipid- and contents-mixing), blocking the conformational changes in the fusion protein required for triggering fusion." 2619.96 C112H191N35O37 CDFGMPWY A 6.76 4 3 1 5 11 -31.25 -4573 1.3 hour 3 min 2 min 110 0 0 12127571 Int J Biochem Cell Biol. 2002 Oct;34(10):1207-20. "San Román K, Villar E, Muñoz-Barroso I." Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus. 10.1016/s1357-2725(02)00045-6 Anti-NDV DRAVPe01883 GRRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA 49 HLFcin 1-49 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae Western blotting [Ref.17481742]human papillomavirus(HPV):inhibition of pseudovirus infection in C33A cells(IC50=0.32±0.18μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic Free Free "Disulfide bonds between Cys10 and Cys46, Cys20 and Cys37." L Not found No mechanism information found in the reference(s). 5743.71 C244H403N85O66S5 HLY R 11.24 11 2 9 12 13 -85.1 -15425 30 hour >20 hour >10 hour 53.67 11250 234.38 17481742 Antiviral Res. 2007 Sep;75(3):258-65. "Mistry N, Drobni P, Näslund J, Sunkari VG, Jenssen H, Evander M." The anti-papillomavirus activity of human and bovine lactoferricin. 10.1016/j.antiviral.2007.03.012 Anti-HPV DRAVPe01884 FKCRRWQWRMKKLGAPSITCVRRAFA 26 BLfcinB 17-42 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae Western blotting [Ref.17481742]human papillomavirus(HPV):inhibition of pseudovirus infection in C33A cells(IC50=0.25±0.24 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic Free Free Disulfide bonds between Cys3 and Cys20. L Not found No mechanism information found in the reference(s). 3196.9 C144H231N47O30S3 DEHNY R 11.84 8 0 8 5 10 -48.46 -6698 1.1 hour 3 min 2 min 52.69 11125 445 17481742 Antiviral Res. 2007 Sep;75(3):258-65. "Mistry N, Drobni P, Näslund J, Sunkari VG, Jenssen H, Evander M." The anti-papillomavirus activity of human and bovine lactoferricin. 10.1016/j.antiviral.2007.03.012 Anti-HPV DRAVPe01885 AGDDQGLDKCVPNSKEK 17 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutinin assay [Ref.22595270]Influenza A virus (A/Roma-ISS/2/08 H1N1):inhibition of viral replication in MDCK cells(EC50=3.7±0.35 pM);##Influenza A virus (A/Parma/24/09 H1N1):inhibition of viral replication in MDCK cells(EC50=3.4±0.14 pM);##Influenza A virus (A/Parma/05/06 H3N2):inhibition of viral replication in MDCK cells(EC50=7.3±0.65 pM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22595270]MDCK cells:CC50>25 μM. No predicted structure available Linear Free Free None L HA The peptide may bind with HA and precent the attachment to target cells. 1803.96 C73H122N22O29S FHIMRTWY DK 4.68 3 4 -1 5 3 -138.82 -5127 4.4 hour >20 hour >10 hour 45.88 0 0 22595270 Pathog Glob Health. 2012 Mar;106(1):12-9. "Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F." Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus. 10.1179/2047773212Y.0000000004 Anti-Anti-Influenza A virus DRAVPe01886 NGESSADWAKN 11 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutinin assay [Ref.22595270]Influenza A virus (A/Roma-ISS/2/08 H1N1):inhibition of viral replication in MDCK cells(EC50=225±5.8 fM);##Influenza A virus (A/Parma/24/09 H1N1):inhibition of viral replication in MDCK cells(EC50=50±1.37 fM);##Influenza A virus (A/Parma/05/06 H3N2):inhibition of viral replication in MDCK cells(EC50=22.5±1.16 pM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22595270]MDCK cells:CC50>25 μM. No predicted structure available Linear Free Free None L HA The peptide may bind with HA and precent the attachment to target cells. 1178.18 C48H71N15O20 CFHILMPQRTVY ANS 4.37 1 2 -1 5 3 -156.36 -3427 1.4 hour 3 min >10 hour 18.18 5500 550 22595270 Pathog Glob Health. 2012 Mar;106(1):12-9. "Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F." Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus. 10.1179/2047773212Y.0000000004 Anti-Anti-Influenza A virus DRAVPe01887 SKHSSLDCVLRP 12 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutinin assay [Ref.22595270]Influenza A virus (A/Roma-ISS/2/08 H1N1):inhibition of viral replication in MDCK cells(EC50=4±0.37 pM);##Influenza A virus (A/Parma/24/09 H1N1):inhibition of viral replication in MDCK cells(EC50=3.1±0.12 pM);##Influenza A virus (A/Parma/05/06 H3N2):inhibition of viral replication in MDCK cells(EC50=5.8±0.7 pM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.22595270]MDCK cells:CC50>25 μM. No predicted structure available Linear Free Free None L HA The peptide may bind with HA and precent the attachment to target cells. 1341.55 C56H96N18O18S AEFGIMNQTWY S 7.97 3 1 2 4 3 -40 -2889 1.9 hour >20 hour >10 hour 89.17 0 0 22595270 Pathog Glob Health. 2012 Mar;106(1):12-9. "Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F." Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus. 10.1179/2047773212Y.0000000004 Anti-Anti-Influenza A virus DRAVPe01888 AVSKVLHLEGEVNKISALLSTNKAVVSLSNGVSVLTSKVLDLDNYIDKQLLPIVNK 56 HR1-30a Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cell fusion assay [Ref.12615056]respiratory syncytial virus(RSV):inhibition of cell fusion in Hep2 cells( IC50=1.68 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L F protein Peptide derived from hRSV F protein give strong virus–cell fusion inhibition effect. 5989 C268H458N70O83 CFMRW LV 8.35 7 5 2 17 25 33.75 -3793 4.4 hour >20 hour >10 hour 142.5 1490 27.09 12615056 Biochem Biophys Res Commun. 2003 Mar 14;302(3):469-75. "Wang E, Sun X, Qian Y, Zhao L, Tien P, Gao GF." Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. 10.1016/s0006-291x(03)00197-9 Anti-RSV DRAVPe01889 NFYDPLVFPSDEFDASISQVNEKINQSLASIRKSDELLHNVNAGK 45 HR2-30a Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RSV Paramyxoviridae Cell fusion assay [Ref.12615056]respiratory syncytial virus(RSV):inhibition of cell fusion in Hep2 cells( IC50=2.93 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L F protein Peptide derived from hRSV F protein give strong virus–cell fusion inhibition effect. 5051.56 C223H346N60O74 CMTW S 4.65 5 7 -2 13 16 -51.11 -9449 1.4 hour 3 min >10 hour 86.67 1490 33.86 12615056 Biochem Biophys Res Commun. 2003 Mar 14;302(3):469-75. "Wang E, Sun X, Qian Y, Zhao L, Tien P, Gao GF." Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. 10.1016/s0006-291x(03)00197-9 Anti-RSV DRAVPe01890 NKGCATCSIGAACLVDGPIPDFEIAGAtGLfGLWG 35 Subtilosin-A Bacillus subtilis O07623 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1PXQ HSV-2 Herpesviridae Plaque formation assay "[Ref.25087911]herpes simplex virus type 2(HSV-2): inhibition of viral replication in Vero cells(90% inhibition at 25 μg/mL,EC50= 18.2μg/mL)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.25087911]Vero cells: CC50=316.8 μg/mL. No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The N-terminal and C-terminal cyclized by a amide bond. Thioether bridges between Cys4 and Phe31,Cys7 and Thr28,Cys13 and Phe22." "Mixed(D-Thr28,D-Phe31)" Not found Subtilosin displays antiviral and virucidal actions against HSV-2. The target of subtilosin inhibitory effect would be late stages of the viral replicative cycle such as viral glycoprotein intracellular transport. 3425.94 C139H214N36O41S3 HMQRY G 4.03 1 3 -2 13 14 63.14 1593 1.4 hour 3 min >10 hour 89.43 5625 165.44 25087911 J Appl Microbiol. 2014 Nov;117(5):1253-9. "Quintana VM, Torres NI, Wachsman MB, Sinko PJ, Castilla V, Chikindas M." Antiherpes simplex virus type 2 activity of the antimicrobial peptide subtilosin. 10.1111/jam.12618 Anti-HSV-2 DRAVPe01891 RRKKAAVALLPAVLLALLAP 20 EB Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutinin assay [Ref.17005658]Influenza A virus(A/Hong Kong/483/97 ([HK/483] strain H5N1)): inhibition of viral replication by preventing attachment to cRBCs(IC50=8 μM); inhibition of influenza virus-induced cell death and replication in vitro(IC50=4.5 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17005658]No cytotoxicity against MDCK cells up to 50μM No predicted structure available Linear Free Free None L HA "The binding of EB to HA could lead to a conformation change in HA, decreasing the affinity for sialic acids on the cell surface. " 2084.67 C98H178N28O21 CDEFGHIMNQSTWY AL 12.02 4 0 4 0 14 110 752 1 hour 2 min 2 min 176 0 0 17005658 J Virol. 2006 Dec;80(24):11960-7. "Jones JC, Turpin EA, Bultmann H, Brandt CR, Schultz-Cherry S." Inhibition of influenza virus infection by a novel antiviral peptide that targets viral attachment to cells. 10.1128/JVI.01678-06 Anti-Anti-Influenza A virus DRAVPe01892 EF 2 EF Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming reduction assay [Ref.24612829]dengue virus 2(DENV2):inhibition of viral entry in Vero cells(IC50=96.50 µM); inhibition of viral replication in Vero cells(83.47% inhibition at 200 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24612829]No cytotoxicity against Vero cells up to 500 µM. No predicted structure available Linear Free Free None L E protein No mechanism information found in the reference(s). 294.31 C14H18N2O5 ACDGHIKLMNPQRSTVWY EF 4 0 1 -1 0 1 -35 -383 1 hour 30 min >10 hour 0 0 0 24612829 Chem Biol Drug Des. 2014 Aug;84(2):148-57. "Panya A, Bangphoomi K, Choowongkomon K, Yenchitsomanus PT. " Peptide inhibitors against dengue virus infection. 10.1111/cbdd.12309 Anti-DENV DRAVPe01893 KEN 3 KEN Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming reduction assay [Ref.24612829]dengue virus 2(DENV2):inhibition of viral entry in Vero cells(IC50=331.9 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.24612829]No cytotoxicity against Vero cells up to 500 µM. No predicted structure available Linear Free Free None L E protein No mechanism information found in the reference(s). 389.41 C15H27N5O7 ACDFGHILMPQRSTVWY EKN 6 1 1 0 1 0 -363.33 -1900 1.3 hour 3 min 2 min 0 0 0 24612829 Chem Biol Drug Des. 2014 Aug;84(2):148-57. "Panya A, Bangphoomi K, Choowongkomon K, Yenchitsomanus PT. " Peptide inhibitors against dengue virus infection. 10.1111/cbdd.12309 Anti-DENV DRAVPe01894 SVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPG 41 MLH40 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae cell-based flavivirus immunodetection assay [Ref.25891143]dengue virus 1(DENV1):inhibition of viral infection in Vero cells(IC50=30.35 ± 1.25 μM);##dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=31.41 ± 1.09 μM);##dengue virus 3(DENV3):inhibition of viral infection in Vero cells(IC50=27.95 ± 1.41 μM);##dengue virus 4(DENV4):inhibition of viral infection in Vero cells(IC50=24.45 ± 1.20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 4684.37 C209H325N61O58S2 CDFNY EGTV 6.79 7 4 3 11 14 -30.73 -5772 1.9 hour >20 hour >10 hour 80.73 16500 412.5 25891143 Chem Biol Drug Des. 2015 Nov;86(5):1093-104. "Panya A, Sawasdee N, Junking M, Srisawat C, Choowongkomon K, Yenchitsomanus PT. " A peptide inhibitor derived from the conserved ectodomain region of DENV membrane (M) protein with activity against dengue virus infection. 10.1111/cbdd.12576 Anti-DENV DRAVPe01895 GLLYFAIFFVAAWHIRGR 18 H2-2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=1.60 ± 0.11 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=2.19 ± 0.16 μM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. [Ref.26251517]Huh7.5.1 cells: CC50=83.64 ± 6.95 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 2137.56 C107H153N27O20 CDEKMNPQST AF 10.84 3 0 3 3 12 107.78 766 30 hour >20 hour >10 hour 119.44 6990 411.18 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. "Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. " A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. 10.1074/jbc.M115.662452 Anti-HCV DRAVPe01896 HGLLYFAIFFVAAWHIRGR 19 H2-3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=0.54 ± 0.08 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=1.09 ± 0.11 μM);H2-3 peptide inactivated HCV(EC50=82.11 nM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. [Ref.26251517]Huh7.5.1 cells: CC50=115.99 ± 16.68 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 2274.7 C113H160N30O21 CDEKMNPQST AF 10.84 4 0 4 3 12 85.26 300 3.5 hour 10 min >10 hour 113.16 6990 388.33 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. "Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. " A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. 10.1074/jbc.M115.662452 Anti-HCV DRAVPe01897 WPFCLLLMAL 10 H3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=0.52 ± 0.07 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=1.54 ± 0.73 μM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. [Ref.26251517]Huh7.5.1 cells: CC50=47.22 ± 5.29 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1206.57 C60H91N11O11S2 DEGHIKNQRSTVY L 5.52 0 0 0 1 7 217 3043 2.8 hour 3 min 2 min 166 5500 611.11 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. "Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. " A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. 10.1074/jbc.M115.662452 Anti-HCV DRAVPe01898 LYGNEGCGWAGWLLSPRG 18 SL173 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae ELISA [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(80% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1936.17 C88H126N24O24S DFHIKMQTV G 5.99 1 1 0 9 6 -18.33 -470 5.5 hour 3 min 2 min 70.56 12490 734.71 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. "Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. " Peptide inhibitors of hepatitis C virus core oligomerization and virus production. 10.1099/vir.0.008565-0 Anti-HCV DRAVPe01899 GWAGWLLSPRGSRPSWGP 18 SL174 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HCV Flaviviridae ELISA [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(15% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1967.22 C92H131N27O22 CDEFHIKMNQTVY G 12 2 0 2 7 6 -61.67 -1764 30 hour >20 hour >10 hour 48.89 16500 970.59 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. "Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. " Peptide inhibitors of hepatitis C virus core oligomerization and virus production. 10.1099/vir.0.008565-0 Anti-HCV DRAVPe01900 GWAGWLLSPRGSRPS 15 SL175 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae ELISA [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(50% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 1626.84 C74H111N23O19 CDEFHIKMNQTVY GS 12 2 0 2 6 5 -54.67 -2091 30 hour >20 hour >10 hour 58.67 11000 785.71 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. "Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. " Peptide inhibitors of hepatitis C virus core oligomerization and virus production. 10.1099/vir.0.008565-0 Anti-HCV DRAVPe01901 MDVNP 5 PB1 (1–5) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=185 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 574.65 C23H38N6O9S ACEFGHIKLQRSTWY DMNPV 3.8 0 1 -1 1 1 -50 -897 30 hour >20 hour >10 hour 58 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01902 MDVNPTLLFLKVPAQNAISTTFPYT 27 PB1 (1–25) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=122 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 2782.25 C129H197N29O35S CEGHRW T 5.59 1 1 0 8 10 28.89 -722 30 hour >20 hour >10 hour 86.67 1490 57.31 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01903 TLLFLKVPAQNAISTTFPYT 21 PB1 (6–25) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=129 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 2225.61 C106H163N23O28 CDEGHMRW T 8.26 1 0 1 7 9 49.05 175 7.2 hour >20 hour >10 hour 97.62 1490 74.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01904 AQNAISTTFPYT 12 PB1 (14–25) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=380 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1313.43 C59H88N14O20 CDEGHKLMRVW T 5.57 0 0 0 6 4 -15.83 -1191 4.4 hour >20 hour >10 hour 49.17 1490 135.45 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01905 MEVVQQTRMDKLTQGRQTYD 21 PB1 (111–130) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=58 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 2427.73 C100H165N31O34S2 ACFHINPSW Q 5.88 3 3 0 5 3 -120 -7101 30 hour >20 hour >10 hour 46.19 1490 74.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01906 LPVGGNEKKAKLANVVRKMM 21 PB1 (271–290) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=33 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 2183.7 C95H169N29O24S2 CDFHIQSTWY K 10.46 5 1 4 4 7 -25.71 -2505 5.5 hour 3 min 2 min 88.1 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01907 FNESTR 6 PB1 (381–386) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=664 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 752.78 C31H48N10O12 ACDGHIKLMPQVWY EFNRST 6 1 1 0 3 1 -170 -3136 1.1 hour 3 min 2 min 0 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01908 FNESTRKKIE 10 PB1 (381–390) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=400 ± 8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1251.41 C54H90N16O18 ACDGHLMPQVWY EK 8.59 3 2 1 3 2 -170 -4435 1.1 hour 3 min 2 min 39 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01909 FNESTRKKIEKIRPLLVEGT 21 PB1 (381–400) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=23 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 2358.77 C105H178N30O30 ACDHMQWY EK 9.7 5 3 2 5 6 -72.86 -5446 1.1 hour 3 min 2 min 88.1 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01910 KIRPLLVEGT 10 PB1 (391–400) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=71 ± 3μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1125.38 C51H92N14O14 ACDFHMNQSWY L 8.75 2 1 1 2 4 17 -1011 1.3 hour 3 min 2 min 146 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01911 MFNMLSTVLG 10 PB1 (411–420) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=369 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1112.37 C49H81N11O14S2 ACDEHIKPQRWY LM 5.28 0 0 0 4 4 130 989 30 hour >20 hour >10 hour 107 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01912 IGVTVI 6 PB1 (525–530) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=833 ± 6 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 600.76 C28H52N6O8 ACDEFHKLMNPQRSWY IV 5.52 0 0 0 2 4 271.67 1629 20 hour 30 min >10 hour 226.67 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01913 IGVTVIKNNMI 11 PB1 (525–535) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=416 ± 3μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1201.49 C53H96N14O15S ACDEFHLPQRSWY I 8.75 1 0 1 4 5 107.27 473 20 hour 30 min >10 hour 159.09 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01914 TLLFLKVP 8 PB1 (6–13) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=102 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 930.2 C47H79N9O10 ACDEGHIMNQRSWY L 8.41 1 0 1 1 5 152.5 1366 7.2 hour >20 hour >10 hour 182.5 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01915 TLLFLKVP 8 PB1 (6–13)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=35 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 930.2 C47H79N9O10 ACDEGHIMNQRSWY L 8.41 1 0 1 1 5 152.5 1366 7.2 hour >20 hour >10 hour 182.5 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01916 TLLFLKVP 8 Ac-PB1 (6–13) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=33 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 930.2 C47H79N9O10 ACDEGHIMNQRSWY L 8.41 1 0 1 1 5 152.5 1366 7.2 hour >20 hour >10 hour 182.5 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01917 TLLFLKVP 8 Ac-PB1 (6–13)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=12 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 930.2 C47H79N9O10 ACDEGHIMNQRSWY L 8.41 1 0 1 1 5 152.5 1366 7.2 hour >20 hour >10 hour 182.5 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01918 TLLFLKVPA 9 PB1 (6–14) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=34 ± 2 μM);##Influenza A virus(A/Puerto Rico/8/34 (H1N1)):antiviral activity of the peptide in MDCK cells(ED50=8.9 ± 1.0 μM);##Influenza A virus(A/Aichi/2/68 (H3N2)):antiviral activity of the peptide in MDCK cells(ED50=10.7 ± 0.9 μM);##Influenza A virus(A/Mallard/Pennsylvania/10218/84 (H5N2)):antiviral activity of the peptide in MDCK cells(ED50=8.5 ± 1.1 μM);##Influenza A virus(A/Vladivostok/02/09 of H1N1):antiviral activity of the peptide in MDCK cells(ED50=1.7 ± 0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1001.28 C50H84N10O11 CDEGHIMNQRSWY L 8.41 1 0 1 1 6 155.56 1547 7.2 hour >20 hour >10 hour 173.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01919 TLLFLKVPA 9 PB1 (6–14)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=6 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1001.28 C50H84N10O11 CDEGHIMNQRSWY L 8.41 1 0 1 1 6 155.56 1547 7.2 hour >20 hour >10 hour 173.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01920 TLLFLKVPA 9 Ac-PB1 (6–14) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=82 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1001.28 C50H84N10O11 CDEGHIMNQRSWY L 8.41 1 0 1 1 6 155.56 1547 7.2 hour >20 hour >10 hour 173.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01921 TLLFLKVPA 9 Ac-PB1 (6–14)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=4 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1001.28 C50H84N10O11 CDEGHIMNQRSWY L 8.41 1 0 1 1 6 155.56 1547 7.2 hour >20 hour >10 hour 173.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01922 GDPPY 5 PB1 (26–30) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=115 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 547.57 C25H33N5O9 ACEFHIKLMNQRSTVW P 3.8 0 1 -1 2 0 -168 -792 30 hour >20 hour >10 hour 0 1490 372.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01923 GDPPY 5 PB1 (26–30)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=100 ± 5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 547.57 C25H33N5O9 ACEFHIKLMNQRSTVW P 3.8 0 1 -1 2 0 -168 -792 30 hour >20 hour >10 hour 0 1490 372.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01924 GDPPY 5 Ac-PB1 (26–30) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=95 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 547.57 C25H33N5O9 ACEFHIKLMNQRSTVW P 3.8 0 1 -1 2 0 -168 -792 30 hour >20 hour >10 hour 0 1490 372.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01925 GDPPY 5 Ac-PB1 (26–30)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=254 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 547.57 C25H33N5O9 ACEFHIKLMNQRSTVW P 3.8 0 1 -1 2 0 -168 -792 30 hour >20 hour >10 hour 0 1490 372.5 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01926 LLVEGT 6 PB1 (395–400) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=91 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 630.74 C28H50N6O10 ACDFHIKMNPQRSWY L 4 0 1 -1 2 3 120 544 5.5 hour 3 min 2 min 178.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01927 LLVEGT 6 PB1 (395–400)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=794 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 630.74 C28H50N6O10 ACDFHIKMNPQRSWY L 4 0 1 -1 2 3 120 544 5.5 hour 3 min 2 min 178.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01928 LLVEGT 6 Ac-PB1 (395–400) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=297 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 630.74 C28H50N6O10 ACDFHIKMNPQRSWY L 4 0 1 -1 2 3 120 544 5.5 hour 3 min 2 min 178.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01929 LLVEGT 6 Ac-PB1 (395–400)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=744 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 630.74 C28H50N6O10 ACDFHIKMNPQRSWY L 4 0 1 -1 2 3 120 544 5.5 hour 3 min 2 min 178.33 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01930 KNNMINNDLG 10 PB1 (531–540) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=51 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1132.26 C45H77N15O17S ACEFHPQRSTVWY N 5.84 1 1 0 5 2 -116 -2770 1.3 hour 3 min 2 min 78 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01931 KNNMINNDLG 10 PB1 (531–540)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=44 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1132.26 C45H77N15O17S ACEFHPQRSTVWY N 5.84 1 1 0 5 2 -116 -2770 1.3 hour 3 min 2 min 78 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01932 KNNMINNDLG 10 Ac-PB1 (531–540) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=71 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Free None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1132.26 C45H77N15O17S ACEFHPQRSTVWY N 5.84 1 1 0 5 2 -116 -2770 1.3 hour 3 min 2 min 78 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01933 KNNMINNDLG 10 Ac-PB1 (531–540)-NH2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A virus Orthomyxoviridae Hemagglutination assay [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=109 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Acetylation Amidation None L Not found "The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication." 1132.26 C45H77N15O17S ACEFHPQRSTVWY N 5.84 1 1 0 5 2 -116 -2770 1.3 hour 3 min 2 min 78 0 0 25446335 Antiviral Res. 2015 Jan;113:4-10. "Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI." Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. 10.1016/j.antiviral.2014.10.015 Anti-Anti-Influenza A virus DRAVPe01934 LNLFKKTINGLISDSLVIR 19 AVP-p Synthetic construct A0A7D5DRX8## P03540 Experimentally Validated 3052300 GPC QLA46850.1 348 to 366 pfam00798 MK896487 Genomic RNA Not Available None "PICV,JUNV" Arenaviridae Plaque reduction assay "[Ref.24850726]Pichinde virus (PICV):inhibition of viral infection in Vero cells(IC50=7.05 ± 2.19 μM);##Arenaviruses (TAMV, JUNV, MACV, LASV): Inhibition (IC50 = 2–10 μM);##Complete inhibition of viral plaque formation at ~20 μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref.24850726]No significant loss of viability was observed in Vero cells or human foreskin fibroblasts (HFF) up to 100 μM. No predicted structure available Linear Free Free None L Membrane That untimely deployment of fusion machinery by the peptide could render virions less able to engage in on-pathway receptor binding or endosomal fusion. 2144.59 C98H170N26O27 ACEHMPQWY L 9.99 3 1 2 6 9 53.68 -1499 5.5 hour 3 min 2 min 158.95 0 0 24850726 J Virol. 2014 Aug;88(15):8556-64. "Spence JS, Melnik LI, Badani H, Wimley WC, Garry RF. " Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism. 10.1128/JVI.01133-14 Anti-PICV DRAVPe01935 GRKKRRQRRRC 11 TAT-Cd0 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Antiviral assay [Ref.21029018]Herpes simplex virus type 1(HSV-1):inhibition of viral infection in human corneal epithelial (HCE) cells(EC50=0.20 μM); exert antiviral activity by entry block(EC50=0.1 μM);exert antiviral activity by postentry(EC50~30.0 μM);exert antiviral activity by cell protection(EC50=0.4 μM);exert antiviral activity by virus inactivation(EC50=9.5 μM);exert antiviral activity by inhibitng attachment(EC50=3.0 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.21029018]human corneal epithelial (HCE) cells:CC50~100 μM. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1499.81 C58H114N32O13S ADEFHILMNPSTVWY R 12.3 8 0 8 2 0 -329.09 -10394 30 hour >20 hour >10 hour 0 0 0 21029018 J Ocul Pharmacol Ther. 2010 Dec;26(6):541-7. "Larsen IV, Brandt CR." A cationic TAT peptide inhibits Herpes simplex virus type 1 infection of human corneal epithelial cells. 10.1089/jop.2010.0076 DRAVPa1018 Anti-HSV-1 DRAVPe01936 GREERRQRRRC 11 "E50,51TAT-Cd0" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Antiviral assay [Ref.21029018]Herpes simplex virus type 1(HSV-1):inhibition of viral infection in human corneal epithelial (HCE) cells(EC50~30.0 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 1501.69 C56H104N30O17S ADFHIKLMNPSTVWY R 11.7 6 2 4 2 0 -321.82 -10646 30 hour >20 hour >10 hour 0 0 0 21029018 J Ocul Pharmacol Ther. 2010 Dec;26(6):541-7. "Larsen IV, Brandt CR." A cationic TAT peptide inhibits Herpes simplex virus type 1 infection of human corneal epithelial cells. 10.1089/jop.2010.0076 Anti-HSV-1 DRAVPe01937 NDSRGIDAEEELETKAELVITKLKTPLMRGKVVVGAAGA 39 MDVgHH2L Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "NDV,MDV" "Paramyxoviridae, Herpesviridae" Plaque formation assay [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=43.4 ± 2.0 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=34.0 ± 2.00 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L membrane "peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes " 4110.74 C177H306N50O59S CFHQWY AE 5.15 6 7 -1 9 15 -17.44 -6044 1.4 hour 3 min >10 hour 102.56 0 0 24412629 J Virol Methods. 2014 Apr;199:11-6. "Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ." In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. 10.1016/j.jviromet.2013.12.022 "Anti-NDV,Anti-MDV" DRAVPe01938 NADIIKSLIRKTIINASKNTASLSILQHLYVLRS 34 MDVgBH3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "NDV,MDV" "Paramyxoviridae, Herpesviridae" Plaque formation assay [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=52.9 ± 0.9 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=37.5 ± 1.2 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L membrane "peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes " 3795.48 C169H293N49O49 CEFGMPW I 10.45 6 1 5 11 15 22.06 -4402 1.4 hour 3 min >10 hour 143.53 1490 45.15 24412629 J Virol Methods. 2014 Apr;199:11-6. "Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ." In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. 10.1016/j.jviromet.2013.12.022 "Anti-NDV,Anti-MDV" DRAVPe01939 LGNVNNSISNALDKLEESNSKLDKVNVKLTGTSAL 35 NDVHR2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None "NDV,MDV" "Paramyxoviridae, Herpesviridae" Plaque formation assay [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=18.9 ± 2.8 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=65.3 ±0.9 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L membrane "peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes " 3687.12 C156H269N45O57 CFHMPQRWY LN 6.21 4 4 0 15 12 -38 -6318 5.5 hour 3 min 2 min 108.57 0 0 24412629 J Virol Methods. 2014 Apr;199:11-6. "Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ." In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. 10.1016/j.jviromet.2013.12.022 "Anti-NDV,Anti-MDV" DRAVPe01940 TIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFV 43 HRA1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HMPV Paramyxoviridae RT-PCR assay [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=177 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). No predicted structure available Linear Free Free None L F protein "In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process." 4656.4 C204H353N59O64 CHMPQWY V 9.52 7 5 2 12 19 4.65 -6990 7.2 hour >20 hour >10 hour 115.58 0 0 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-MPV DRAVPe01941 AKTIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFVSKN 48 HRA2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HMPV Paramyxoviridae RT-PCR assay [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=2.1 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). No predicted structure available Linear Free Free None L F protein "In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process." 5185.01 C226H393N67O71 CHMPQWY AKV 9.99 9 5 4 14 20 -17.29 -8923 4.4 hour >20 hour >10 hour 105.63 0 0 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-MPV DRAVPe01942 LESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRE 35 HRA3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HMPV Paramyxoviridae RT-PCR assay [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=3240 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). No predicted structure available Linear Free Free None L F protein "In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process." 3683.22 C158H277N47O53 CDFHMPQWY AV 8.5 5 4 1 11 15 -2 -5500 5.5 hour 3 min 2 min 111.43 0 0 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-MPV DRAVPe01943 FNVALDQVFESIENSQALVDQSNRILSSAEKGNTG 35 HRB5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HMPV Paramyxoviridae RT-PCR assay [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=1520 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). No predicted structure available Linear Free Free None L F protein "In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process." 3782.09 C161H258N46O59 CHMPWY S 4.18 2 5 -3 12 13 -34 -7110 1.1 hour 3 min 2 min 89.14 0 0 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-MPV DRAVPe01944 PEDQFNVALDQVFESIENSQALVDQSNRILSSAEKGNTG 39 HRB6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HMPV Paramyxoviridae RT-PCR assay [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=3310 nM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). No predicted structure available Linear Free Free None L F protein "In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process." 4251.54 C180H285N51O68 CHMWY S 3.95 2 7 -5 12 13 -61.54 -9217 >20 hour >20 hour ? 80 0 0 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-MPV DRAVPe01945 SWLVNRDWFHDLNLPWTGSSAGTWQ 25 TP1 Synthetic construct No entry found Experimentally Validated 64293 Genome polyprotein Genome polyprotein Genome polyprotein Not Available JF895923 Genomic RNA Not Available 6ZQJ TMUV Flaviviridae "Plaque assay, Western blotting" [Ref.32456819]Tembusu virus (TMUV):inhibition of viral infection in BHK-21 cells(IC50=14.19 mg/L). No hemolysis information or data found in the reference(s) presented in this entry [Ref.32456819]No cytotoxicity against BHK-21 cells up to 150mg / L. No predicted structure available Linear Free Free None L Not found TP1 functions through a mechanism that involves release of the viral genome and interference with cellular TMUV binding 2974.24 C138H189N37O38 CEIKMY W 5.19 2 2 0 9 10 -59.2 -3639 1.9 hour >20 hour >10 hour 62.4 22000 916.67 32456819 Vet Microbiol. 2020 Jun;245:108708. "Zhao D, Zhang L, Han K, Liu Q, Yang J, Huang X, Liu Y, Li Y, Zhao P. " Peptide inhibitors of tembusu virus infection derived from the envelope protein.  10.1016/j.vetmic.2020.108708 Anti-TMUV DRAVPe01946 MVALGDTAWDFGSVGGVLTSIGKGIHQVFGSAFKSL 36 TP2 Synthetic construct No entry found Experimentally Validated 64293 10971339 JF895923.2 Not Available TIGR04240 JF895923 Genomic RNA Not available None TMUV Flaviviridae "Plaque assay, Western blotting" [Ref.32456819]Tembusu virus (TMUV):inhibition of viral infection in BHK-21 cells(IC50=7.64 mg/L). No hemolysis information or data found in the reference(s) presented in this entry [Ref.32456819]No cytotoxicity against BHK-21 cells up to 150mg / L. No predicted structure available Linear Free Free None L Not found TP2 might be an interference factor between TMUV and the cell. 3654.2 C167H258N42O48S CENPRY G 6.5 3 2 1 13 16 64.17 891 30 hour >20 hour >10 hour 94.72 5500 157.14 32456819 Vet Microbiol. 2020 Jun;245:108708. "Zhao D, Zhang L, Han K, Liu Q, Yang J, Huang X, Liu Y, Li Y, Zhao P. " Peptide inhibitors of tembusu virus infection derived from the envelope protein.  10.1016/j.vetmic.2020.108708 Anti-TMUV DRAVPe01947 RRRQRRKKRGYGFVNLLFLVVE 22 TAT-Kα2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "VSV,NDV,RSV,Influenza virus, HSV" "Herpesviridae,Paramyxoviridae,Orthomyxoviridae" Plaque assay [Ref.28687749]Vesicular stomatitis virus(VSV):inhibition of viral infection in 293T cells(IC50=2.9 μM);##Respiratory Syncytial Virus(RSV):inhibition of viral infection in Hep2 cells(IC50=3.4 μM);##Newcastle disease virus(NDV):inhibition of viral infection(IC50=0.8 μM);##Parainfluenza virus:inhibition of viral infection(IC50=2.4 μM);##Influenza virus (H1N1) A/Puerto Rico/8/34:inhibition of viral infection(IC50=0.5 μM);##Influenza virus (H5N2) A/bird/Korea/W81/2005:inhibition of viral infection(IC50=0.8 μM);##Influenza virus (H7N3) A/Aquatic bird/Korea/W44/2005:inhibition of viral infection(IC50=1.2 μM);##Influenza virus (H9N2) A/Chicken/Korea/116/2004:inhibition of viral infection(IC50=0.7 μM);##Porcine epidemic diarrhea virus:inhibition of viral infection(IC50=3.5 μM);##Herpes simplex virus:inhibition of viral infection(IC50=5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.28687749]No cytotoxicity against MDCK cells up to 100 μM. No predicted structure available Linear Free Free None L Envolope display virucidal activity by disrupting viral envelopes. 2791.35 C126H212N44O28 ACDHIMPSTW R 12.01 8 1 7 4 8 -80.91 -8503 1 hour 2 min 2 min 92.73 1490 70.95 28687749 Sci Rep. 2017 Jul 7;7(1):4875. "Moon HJ, Nikapitiya C, Lee HC, Park ME, Kim JH, Kim TH, Yoon JE, Cho WK, Ma JY, Kim CJ, Jung JU, Lee JS." Inhibition of highly pathogenic avian influenza (HPAI) virus by a peptide derived from vFLIP through its direct destabilization of viruses 10.1038/s41598-017-04777-4 "Anti-VSV,NDV,Anti-RSV,Anti-Influenza virus, Anti-HSV" DRAVPe01948 MGRFKRFRKKFKKLFKKLS 19 Bomidin Synthetic construct P54228 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "DENV, HSV,SARS-CoV-2" "Flaviviridae,Herpesviridae,Coronaviridae" "Plaque-formation assay,fluorescent focus assay, ELISA" [Ref.35663971]Dengue virus 2(DENV2):inhibition of viral infection in Huh7 cells(50% inhibition at 10 μM);##HSV:inhibition of viral infection in Huh7 cells(50% inhibition at 10 μM);##SARS-CoV-2:inhibition of viral infection in Huh7 cells(80% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.35663971]Vero E6 cells:CC50=169.6 ± 1.1 µM. No predicted structure available Linear Free Free None L membrane bomidin readily disrupted viral membranes (with components similar to those in the endoplasmic reticulum) and bacterial membranes but did not alter the overall structures of the cell membranes 2474.14 C118H197N35O21S ACDEHINPQTVWY K 12.32 10 0 10 2 6 -112.11 -6196 30 hour >20 hour >10 hour 41.05 0 0 35663971 Front Immunol. 2022 May 19;13:851642. "Liu R, Liu Z, Peng H, Lv Y, Feng Y, Kang J, Lu N, Ma R, Hou S, Sun W, Ying Q, Wang F, Gao Q, Zhao P, Zhu C, Wang Y, Wu X. " Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses. 10.3389/fimmu.2022.851642 "Anti-DENV, Anti-HSV,Anti-SARS-CoV-2" DRAVPe01949 DHVTPDIAYNPRTYM 15 Pep-RTYM Acacia catechu No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus-Forming Unit (FFU) Assay [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=7.9 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. No predicted structure available Linear Free Free None L Not found the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. 1792.98 C79H117N21O25S CEFGKLQSW DPTY 5.21 2 2 0 5 3 -86.67 -3596 1.1 hour 3 min >10 hour 52 2980 212.86 33172110 Viruses. 2020 Nov 6;12(11):1267. "Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT. " Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. 10.3390/v12111267 Anti-DENV DRAVPe01950 DHVTPDIAYNPWAYF 15 Pep-WAYF Acacia catechu No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Focus-Forming Unit (FFU) Assay [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=15.67 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. No predicted structure available Linear Free Free None L Not found the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. 1808.97 C87H113N19O24 CEGKLMQRS ADPY 4.2 1 2 -1 4 6 -40 -1370 1.1 hour 3 min >10 hour 58.67 8480 605.71 33172110 Viruses. 2020 Nov 6;12(11):1267. "Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT. " Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. 10.3390/v12111267 Anti-DENV DRAVPe01951 DHVTPDIAYNP 11 Pep-CORE Acacia catechu No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None DENV Flaviviridae Focus-Forming Unit (FFU) Assay [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=20.89 μM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. No predicted structure available Linear Free Free None L Not found the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. 1241.32 C55H80N14O19 CEFGKLMQRSW DP 4.2 1 2 -1 3 3 -76.36 -2068 1.1 hour 3 min >10 hour 70.91 1490 149 33172110 Viruses. 2020 Nov 6;12(11):1267. "Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT. " Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. 10.3390/v12111267 Anti-DENV DRAVPe01952 KKR 3 Cmpd 2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None ZIKV Flaviviridae Protease assay [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(IC50=41.0 ± 3.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Phenylacetyl Free None L NS2B-NS3 viral serine protease The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. 430.55 C18H38N8O4 ACDEFGHILMNPQSTVWY K 11.17 3 0 3 0 0 -410 -2602 1.3 hour 3 min 2 min 0 0 0 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. "Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM. " SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  10.1016/j.bmc.2022.116631 Anti-ZIKV DRAVPe01953 KKR 3 Cmpd 11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None ZIKV Flaviviridae Protease assay [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(IC50=3.6 ± 0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Phenylacetyl Amidation None L NS2B-NS3 viral serine protease The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. 430.55 C18H38N8O4 ACDEFGHILMNPQSTVWY K 11.17 3 0 3 0 0 -410 -2602 1.3 hour 3 min 2 min 0 0 0 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. "Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM. " SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  10.1016/j.bmc.2022.116631 Anti-ZIKV DRAVPe01954 GKR 3 Cmpd 12 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None ZIKV Flaviviridae Protease assay [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(40% inhibition at 100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Phenylacetyl Free None L NS2B-NS3 viral serine protease The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. 359.43 C14H29N7O4 ACDEFHILMNPQSTVWY GKR 11 2 0 2 1 0 -293.33 -1953 30 hour >20 hour >10 hour 0 0 0 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. "Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM. " SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  10.1016/j.bmc.2022.116631 Anti-ZIKV DRAVPe01955 GKR 3 Cmpd 13 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None ZIKV Flaviviridae Protease assay [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(40% inhibition at 100 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Phenylacetyl Amidation None L NS2B-NS3 viral serine protease The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. 359.43 C14H29N7O4 ACDEFHILMNPQSTVWY GKR 11 2 0 2 1 0 -293.33 -1953 30 hour >20 hour >10 hour 0 0 0 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. "Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM. " SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  10.1016/j.bmc.2022.116631 Anti-ZIKV DRAVPe01956 ALWMTLLKKVLKAAAKAALNAVLVGANA 28 Dermaseptin-4 Phyllomedusa sauvagii P80280 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Chemiluminescence Reporter Gene Assay [Ref.15780876]human immunodeficiency virus type 1 (HIV-1):Inhibition of viral infection in Vero P4-CCR5 cells(IC50=2 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15780876]P4-CCR5 cells:CC50=5.6 μM. No predicted structure available Linear Free Amidation None L viral membrane "exerts a selective activity on viral particles and disturbs their organization by breaking the viral membrane, leading to the exposure of HIV-1 core and its dissociation. " 2850.55 C132H229N35O32S CDEFHIPQRSY A 10.48 4 0 4 4 19 103.21 2550 4.4 hour >20 hour >10 hour 146.79 5500 203.7 15780876 Virology. 2005 Apr 10;334(2):264-75.  "Lorin C, Saidi H, Belaid A, Zairi A, Baleux F, Hocini H, Bélec L, Hani K, Tangy F." The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro.  10.1016/j.virol.2005.02.002 Anti-HIV DRAVPe01957 ALWKTLLKKVLKAAAK 16 Dermaseptin S4 (1-16)[M4K] Synthetic construct P80280 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Chemiluminescence Reporter Gene Assay [Ref.15780876]human immunodeficiency virus type 1 (HIV-1):Inhibition of viral infection in Vero P4-CCR5 cells(IC50=28 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.15780876]P4-CCR5 cells:CC50>100 μM. No predicted structure available Linear Free Amidation None L viral membrane "exerts a selective activity on viral particles and disturbs their organization by breaking the viral membrane, leading to the exposure of HIV-1 core and its dissociation. " 1782.29 C86H152N22O18 CDEFGHIMNPQRSY K 10.6 5 0 5 1 10 34.38 297 4.4 hour >20 hour >10 hour 140.63 5500 366.67 15780876 Virology. 2005 Apr 10;334(2):264-75.  "Lorin C, Saidi H, Belaid A, Zairi A, Baleux F, Hocini H, Bélec L, Hani K, Tangy F." The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro.  10.1016/j.virol.2005.02.002 Anti-HIV DRAVPe01958 GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP 41 "Beta-defensin 2(BD-2, hBD-2, SAP1)" Homo sapiens O15263 Experimentally Validated 9606 DEFB4A; DEFB4B Z71389.1 24-65 pfam00711 Z71389 mRNA Chromosome 8 - NC_000008.11 1FD4 HIV Retroviridae ELISA "[Ref.16254366]HIV-1 BaL:inhibition of viral infection in TZM-bl cells(80% Inhibition at 100 µg/ml, 68% Inhibition at 50 µg/ml, 55% Inhibition at 25 µg/ml, 45% Inhibition at 12.5 µg/ml, 32% Inhibition at 6.2 µg/ml, 28% Inhibition at 3.1 µg/ml, 18% Inhibition at 1.6 µg/ml, 20% Inhibition at 0.8 µg/ml,);##HIV-1 IIIB:inhibition of viral infection in TZM-bl cells(95% Inhibition at 100 µg/ml, 87% Inhibition at 50 µg/ml, 75% Inhibition at 25 µg/ml, 62% Inhibition at 12.5 µg/ml, 55% Inhibition at 6.2 µg/ml, 35% Inhibition at 3.1 µg/ml, 28% Inhibition at 1.6 µg/ml, 25% Inhibition at 0.8 µg/ml,)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry DRAVPe01958 Cyclic Free Free "Disulfide bonds between Cys8 and Cys37, Cys15 and Cys30, Cys20 and Cys38." L Not found No mechanism information found in the reference(s). 4334.24 C188H311N55O50S6 EMNW CG 9.3 8 1 7 17 9 -10.24 -3697 30 hour >20 hour >10 hour 64.15 1865 46.63 16254366 J Virol. 2005 Nov;79(22):14318-29.  "Sun L, Finnegan CM, Kish-Catalone T, Blumenthal R, Garzino-Demo P, La Terra Maggiore GM, Berrone S, Kleinman C, Wu Z, Abdelwahab S, Lu W, Garzino-Demo A." Human beta-defensins suppress human immunodeficiency virus infection: potential role in mucosal protection.  10.1128/JVI.79.22.14318-14329.2005 Anti-HIV DRAVPe01959 NEYHGFVDKANNENKRKKQQGRDDFVVKPNNFANRRRKDDYNENYYDDVDAADVV 55 Cicadin Cicada flammata P83282 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA "[Ref.11814612]HIV-1:inhibition the activity of reverse transcriptase(11.35±1.8% Inhibition at 0.1 µM, 85.8±2.3% Inhibition at 1 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 6596.04 C283H427N89O95 CILMSTW DN 5.7 12 12 0 15 13 -175.27 -24057 1.4 hour 3 min >10 hour 38.91 5960 110.37 11814612 Peptides. 2002 Jan;23(1):7-11.  "Wang H, Ng TB." "Isolation of cicadin, a novel and potent antifungal peptide from dried juvenile cicadas." 10.1016/s0196-9781(01)00573-3 Anti-HIV DRAVPe01960 CGESCAXISFCFTEVIGCSCKNKVCYLNSIS 31 "Leaf cyclotide, Vhl-1" Viola hederacea P84522 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1ZA8 HIV Retroviridae cytopathic effect assay [Ref.15824119]HIV-1:inhibition of cytopathic effect(EC50=0.87 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Cyclic No specific N-terminal No specific C-terminal "The 'X' at position 7 indicates Methionine sulfoxide. The N-terminal and C-terminal cyclized by a amide bond. Disulfide bonds between Cys1 and Cys18, Cys5 and Cys20, Cys11 and Cys25." L Not found No mechanism information found in the reference(s). 3321.08 C135H212N34O43S6 DHMPQRW C 6.1 2 2 0 17 9 62.9 -1262 1.2 hour >20 hour >10 hour 72.26 1865 62.17 15824119 J Biol Chem. 2005 Jun 10;280(23):22395-405. "Chen B, Colgrave ML, Daly NL, Rosengren KJ, Gustafson KR, Craik DJ. " "Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide." 10.1074/jbc.M501737200 Anti-HIV DRAVPe01961 QSHLSLCRWCCNCCRSNKGC 20 Hepcidin TH2-3 Oreochromis mossambicus I3KHK3 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FMDV Picornaviridae Plaque forming assay "[Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=25.1±1.5 µg/ml, IC90=78.5±7.6 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=120.2±2.5 µg/ml. No predicted structure available Cyclic Free Cyclization(Cys7 and Cys20) "Disulfide bonds between Cys7 and Cys20, Cys10 and Cys13, Cys11 and Cys14." L Not found No mechanism information found in the reference(s). 2301.7 C89H145N33O27S6 ADEFIMPTVY C 8.7 4 0 4 12 3 -38.5 -4828 0.8 hour 10 min >10 hour 39 5875 309.21 30012343 Peptides. 2018 Aug;106:91-95. "Huang HN, Pan CY, Chen JY. " Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. 10.1016/j.peptides.2018.07.003 Anti-FMDV DRAVPe01962 FIHHIIGGLFSVGKHIHSLIHGH 23 "Tilapia piscidin 3, TP3" Oreochromis niloticus L0CMD2 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None FMDV Picornaviridae Plaque forming assay "[Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=2.5±0.2 µg/ml, IC90=25.0±3.2 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=39.0±1.2 µg/ml. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 2557 C121H182N36O26 ACDEMNPQRTWY H 8.79 7 0 7 6 10 59.13 789 1.1 hour 3 min 2 min 131.3 0 0 30012343 Peptides. 2018 Aug;106:91-95. "Huang HN, Pan CY, Chen JY. " Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. 10.1016/j.peptides.2018.07.003 Anti-FMDV DRAVPe01963 FIHHIIGGLFSAGKAIHRLIRRRRR 25 "Tilapia piscidin 4, TP4" Oreochromis niloticus L0CKG3 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FMDV Picornaviridae Plaque forming assay "[Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=1.5±0.1 µg/ml, IC90=7.5±1.3 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=9.7±1.5 µg/ml. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 2981.6 C135H226N50O27 CDEMNPQTVWY R 12.7 10 0 10 4 11 -12.8 -6561 1.1 hour 3 min 2 min 117.2 0 0 30012343 Peptides. 2018 Aug;106:91-95. "Huang HN, Pan CY, Chen JY. " Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. 10.1016/j.peptides.2018.07.003 Anti-FMDV DRAVPe01964 GFIFHIIKGLFHAGKMIHGLV 21 Epinecidin-1 (22-42) Synthetic construct Q6JWQ9 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None FMDV Picornaviridae Plaque forming assay "[Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=0.6±0.1 µg/ml, IC90=12.5±1.1 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=19.5±3.1 µg/ml. No predicted structure available Linear Free Amidation None L Not found No mechanism information found in the reference(s). 2335.88 C114H175N29O22S CDENPQRSTWY GI 10 5 0 5 4 11 109.05 2534 30 hour >20 hour >10 hour 130 0 0 30012343 Peptides. 2018 Aug;106:91-95. "Huang HN, Pan CY, Chen JY. " Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. 10.1016/j.peptides.2018.07.003 Anti-FMDV DRAVPe01965 GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE 33 Pardaxin P-4 Pardachirus marmoratus P81861 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1XC0 FMDV Picornaviridae Plaque forming assay "[Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=2.4±0.1 µg/ml, IC90=12.1±1.1 µg/ml)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=19.5±3.2 µg/ml. DRAVPe01965 Linear Free Free None L Not found No mechanism information found in the reference(s). 3323.88 C154H248N36O45 CDHMNRWY S 8.59 2 1 1 12 15 74.55 1171 30 hour >20 hour >10 hour 112.42 0 0 30012343 Peptides. 2018 Aug;106:91-95. "Huang HN, Pan CY, Chen JY. " Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. 10.1016/j.peptides.2018.07.003 Anti-FMDV DRAVPe01966 AKKAAKKAKKAAKKIEKAAKK 21 RJ5-I15E16 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=112 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2238.84 C101H192N32O24 CDFGHLMNPQRSTVWY K 10.65 11 1 10 0 9 -130.95 -4846 4.4 hour >20 hour >10 hour 56.67 0 0 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01967 AKKAKKKAKKAAKKIKKKAKK 21 RJ9-I15 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=11 µM); inhibition of viral infection in MRC-5 cells(IC50=119 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2352.08 C108H211N35O22 CDEFGHLMNPQRSTVWY K 11.11 14 0 14 0 7 -187.14 -6192 4.4 hour >20 hour >10 hour 47.14 0 0 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01968 ARRARRRARRAARRARRGARR 21 RJ8-R5G18 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=1.9 µM); inhibition of viral infection in MRC-5 cells(IC50=4.8 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=96 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2603.06 C101H196N60O22 CDEFHIKLMNPQSTVWY R 13.08 13 0 13 1 7 -220.48 -18035 4.4 hour >20 hour >10 hour 33.33 0 0 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01969 ARRARRRARRAARRARRWARR 21 RJ8-R5W18 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=9.2 µM); inhibition of viral infection in MRC-5 cells(IC50=2.8 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=162 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2732.22 C110H203N61O22 CDEFGHIKLMNPQSTVY R 13.08 13 0 13 0 8 -222.86 -17896 4.4 hour >20 hour >10 hour 33.33 5500 275 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01970 KAAKKAAKWAKKAAKWAKKAA 21 "RJ2-W9,16" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=111 µM); inhibition of viral infection in MRC-5 cells(IC50=32 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=48 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2254.8 C106H180N32O22 CDEFGHILMNPQRSTVY A 10.9 9 0 9 0 12 -90 -2719 1.3 hour 3 min 2 min 47.62 11000 550 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01971 KYAKKAAKYAKKAAKYAKKAA 21 "RJ2-Y2,9,16" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=146 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2300.82 C108H182N30O25 CDEFGHILMNPQRSTVW AK 10.3 9 0 9 3 9 -108.57 -3408 1.3 hour 3 min 2 min 42.86 4470 223.5 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01972 AAKAWKKAKAWKKAKWWKKAA 21 "RJ2-A1,4,8; K3,6,7,9,13; W5,11,17" Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Not found [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=238 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. No predicted structure available Linear Free Free None L Not found No mechanism information found in the reference(s). 2485.07 C122H190N34O22 CDEFGHILMNPQRSTVY K 10.9 9 0 9 0 12 -115.71 -2615 4.4 hour >20 hour >10 hour 38.1 22000 1100 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. "Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T." "Prediction of activity, synthesis and biological testing of anti-HSV active peptides. " 10.1111/j.1747-0285.2006.00412.x Anti-HSV DRAVPe01973 WNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQ 36 "CHR-1, Env GP (623-658)" Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=17.27 ± 0.31 nM; IC90=26.41 ± 0.55 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L cell membrane "The peptide can interact with the viral NHR to form stable heterologous 6-HBs, resulting in inhibition of fusion between the viral and target cell membranes." 4532.84 C196H288N56O67S ACFGPV E 4.53 4 7 -3 12 8 -156.39 -11884 2.8 hour 3 min 2 min 54.17 17990 514 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. "Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. " HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides 10.1074/jbc.M609148200 Anti-HIV DRAVPe01974 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELLEL 36 "C36, Env GP (628-663)" Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=4.67 ± 0.07 nM; IC90=7.04 ± 0.12 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L cell membrane "The peptide can interact with the viral NHR to form stable heterologous 6-HBs, resulting in inhibition of fusion between the viral and target cell membranes." 4490.88 C195H298N52O68S ACFGPV E 4.14 3 9 -6 9 10 -119.17 -10359 2.8 hour 3 min 2 min 86.67 12490 356.86 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. "Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. " HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides 10.1074/jbc.M609148200 DRAVPa0917 Anti-HIV DRAVPe01975 REINNYTSLIHSLIEESQNQQEKNEQELLELDKWAS 36 "CHR-3, Env GP (633-668)" Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA "[Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=1,470.00 ± 20.0 nM; IC90=2,380.00 ± 35.00 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found CHR-3 interacts with N46 to form unstable 6-HB 4330.69 C186H294N52O67 CFGMPV E 4.42 4 8 -4 10 10 -120.28 -10860 1 hour 2 min 2 min 89.44 6990 199.71 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. "Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. " HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides 10.1074/jbc.M609148200 Anti-HIV DRAVPe01976 HSLIEESQNQQEKNEQELLELDKWASLWNWFNITNW 36 "CHR-5, Env GP (643-678)" Synthetic construct P04578 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA "[Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=2,185.00 ± 15.00 nM; IC90=2,858.00 ± 6.00 nM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Not found CHR-5 can bind to LUVs of POPC 4501.89 C203H295N53O64 CGMPRVY E 4.3 3 7 -4 9 13 -114.17 -8492 3.5 hour 10 min >10 hour 78.61 22000 628.57 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. "Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. " HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides 10.1074/jbc.M609148200 Anti-HIV DRAVPe01977 STSQKSIVAYTM 12 "SARS-CoV S (668–679), SP-10" Synthetic construct(derived from SARS-CoV S protein) P59594##P26436 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.1 668-679 Not Available CM000673.2##AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC SARS-CoV Coronaviridae Biochemical Assay [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=1.88 ± 0.52 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L ACE2 block the binding of S protein to ACE2. 1315.5 C56H94N14O20S CDEFGHLNPRW S 8.31 1 0 1 6 3 -0.83 -1345 1.9 hour >20 hour >10 hour 65 1490 135.45 16337697 Antiviral Res. 2006 Feb;69(2):70-6. "Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY." Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. 10.1016/j.antiviral.2005.10.005 Anti-SARS-CoV DRAVPe01978 GFLYVYKGYQPI 12 "SARS-CoV S (192-203), SP-4" Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae ELISA [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=4.30 ± 2.18 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L ACE2 block the binding of S protein to ACE2. 1447.7 C73H102N14O17 ACDEHMNRSTW Y 8.43 1 0 1 5 4 13.33 723 30 hour >20 hour >10 hour 89.17 4470 406.36 16337697 Antiviral Res. 2006 Feb;69(2):70-6. "Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY." Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. 10.1016/j.antiviral.2005.10.005 Anti-SARS-CoV DRAVPe01979 FYTTTGIGYQPY 12 "SARS-CoV S (483-494), SP-8" Synthetic construct P59594 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae ELISA [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=6.99 ± 0.71 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L ACE2 block the binding of S protein to ACE2. 1410.55 C68H91N13O20 ACDEHKLMNRSVW TY 5.52 0 0 0 8 2 -38.33 -389 1.1 hour 3 min 2 min 32.5 4470 406.36 16337697 Antiviral Res. 2006 Feb;69(2):70-6. "Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY." Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. 10.1016/j.antiviral.2005.10.005 Anti-SARS-CoV DRAVPe01980 IHAEIKNSLKIDNLDVNRCIEAL 23 LEDGF/p75 (355-377) Synthetic construct O75475 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae IN enzymatic assay [Ref.18331842]Human immunodeficiency virus (HIV): Inhibition of integrase activity (3' end processing)(IC50=165±28 µM); inhibition of integrase activity(strand transfer)(IC50=153±28 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L Integrase The LEDGF/p75 peptide modestly inhibited IN catalysis and was dependent on IN–DNA assembly. The peptide was also effective at disrupting LEDGF/p75–IN complex formation. 2622.03 C113H193N33O36S FGMPQTWY I 5.48 4 4 0 5 10 -4.78 -4168 20 hour 30 min >10 hour 140 0 0 18331842 FEBS Lett. 2008 Apr 30;582(10):1425-30. "Al-Mawsawi LQ, Christ F, Dayam R, Debyser Z, Neamati N." Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis. 10.1016/j.febslet.2008.02.076 Anti-HIV DRAVPe01981 IEEQAKTFLDKFQHEVEEIYWQS 23 "Peptide1(ACE2 (21-43)[N13Q,A16V,D18E,L19I,F20Y,Y21W])" Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=11 ± 1 nM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 2898.18 C133H193N31O42 CGMNPR E 4.41 3 6 -3 3 8 -94.78 -5236 20 hour 30 min >10 hour 67.83 6990 317.73 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01982 QDKHEEDYQMYNKGDKED 18 Peptide2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=18 ± 2 nM, 95% inhibition at 0.39 µM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 2272.34 C94H138N26O38S ACFILPRSTVW D 4.38 4 7 -3 4 0 -283.33 -9133 0.8 hour 10 min >10 hour 0 2980 175.29 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01983 DKFNHEAEDLFYQSSLASWNYNT 23 Peptide3 Synthetic construct Q9BYF1 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=6 ± 4 nM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 2779.92 C125H171N31O42 CGIMPRV NS 4.31 2 4 -2 9 7 -108.26 -5803 1.1 hour 3 min >10 hour 42.61 8480 385.45 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01984 IDENARSYIDKFQHDAEEMWYQ 22 Peptide4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=32 ± 2 nM, 95% inhibition at 0.39 µM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 2788.98 C123H174N32O41S CGLPTV DE 4.29 3 6 -3 4 6 -136.82 -7200 20 hour 30 min >10 hour 44.55 8480 403.81 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01985 IYALLENAEDYNLVN 15 Peptide5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=9 ± 4 nM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 1753.93 C79H120N18O27 CFGHKMPQRSTW LN 3.57 0 3 -3 5 7 0.67 -1520 20 hour 30 min >10 hour 136.67 2980 212.86 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01986 SRDKHEEHEKENDRGQ 16 Peptide6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae luciferase assay "[Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=10 ± 5 nM, 100% inhibition at 25 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Amidation None L Spike protein antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. 1994.02 C78H124N30O32 ACFILMPTVWY E 5.43 6 6 0 3 0 -327.5 -10958 1.9 hour >20 hour >10 hour 0 0 0 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  "Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR." Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein 10.1021/acs.jmedchem.1c00477 Anti-SARS-CoV-2 DRAVPe01987 LLGRMKG 7 None Synthetic construct Q91L67 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae Scintillation count [Ref.12469306]Hepatitis B virus(HBV): inhibition of the association of L-HBsAg with HBcAg(IC50=78±5 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L core antigen (HBcAg)(Viral assembly) "During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Peptide inhibits the association of L-HBsAg with core antigen (HBcAg)." 773.99 C33H63N11O8S ACDEFHINPQSTVWY GL 11 2 0 2 2 2 4.29 -640 5.5 hour 3 min 2 min 111.43 0 0 12469306 J Gen Appl Microbiol. 2002 Apr;48(2):103-7. Tan WS. Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens. 10.2323/jgam.48.103 Anti-HBV DRAVPe01988 LDPAFR 6 None Synthetic construct O92921 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae Scintillation count [Ref.12469306]Hepatitis B virus(HBV): inhibition of the association of L-HBsAg with HBcAg(IC50>1000 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L core antigen (HBcAg)(Viral assembly) "During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Peptide inhibits the association of L-HBsAg with core antigen (HBcAg)." 717.82 C33H51N9O9 CEGHIKMNQSTVWY ADFLPR 5.84 1 1 0 0 3 -20 -1393 5.5 hour 3 min 2 min 81.67 0 0 12469306 J Gen Appl Microbiol. 2002 Apr;48(2):103-7. Tan WS. Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens. 10.2323/jgam.48.103 Anti-HBV DRAVPe01989 PLSPPLRNTHPQAMQWNSTTF 21 None Synthetic construct O92921 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae Scintillation count [Ref.12469306]Hepatitis B virus(HBV): inhibition of the association of L-HBsAg with HBcAg(IC50=30±1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L core antigen (HBcAg)(Viral assembly) "During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Peptide inhibits the association of L-HBsAg with core antigen (HBcAg)." 2423.73 C108H163N31O31S CDEGIKVY P 10.18 2 0 2 7 5 -88.57 -3914 >20 hour >20 hour ? 41.9 5500 275 12469306 J Gen Appl Microbiol. 2002 Apr;48(2):103-7. Tan WS. Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens. 10.2323/jgam.48.103 Anti-HBV DRAVPe01990 PTSNHSPTSCPPTCPGYRWMCLRRF 25 HBV S(56-80) Synthetic construct O92921 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae Scintillation count [Ref.12469306]Hepatitis B virus(HBV): inhibition of the association of L-HBsAg with HBcAg(IC50=35±4 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L core antigen (HBcAg)(Viral assembly) "During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Peptide inhibits the association of L-HBsAg with core antigen (HBcAg)." 2895.34 C125H188N38O34S4 ADEIKQV P 9.27 4 0 4 12 3 -77.2 -5675 >20 hour >20 hour ? 15.6 7115 296.46 12469306 J Gen Appl Microbiol. 2002 Apr;48(2):103-7. Tan WS. Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens. 10.2323/jgam.48.103 Anti-HBV DRAVPe01991 GELGRLVYLLDGPGYDPIHCSLAYGDASTLVVF 33 K5-66 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=20.7±3.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-4A site that is of particular interest。 3511.99 C161H244N38O48S KMNQW L 4.22 2 4 -2 12 13 47.58 -320 30 hour >20 hour >10 hour 115.15 4470 139.69 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01992 GELGRLVYLLDGPGYDPI 18 K5-66-A Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=125.4 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-5A site that is of particular interest。 1947.22 C90H139N21O27 ACFHKMNQSTW GL 4.03 1 3 -2 6 6 8.33 -705 30 hour >20 hour >10 hour 124.44 2980 175.29 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01993 GELGRPVYVLGDPGYYATHCIYATTNDALIFSV 33 K6-10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=25.6±3.5 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-6A site that is of particular interest。 3577.03 C164H243N39O49S KMQW GY 4.54 2 3 -1 14 12 27.58 -1197 30 hour >20 hour >10 hour 94.55 5960 186.25 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01994 GELGRPVYVLGDPGYYAT 18 K6-10-A Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=227.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-7A site that is of particular interest。 1927.14 C89H131N21O27 CFHIKMNQSW G 4.37 1 2 -1 8 5 -17.22 -995 30 hour >20 hour >10 hour 81.11 4470 262.94 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01995 GELGRLVYLLDGPGYDPIHCDVVTRGGSHLFNF 33 CP5-46 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=11.3±1.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-8A site that is of particular interest。 3618.08 C164H246N44O47S AKMQW G 5.26 4 4 0 12 11 4.85 -3050 30 hour >20 hour >10 hour 97.27 2980 93.13 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01996 GELDELVYLLDGPGYDPIHCDVVTRGGSRLFNF 33 CP5-46-4D5E Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=1.14±0.053 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-9A site that is of particular interest。 3668.09 C165H248N42O51S AKMQW GL 4.23 3 6 -3 11 11 -5.45 -4231 30 hour >20 hour >10 hour 97.27 2980 93.13 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01997 GELGRLVYLLDGPGYDPIHCD 21 CP5-46-A Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=124 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-10A site that is of particular interest。 2302.59 C103H156N26O32S AFKMNQSTW GL 4.22 2 4 -2 7 6 -12.86 -1915 30 hour >20 hour >10 hour 106.67 2980 149 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01998 GELDELVYLLDGPGYDPIHS 20 CP5-46A-4D5E Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=22.8 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-11A site that is of particular interest。 2202.4 C100H148N22O34 ACFKMNQRTW L 3.77 1 5 -4 6 6 -23 -1666 30 hour >20 hour >10 hour 112 2980 156.84 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe01999 RQIKINFQNRRMKNKKGELDELVYLLDGPGYDPIHS 36 Ant-CP5-46A-4D5E Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref.22965230]hepatitis C virus(HCV): inhibition of NS3–4A activity(IC50=23.6 nM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information or data found in the reference(s) presented in this entry No predicted structure available Linear Free Free None L virus replication inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-12A site that is of particular interest。 4286.92 C190H306N56O55S ACTW KL 9.31 8 5 3 9 9 -104.17 -9945 1 hour 2 min 2 min 83.89 2980 85.14 22965230 J Biol Chem. 2012 Nov 9;287(46):39224-32.  "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe02000 ELLVTFKNAHAKKQEVVVLG 20 peptide 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 1 at 200 μM exhibited cell protection effects against DENV-1 (69.58%) and DENV-4 (59.44%), but lower inhibitory effects were observed against DENV-2 (32.95%) and DENV-3 (12.59%); Peptides 1(200 μM) demonstrated the highest inhibitions of DENV-3 (67.18%) plaque formations; Peptides 1 (200 μM) demonstrated inhibitions of all four DENV serotypes, but much lower inhibitions were observed against DENV-3 at 26.92%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2223.64 C102H171N27O28 CDIMPRSWY V 8.6 4 2 2 3 10 23 -1122 1 hour 30 min >10 hour 126.5 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02001 LKMDKLTLKGMSY 13 peptide 3 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]peptide 3 showed the most promising cell protection effects against DENV-1 (60.28%), DENV(36.23%), DENV-3 (73.85%), and DENV-4 (64.84%) at 200 μM. The IC50 of the cell protection effects of peptide 3 against DENV-3 was determined to be 182.27 μM; peptide 3 demonstrated the most promising antiviral activity during post-infection with good inhibitions of DENV-2 (69.05%) and DENV-3 (61.35%) whereas lower inhibitions were observed against DENV-1 (48.47%) and DENV-4 (34.72%) at 200 μM; Peptide 3 showed the highest inhibitions of plaque formations by DENV-2 (69.05%) and DENV-3 (61.35%); Peptide 3 reduced the RNA copy numbers of DENV-2 and DENV-3 by 43.83% and 50.72%, DENV-1 (31.85%); peptide 3 inhibited DENV-4 attachment to Vero cells by 39.58% but almost no inhibition was observed against DENV-1 (7.62%) and DENV-3 (2.56%). " No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found It is possible that peptide 3 inhibited DENV-2 by inhibiting the virus particle itself and this was supported by the observation that peptide 3 showed good direct virus-inactivating effects against DENV-2. 1527.9 C68H118N16O19S2 ACEFHINPQRVW KL 9.529999999999999 3 1 2 4 3 -24.62 -1108 5.5 hour 3 min 2 min 90 1490 124.17 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02002 TGKFKVVKEIAETQHGTIVIRVQYE 25 Peptide 4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]peptides 4 demonstrated some cell protection effects against DENV-2 and DENV-4 at 47.38%, inhibitions against the other DENV serotypes were very low; Peptide 4 at 200 μM showed the highest inhibitory effects against DENV-2 (74.26%), but it exhibited very low inhibition of DENV-4 and it could not inhibit DENV-1 and DENV-3 plaque formations; peptide 4 demonstrated the highest inhibitory effects against DENV-1 (80.37%),DENV-2 (44.77%) and DENV-4 (72.22%) during post-infection. The IC50 of the inhibitory effects of peptide 4 against DENV-1 during post-infection was determined to be 161.07 μM; Peptide 4 was observed to inhibit DENV-1 and DENV-4 replications significantly with reductions of RNA copy numbers by 63.86% and 70.37%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 2874.33 C130H213N35O38 CDLMNPSW V 8.130000000000001 5 3 2 6 9 -24.8 -3800 7.2 hour >20 hour >10 hour 97.2 1490 62.08 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02003 PFGDSYIVIGVGDSALTLHWFRK 23 Peptide 5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]peptides 5 demonstrated some cell protection effects against DENV-2 and DENV-4 at 59.72%, inhibitions against the other DENV serotypes were very low; exhibited good direct virus-inactivating effects against DENV-2 (64.61%) and DENV-4 (77.08%) whereas lower inhibitions were observed against DENV-1 (16.90%) and DENV-3 (29.80%). The IC50 of the direct virus-inactivating effects of peptide 5 against DENV-4 was determined to be 121.26 μM; peptide 5 demonstrated the highest inhibitory effects against DENV-4 (89.31%) and DENV-2 (19.94%) during post-infection. The IC50 of the inhibition of DENV-4 by peptide 5 during post-infection was determined to be 141.42 μM; Peptide 5 was observed to inhibit DENV-4 replications significantly with reductions of RNA copy numbers by 75.80%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found "peptide 5 could exert virucidal activity by damaging the protein coat of the virus, penetrating the virion, or destroying the viral genome to reduce viral infectivity. " 2578.95 C122H180N30O32 CEMNQ G 7.17 3 2 1 7 10 28.26 -1140 >20 hour >20 hour ? 97.39 6990 317.73 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02004 IQTSGGTSI 9 Peptide 6 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 6 at 200 μM exhibited cell protection effects against DENV-1 (40.88%) and DENV-4 (51.27%), but lower inhibitory effects were observed against DENV-2 (10%) and DENV-3 (22.05%); Peptides 6 (200 μM) demonstrated inhibitions of all four DENV serotypes, but much lower inhibitions were observed against DENV-3 at 3.33%, respectively." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 862.94 C35H62N10O15 ACDEFHKLMNPRVWY GIST 5.52 0 0 0 6 2 18.89 -576 20 hour 30 min >10 hour 86.67 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02005 MVDRGWGNGCGLFGKGGI 18 Peptide 7 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 7 at 200 μM exhibited good inhibitions of DENV-1 (67.17%) plaque formation, but much lower inhibitions were observed against DENV-2 to 4 ranging from 28.31 to 37.73%; peptide 7 (200 μM) showed good direct virus-inactivating effects against DENV-3 (64.03%) and DENV-4 (78.76%) whereas lower inhibitions were observed against DENV-1 (32.66%) and DENV-2 (47.84%); peptide 7 demonstrated highly significant inhibition of DENV-4 at 84.82% during post-infection, much lower inhibitions were observed against DENV-2 and 3 at 9.13% and 2.24%; Peptide 7 was observed to inhibit DENV-4 replications significantly with reductions of RNA copy numbers by 77.01%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1824.11 C79H122N24O22S2 AEHPQSTY G 7.98 2 1 1 9 5 3.33 -643 30 hour >20 hour >10 hour 59.44 5500 323.53 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02006 GAMHTALTGATE 12 Peptide 8 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 8 at 200 μM exhibited good inhibitions of DENV-1 (70.19%) plaque formation, but much lower inhibitions were observed against DENV-2 to 4 ranging from 28.31 to 37.73%; Peptides 8 showed highly significant inhibitions of DENV-4 plaque formation (80.31–83.92%), but lower inhibitions were observed against DENV-1 to 3 (5.34–55.46%); Peptide 8 was observed to inhibit DENV-4 replications significantly with reductions of RNA copy numbers by 73.42%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1159.28 C47H78N14O18S CDFIKNPQRSVWY AT 5.24 1 1 0 5 4 12.5 -460 30 hour >20 hour >10 hour 57.5 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02007 HAVGNDTSNHGVTA 14 Peptide 9 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 9 showed highly significant inhibitions of DENV-4 plaque formation (80.31–83.92%), but lower inhibitions were observed against DENV-1 to 3 (5.34–55.46%); Peptides 9 (200 μM) demonstrated the highest inhibitions of DENV-4 (83.92%) plaque formations; Peptide 9 at 200 μM showed inhibitions of all four DENV serotypes, but significantly lower inhibitions against DENV-2 (1.67%) and DENV-3 (3.48%) were observed. " No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1379.41 C55H86N20O22 CEFIKLMPQRWY AGHNTV 5.97 2 1 1 7 4 -56.43 -2628 3.5 hour 10 min >10 hour 55.71 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02008 SPRTGLDFNEMI 12 Peptide 10 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptide 10 (200 μM) exhibited inhibitions of all four DENV serotypes, with high inhibitions of DENV-4 at 81.13%, followed by DENV-3 at 60.47% and DENV-1 at 47.01%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1379.55 C59H94N16O20S ACHKQVWY DEFGILMNPRST 4.37 1 2 -1 4 3 -45.83 -2695 1.9 hour >20 hour >10 hour 65 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02009 TNTTT 5 Peptide 11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 11 at 200 μM exhibited cell protection effects below 50% against all four DENV serotypes(DENV-1, DENV-2, DENV-3, DENV-4); peptides 11 (200 μM) also showed inhibitions of all four DENV serotypes, but significantly lower inhibitions were observed against DENV-3 at 3.57%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 536.54 C20H36N6O11 ACDEFGHIKLMPQRSVWY T 5.19 0 0 0 5 0 -126 -1692 7.2 hour >20 hour >10 hour 0 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02010 DANFV 5 Peptide 12 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]Peptides 12 at 200 μM exhibited cell protection effects below 50% against all four DENV serotypes(DENV-1, DENV-2, DENV-3, DENV-4); peptide 12 (200 μM) also showed inhibitions of all four DENV serotypes, but significantly lower inhibitions were observed against DENV-3 at 2.28%." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM. No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 564.6 C25H36N6O9 CEGHIKLMPQRSTWY ADFNV 3.8 0 1 -1 1 3 36 -653 1.1 hour 3 min >10 hour 78 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02011 PFGDSYIVI 9 peptides 5F Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]At 100 μM, peptides 5F demonstrated some cell protection effects against DENV-1 (22.89%), DENV-2 (48.28%) and DENV-4(66.72%); Peptide 5F at 100 μM was observed to exhibit higher inhibition of DENV-4 at 66.72% during the pre-infection stage when compared to peptide 5 which only demonstrated 59.72% inhibition of DENV-4 at 200 μM; Peptides 5F(100 μM) also demonstrated direct virus-inactivating effects against DENV-1 at 46.75%, DENV-2(75.15%), DENV-3(10.81%), DENV-4(70.15%); Peptides 5F at 100 μM showed inhibitions against DENV-1 during the post-infection stage at 49.65%, DENV-2(47.49%), DENV-4(91.58%)." No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM.(cell viability was found to range between 92.98 and 100% at 200 μM). No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1010.15 C49H71N9O14 ACEHKLMNQRTW I 3.8 0 1 -1 3 4 93.33 554 >20 hour >20 hour ? 118.89 1490 186.25 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02012 VIGVGDSAL 9 peptides 5FG Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]At 100 μM, peptides 5FG demonstrated some cell protection effects against DENV-1 (24.83%), DENV-4(57.09%) and DENV-2 (52.21%); Peptides 5FG (100 μM) also demonstrated direct virus-inactivating effects against DENV-1 at 46.72%, DENV-2 at (66.48%), DENV-4(70.3%); Peptides 5FG at 100 μM showed inhibitions against DENV-1 during the post-infection stage at 35.96%, DENV-2(6.85%), DENV-4(81.19%)" No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM.(cell viability was found to range between 92.98 and 100% at 200 μM). No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 829.95 C36H63N9O13 CEFHKMNPQRTWY GV 3.8 0 1 -1 3 5 148.89 949 100 hour >20 hour >10 hour 162.22 0 0 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02013 LTLHWFRK 8 peptides 5G Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae "Antiviral assays(Cell protection assay, Direct virus inhibition assay, Post-infection assay, Viral attachment assay, Viral entry assay)" "[Ref.36739680]At 100 μM, peptides 5G demonstrated some cell protection effects against DENV-1 (25.24%), DENV-4(26.80%), DENV-2 (49.24%) and DENV-3(41.08%); Peptide 5G (100 μM) demonstrated a slight increase in inhibition of DENV-3 at 41.08% during pre-infection whereas peptide 5 at 200 μM only showed 37.41% inhibition against DENV-3; Peptides 5G (100 μM) also demonstrated direct virus-inactivating effects against DENV-1 at 48.23%, DENV-2 (56.25%), DENV-3(29.91%), DENV-4(72.27%); Peptides 5G at 100 μM showed inhibitions against DENV-1 during the post-infection stage at 24.59%, DENV-4(71.95%)" No hemolysis information or data found in the reference(s) presented in this entry [Ref.36739680]did not exhibit any significant cytotoxic effects towards Vero cells up to 200 μM.(cell viability was found to range between 92.98 and 100% at 200 μM). No predicted structure available Linear Acetylation Amidation None L Not found No machanism information found in the reference(s) presented in this entry 1100.33 C54H81N15O10 ACDEGIMNPQSVY L 11 3 0 3 1 4 -35 -1255 5.5 hour 3 min 2 min 97.5 5500 785.71 36739680 Virology. 2023 Mar;580:10-27. "Lee MF, Anasir MI, Poh CL. " Development of novel antiviral peptides against dengue serotypes 1-4.  10.1016/j.virol.2023.01.016 Anti-DENV DRAVPe02014 QLESLTDRELLLLIARKTCGSVE 23 E30pep-wt Synthetic construct Q05323 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Immunofluorescence [Ref.12912982]Ebola virus(EBOV): inhibition of the oligomerization of VP30(IC50= 1 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Amination Carboxylation None L Transcription "E30pep-wt seemed to bind efficiently to VP30 and consequently blocked the oligomerization of the protein. When E30pep-wt was transfected into EBOV-infected cells, the peptide inhibited viral replication suggesting that inhibition of VP30 oligomerization represents a target for EBOV antiviral drugs. " 2588.01 C111H195N31O37S FHMNPWY L 4.87 3 4 -1 6 9 8.7 -3951 0.8 hour 10 min >10 hour 135.65 0 0 12912982 J Biol Chem. 2003 Oct 24;278(43):41830-6. "Hartlieb B, Modrof J, Mühlberger E, Klenk HD, Becker S." Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide.  10.1074/jbc.M307036200 Anti-EBOV DRAVPe02015 GWKRIKQRIKDKLRNL 16 WL-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Plaque-forming assay [Ref.37342565]herpes simplex virus 1(HSV-1): WL-1 significantly inhibited the replication of HSV-1 on Vero cells(10 μM concentration with a 50% antiviral activity). No hemolysis information or data found in the reference(s) presented in this entry [Ref.37342565]WL-1 did not exert toxic effects on neuronal cell (U251) and epithelial cell (Vero) up to 50 μM concentration. No predicted structure available Linear Free Free None L virus replication "WL-1 may damage the viral membrane envelope or inhibit HSV-1 adsorption to cells, or perhaps participates in the regulation of the viral replication cycle and inflammatory response caused by viral infection." 2052.5 C92H162N32O21 ACEFHMPSTVY K 11.74 7 1 6 2 5 -151.88 -6491 30 hour >20 hour >10 hour 97.5 5500 366.67 37342565 Front Microbiol. 2023 Jun 5;14:1201505. "Guo X, An Y, Tan W, Ma L, Wang M, Li J, Li B, Hou W, Wu L." Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection.  10.3389/fmicb.2023.1201505. Anti-HSV-1 DRAVPe02055 Not reported 0 Salaciachinensis Natural Construct(isolated from digest of thai medicinal plants) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 0.25 µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13404 Anti-DENV DRAVPe02053 Not reported 0 Andrographispaniculata (Burm.f.) Wall.exNees Natural Construct(isolated from digest of thai medicinal plants) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 2.31 µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13402 Anti-DENV DRAVPe02054 Not reported 0 Sennagarrettiana (Craib) Irwin & Barneb Natural Construct(isolated from digest of thai medicinal plants) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 0.31 µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13403 Anti-DENV DRAVPe02052 Not reported 0 Diospyros Mollis Griff Natural Construct(isolated from digest of thai medicinal plants) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 2.4 µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13401 Anti-DENV DRAVPe02051 Not reported 0 Thunbergia laurifolia Lindl Natural Construct(isolated from digest of thai medicinal plants) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 1.54 µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13400 Anti-DENV DRAVPe02049 EDVLL 5 SLP9 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 12.8 ± 0.5 μg/ml [Ref:30973929] high hemolytic activity [Ref:30973929] CC50: 52.2 ± 2.0 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 587.67 C26H45N5O10 ADCHMSTWYOU L 3.67 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215236 Anti-PEDV DRAVPe02050 EVLDL 5 SLP10 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 10.6 ± 0.5 μg/ml [Ref:30973929] high hemolytic activity [Ref:30973929] CC50: 82.8 ± 3.4 μg/ml No predicted structure available Cyclic Heptaalkyl-biphenyl-acid- Amination Heptaalkyl-biphenyl-acid- L/D Membrane Inhibiting viral membrane fusion 587.67 C26H45N5O10 ARNCQGHIKMFPSTWYOU L 3.67 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215237 Anti-PEDV DRAVPe02047 EVLDL 5 SLP7 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 14.0 ± 0.6 μg/ml [Ref:30973929] high hemolytic activity [Ref:30973929] CC50: 274.1 ± 21.0 μg/ml No predicted structure available Linear palmitoylation Amination SLP7 is a version of SLP3 that contains only L-amino acids L Membrane Inhibiting viral membrane fusion 814 C26H45N5O10 ARNCQGHIKMFPSTWYOU L 3.36 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215234 Anti-PEDV DRAVPe02048 EVLLD 5 SLP8 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 2.6 ± 0.2 μg/ml "[Ref:30973929] SLP8 has a low hemolytic activity," [Ref:30973929] CC50: 217.5 ± 18.9 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 587.67 C26H45N5O10 ADCHMSTWYOU L 3.67 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215235 Anti-PEDV DRAVPe02046 KVLKL 5 SLP6 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 6.1 ± 0.3 μg/ml [Ref:30973929] high hemolytic activity [Ref:30973929] CC50: 12.6 ± 0.4 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 599.81 C29H57N7O6 ARNDCQEGHIMFPSTWYOU LK 10 0 2 -2 2 3 0.8 0.8133 1.3 hours 3 mins 3 mins 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215233 Anti-PEDV DRAVPe02045 EVLDL 5 SLP5 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929]PEDV:EC50 16.5 ± 0.6 μg/ml [Ref:30973929] hemolytic activity is reduced [Ref:30973929] CC50: 847.2 ± 124.9 μg/ml No predicted structure available Linear palmitoylation Carboxylation None L Membrane Inhibiting viral membrane fusion 587.67 C26H45N5O10 ARNCQGHIKMFPSTWYOU L 3.67 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215232 Anti-PEDV DRAVPe02043 EVLDL 5 SLP3 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 16.9 ± 1.6 μg/ml [Ref:30973929] hemolytic activity is reduced [Ref:30973929] CC50: 69.7 ± 2.6 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 587.67 C26H45N5O10 ARNCQGHIKMFPSTWYOU L 3.67 0 2 -2 2 3 0.96 0.8133 1 hour 30 mins >10 hours 214 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215230 Anti-PEDV DRAVPe02044 EVLL 4 SLP4 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 5.4 ± 0.4 μg/ml [Ref:30973929] high hemolytic activity [Ref:30973929] CC50: 12.9 ± 0.2 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 526.64 C22H46N4O10 ARNCQGHIKMFPSTWYOU EVL 4.25 0 1 -1 1 3 0.905 0.656 1.3 hours 3 mins 3 mins 10.7 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215231 Anti-PEDV DRAVPe02041 EVLADLV 7 SLP1 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV: EC50 8.0 ± 0.3 μg/ml [Ref:30973929] Low Hemolytic Activity [Ref:30973929] CC50: 52.6 ± 2.3 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 757.88 C34H59N7O12 RNCQGHIKMFPSTWWYOU LV 3.67 0 2 -2 2 5 1.543 0.7771 1 hour 30 mins >10 hours 208.57 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215228 Anti-PEDV DRAVPe02042 EVLDLV 6 SLP2 Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV; EC50 5.3 ± 0.5 μg/ml [Ref:30973929] Low Hemolytic Activity [Ref:30973929] CC50: 33.0 ± 1.6 μg/ml No predicted structure available Linear palmitoylation Amination None L Membrane Inhibiting viral membrane fusion 686.8 C31H54N6O11 ARNCQGHIKMFPSTWYOU LV 3.67 0 2 -2 2 4 1.5 0.7771 1 hour 30 mins >10 hours 226.67 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215229 Anti-PEDV DRAVPe02040 EVLADL 6 Surfactin Synthetic Construct(derived from Bacillus subtilis) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque reduction assay [Ref:30973929] PEDV; EC50 11.4 ± 0.7 μg/ml [Ref:30973929] Low Hemolytic Activity [Ref:30973929] CC50:45.9 ± 0.9 μg/ml No predicted structure available Linear palmitoylation Free None L Membrane surfactin exerts its antiviral effects by inhibiting viral membrane fusion. Membrane fusion between the viral envelope and the cell membrane is essential for enveloped viruses to invade host cells. Surfactin can act directly on virus particles by insertion into the viral envelopes’ lipid bilayer and thereby reduce the membrane fusion rate. 644.72 C28H48N6O11 RNCQGHIKMFPSTWWYOU V 3.67 0 2 -2 2 5 1.167 0.7771 1 hour 30 mins >10 hours 178.33 0 0 30973929 "PloS one, 14(4), e0215227." "Yuan, L., Zhang, S., Peng, J., Li, Y., & Yang, Q. (2019)." Synthetic surfactin analogues have improved anti-PEDV properties 10.1371/journal.pone.0215227 Anti-PEDV DRAVPe02039 KLTILNKDGILRSVILSFN 19 Scrambled-2 Synthetic Construct (AVP-p scrambled form) No entry found Experimentally Validated None GPC Not Available Not available Not Available Not Available Not Available Not Available None JUNV Arenaviridae Plaque Reduction Assays [Ref.24850726]JUNV:demonstrated some inhibitory activity. No hemolysis information or data found in the reference(s) presented in this entry [Ref.24850726]no acute cytotoxicity No predicted structure available Cyclic Free Free None L Membrane "Fusion inhibitor, deployment of fusion machinery by the peptide could render virions less able to engage in on-pathway receptor binding or endosomal fusion" 2144.59 C98H170N26O27 ACQEHMPWYOU IL 9.99 3 1 2 6 9 0.537 -1499 5.5 hours 3 min 2 min 158.95 0 0 24850726 "Journal of virology, 88(15), 8556–8564." "Spence, J. S., Melnik, L. I., Badani, H., Wimley, W. C., & Garry, R. F. (2014)." Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism 10.1128/JVI.01133-14 Anti-JUNV DRAVPe02035 VNKKIEEIDKKIEELNKKLEELEKKLEEVNKK 32 NOVEL-2 Synthetic Construct No entry found Experimentally Validated None "HR1, HR2" AAS00690##AAK27168 Not available Not Available Not Available Not Available Not Available None " NDV, IBV" Paramyxoviridae Fusion Assay "[Ref. 21601229]NDV : Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 25 μM).##IBV:Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 26 μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein Entry inhibition 3909.58 C173H303N45O56 ARCQMFPSTUOYW EK 6.45 10 10 0 -1.481 100 hours >20 hours >10 hours 103.44 0 0 21601229 "Virology, 416(1-2), 65–74." "Wang, X. J., Li, C. G., Chi, X. J., & Wang, M. (2011)." Characterisation and evaluation of antiviral recombinant peptides based on the heptad repeat regions of NDV and IBV fusion glycoproteins 10.1016/j.virol.2011.05.001 "Anti-NDU,Anti-IBV" DRAVPe02036 TLTTKLY 7 TLTTKLY Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not available Not Available Not Available Not Available Not Available None " NDV, IBV" Paramyxoviridae competition assay [Ref. 12021868]NDV: Inhibition of hemolytic activity and viral propagation in embryonated chicken eggs. Inhibition of phage binding with the same sequence. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein Entry inhibition 839 C39H66N8O12 ARNDCQEGHIMFPSWVOu LT 8.26 1 0 1 2 5 0.043 7.2 hours >20 hours >10 hours 111.43 1490 1.776  12021868##16377031 "Archives of virology, 147(5), 981–993;## Peptides, 27(6), 1217–1225." "Ramanujam, P., Tan, W. S., Nathan, S., & Yusoff, K. (2002);##Chia, S. L., Tan, W. S., Shaari, K., Abdul Rahman, N., Yusoff, K., & Satyanarayanajois, S. D. (2006)." Novel peptides that inhibit the propagation of Newcastle disease virus;##Structural analysis of peptides that interact with Newcastle disease virus  10.1007/s00705-001-0778-y;##10.1016/j.peptides.2005.11.018 Anti-NDU DRAVPe02037 CTLTTKLYC 9 CTLTTKLYC Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not available Not Available Not Available Not Available Not Available None " NDV, IBV" Paramyxoviridae competition assay [Ref. 12021868]NDV: Inhibition of hemolytic activity and viral propagation in embryonated chicken eggs. Inhibition of phage binding with the same sequence. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein Entry inhibition 1045.28 C45H76N10O14S2 ARNDQEGHIMFPWVOU CLT 8.05 1 0 1 0.589 1.2 hours >20 hours >10 hours 86.67 1490 1.425  12021868##16377031 "Archives of virology, 147(5), 981–993;## Peptides, 27(6), 1217–1225." "Ramanujam, P., Tan, W. S., Nathan, S., & Yusoff, K. (2002);##Chia, S. L., Tan, W. S., Shaari, K., Abdul Rahman, N., Yusoff, K., & Satyanarayanajois, S. D. (2006)." Novel peptides that inhibit the propagation of Newcastle disease virus;##Structural analysis of peptides that interact with Newcastle disease virus  10.1007/s00705-001-0778-y;##10.1016/j.peptides.2005.11.018 Anti-NDU DRAVPe02034 NASDMEIKKVNKKIEEYIKKIEEVEKKLEEVNKK 34 NOVEL-1 Synthetic Construct No entry found Experimentally Validated None "HR1, HR2" AAS00690##AAK27168 Not available Not Available Not Available Not Available Not Available None " NDV, IBV" Paramyxoviridae Fusion Assay "[Ref. 21601229]NDV:Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 25 μM).##IBV:Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 25μM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Spike Protein "Entry inhibition, The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections. The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections." 4105.8 C181H311N47O58S1 RCQGHFPTWOU EK 8.19 10 9 1 0.2941 -1.324 2.9788 1.4 hours 3 min >10 hours 85.88 1490 0.363 21601229 "Virology, 416(1-2), 65–74." "Wang, X. J., Li, C. G., Chi, X. J., & Wang, M. (2011)." Characterisation and evaluation of antiviral recombinant peptides based on the heptad repeat regions of NDV and IBV fusion glycoproteins 10.1016/j.virol.2011.05.001 "Anti-NDU,Anti-IBV" DRAVPe02032 YKYRYL 6 BD-11b S protein of SARS-CoV No entry found Experimentally Validated None S1 Protein Not Available Y438-L443 Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Cell-cell fusion "[Ref.22265858]SARS-CoV:14 mM (IC90) Vero Ex cells, 7 mM (IC90) CaCo2 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Block attachment to the host cells 905.06 C45H64N10O10 ANDCQEGHIMFPSTWVOU Y 9.53 2 0 2 -1.417 2.8 hours 10 min 2 min 65 4470 4.939 22265858 "Antiviral research, 94(3), 288–296." "Struck, A. W., Axmann, M., Pfefferle, S., Drosten, C., & Meyer, B. (2012)" A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2 10.1016/j.antiviral.2011.12.012 Anti-SARS-Cov DRAVPe02033 WNFFDWFSGLMSWFGGPLK 19 RVFV-6 Synthetic Construct P03518 Experimentally Validated 11588 GP P03518 450-468 pfam19019 M11157 Genomic RNA Not Available 4HJ1 "RVFV, Ebola virus" Nil Not Available Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not Found Fusion inhibitor 2322.67 C117H148N24O25S1 ARCQEHITYVOU GFW 5.84 1 1 0 0 0.142 2.8 hours 3 min 2 min 41.05 16500 7.104 24069485 "PLoS neglected tropical diseases, 7(9), e2430. " "Koehler, J. W., Smith, J. M., Ripoll, D. R., Spik, K. W., Taylor, S. L., Badger, C. V., Grant, R. J., Ogg, M. M., Wallqvist, A., Guttieri, M. C., Garry, R. F., & Schmaljohn, C. S. (2013)." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 "Anti-RVFV,Anti-Ebola virus,Anti-Andes virus,Anti-vesicular stomatitis virus" DRAVPe02031 LEAIPCSIPPEFLFGKPFVFLEAIPCSIPPEFLFGKPFVF 40 VIR-576 Synthetic Construct No entry found Experimentally Validated None E2 Protein Not Available 29 -72  cd02056##cd02056 Not Available Not Available Not Available 2L6S## 2L6T HIV-1 Retroviridae inhibition assay  Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein Not Available 4485.41 C224H324N42O51S2 RNDQHMTWYOU EILFP 4.49 2 4 -2 0.89 5.5 hours 3 min 2 min 97.5 125 0.028 21543477##17448989##21178138 "Journal of virology, 85(14), 7037–7047## Cell, 129(2), 263–275 ## Science translational medicine, 2(63), 63re3." "Koedel, Y., Eissmann, K., Wend, H., Fleckenstein, B., & Reil, H. (2011)## Münch, J., Ständker, L., Adermann, K., Schulz, A., Schindler, M., Chinnadurai, R., Pöhlmann, S., Chaipan, C., Biet, T., Peters, T., Meyer, B.,## Wilhelm, D., Lu, H., Jing, W., Jiang, S., Forssmann, W. G., & Kirchhoff, F.## Forssmann, W. G., The, Y. H., Stoll, M., Adermann, K., Albrecht, U., Tillmann, H. C., Barlos, K., Busmann, A., Canales-Mayordomo, A., Giménez-Gallego, G., Hirsch, J., Jiménez-Barbero, J., Meyer-Olson, D" Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition## Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide##Short-term monotherapy in HIV-infected patients with a virus entry inhibitor against the gp41 fusion peptide. 10.1128/JVI.02366-10##10.1016/j.cell.2007.02.042##10.1126/scitranslmed.3001697 Anti-HIV-1 DRAVPe02030 CANLLLQYGSFCTQLNRALSGIA 23 P9 synthetic Construct (Derived from SARS-CoV: 694009)) P59594 Experimentally Validated 694009  "S2 (918758), " AY278741.1 731-753 pfam01601##cd22378 AY278741 Genomic RNA N/A 7SG4 SARS-CoV Coronaviridae Syncytia inhibition assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Spike Protein P9 themselves can markedly inhibit syncytia formation 2456.86 C107H174N30O32S2 DEHKMPVW ALCGNQS 6.72 1 0 1 0.6 1.2 hours >20 hours >10 hours 114.78 1490 0.606 15811330 Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential "Lu, W., Wu, X. D., Shi, M. D., Yang, R. F., He, Y. Y., Bian, C., Shi, T. L., Yang, S., Zhu, X. L., Jiang, W. H., Li, Y. X., Yan, L. C., Ji, Y. Y., Lin, Y., Lin, G. M., Tian, L., Wang, J., Wang, H. X., Xie, Y. H., Pei, G., … Sun, B. (2005)." "FEBS letters, 579(10), 2130–2136." 10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02038 RTILLFIGVKDLLKNSNSI 19 Scrambled-1 Synthetic Construct (AVP-p scrambled form) No entry found Experimentally Validated None GPC Not Available Not available Not Available Not Available Not Available Not Available None JUNV Arenaviridae Plaque Reduction Assays [Ref.24850726]JUNV:demonstrated some inhibitory activity No hemolysis information or data found in the reference(s) presented in this entry [Ref.24850726]no acute cytotoxicity No predicted structure available Cyclic Free Free None L Membrane "Fusion inhibitor, deployment of fusion machinery by the peptide could render virions less able to engage in on-pathway receptor binding or endosomal fusion" 2144.59 C98H170N26O27 ACQEHMPWYOU IL 9.99 3 1 2 6 9 0.537 -1499 5.5 hours 3 min 2 min 158.95 0 0 24850726 "Journal of virology, 88(15), 8556–8564." "Spence, J. S., Melnik, L. I., Badani, H., Wimley, W. C., & Garry, R. F. (2014)." Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism 10.1128/JVI.01133-14 Anti-JUNV DRAVPe02029 RNTREVFAQVKQMYKTPTLKYFG 23 P10 synthetic Construct (Derived from SARS-CoV: 694009) P59594 Experimentally Validated 694009  "S2 (918758), " AY278741.1 amino acid residues fragments (758–780) cd22378 AY278741 Genomic RNA N/A 5XJK SARS-CoV Coronaviridae Syncytia inhibition assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein "P10 antisera had specific binding to the S fragments and S protein expressed in E. coli and SARS‐CoV infected cell lysates, suggesting that those Abs have a potential to recognize S protein of SARS‐CoV in its natural form" 2806.6 C128H201N35O34S1 CDHISW KTEQRY 10.58 5 1 4 -0.865 1 hours 2 min 2 min 46.52 2980 1.06 15811330 "Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential. FEBS letters, 579(10), 2130–2136. https://doi.org/10.1016/j.febslet.2005.02.070" "Xia, S., Liu, M., Wang, C., Xu, W., Lan, Q., Feng, S., Qi, F., Bao, L., Du, L., Liu, S., Qin, C., Sun, F., Shi, Z., Zhu, Y., Jiang, S., & Lu, L. (2020)" Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential 10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02028 PSSKRFQPFQQFGRDVSDFTDSVRDPKTSE 30 PL8 Synthetic construct U5WLK5##P59594 Experimentally Validated 694009  S2 (918758) KC881005 N/A cd22378 KC881005 Genomic RNA N/A 8WLY##5WRG## 5XLR## 6M3W SARS-CoV Coronaviridae Syncytia inhibition assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein "P8 antisera had specific binding to the S fragments and S protein expressed in E. coli and SARS‐CoV infected cell lysates, suggesting that those Abs have a potential to recognize S protein of SARS‐CoV in its natural form" 3489.76 C152H230N44O51 ACHILMNWY DFSPQR 6.1 5 5 0 0 -1.343 >20 hours >20 hours 19.33 0 0 15811330 "FEBS letters, 579(10), 2130–2136. " "Xia, S., Liu, M., Wang, C., Xu, W., Lan, Q., Feng, S., Qi, F., Bao, L., Du, L., Liu, S., Qin, C., Sun, F., Shi, Z., Zhu, Y., Jiang, S., & Lu, L. (2020)" Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential 10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02026 ARLPRTMV 8 Pal M1 Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None IAV(H5N1) Orthomyxoviridae Not Available No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available micelle C16 Free None L HA Not Available 1181 C40H74N14O10S1 NDCQEGHIKFSWYOU RALPPTV 12 2 0 2 7 7 0.05 1.1429 "4.4 hours (mammalian reticulocytes, in vitro)" >20 hours >10 hours 97.5 0 0 23777281 "BMC biotechnology, 13, 51." "Hüttl, C., Hettrich, C., Miller, R., Paulke, B. R., Henklein, P., Rawel, H., & Bier, F. F. (2013)" Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity 10.1186/1472-6750-13-51 Anti-IAV(H5N1) DRAVPe02027 ARLPR 5 Pal S1 Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None IAV(H5N1) Orthomyxoviridae Not Available No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available micelle C16 Free None L HA Not Available 849 C26H49N11O6 NDCQEGHIKMFPSTWYVOU ARLP 12 2 0 2 5 5 -1 1.12 "4.4 hours (mammalian reticulocytes, in vitro)" >20 hours >10 hours 98 0 0 23777281 "BMC biotechnology, 13, 51." "Hüttl, C., Hettrich, C., Miller, R., Paulke, B. R., Henklein, P., Rawel, H., & Bier, F. F. (2013)" Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity 10.1186/1472-6750-13-51 Anti-IAV(H5N1) DRAVPe02025 ARLPRTMVHPKPAQP 15 C18-s2 Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not available None Influenza virus Orthomyxoviridae Not Available [Ref:20476787]C17H35CO-ARLPRTMV-NH2:Inhibition of influenza A/H1N1/Puerto Rico/8/34 virus (IC50=3.0 and 1.9 μM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear C17H35CO Amidation None L Membrane Not Available 1699.05 C75H127N25O18S1 NDCEGIFSWYOU ARP 12 3 0 3 6 9 -0.88 1.2143 "4.4 hours (mammalian reticulocytes, in vitro)" >20 hours >10 hours 58.67 0 0 36232735##20476787 "International journal of molecular sciences, 23(19), 11433##Journal of medicinal chemistry, 53(11), 4441–4449" "Agamennone, M., Fantacuzzi, M., Vivenzio, G., Scala, M. C., Campiglia, P., Superti, F., & Sala, M. (2022)##Matsubara, T., Onishi, A., Saito, T., Shimada, A., Inoue, H., Taki, T., Nagata, K., Okahata, Y., & Sato, T. (2010)." Antiviral Peptides as Anti-Influenza Agents##Sialic acid-mimic peptides as hemagglutinin inhibitors for anti-influenza therapy 10.3390/ijms231911433##10.1021/jm1002183 Anti-IAV DRAVPe02023 ISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE 38 CRAMP-2 Natural Construct (obtained from Mouse cathelicidin) P51437 Experimentally Validated 10090 CAMP(12796) U43409.1 135-172 pfam12153 CM001002.3 mRNA "Chromosome 9,(125-172)" None EV71 Picornaviridae Hemagglutination inhibition assay [Ref:33508330]CRAMP:Reduction of intracellular EV71 RNA copy numbers by 95.7% and 97.6%. No hemolysis information or data found in the reference(s) presented in this entry [Ref:33508330]CRAMP:No cytotoxicity against U251 cells. No predicted structure available Linear Free Free None L Membrane "CRAMP significantly inhibited EV71 replication, suggesting that CRAMP possibly enhanced the antiviral immune response of host cells.CRAMP did not directly inactivate EV71 virons, but effectively regulated IFN-β and IL-6 response and markedly inhibited viral binding. " 4291.2 C197H338N56O50 DCHMTWYOU K 10.46 10 3 7 18 12 -0.582 1.59 20 hours 30 mins >10 hours 102.63 0 0 33508330 "Antiviral research, 187, 105021." "Yu, J., Dai, Y., Fu, Y., Wang, K., Yang, Y., Li, M., Xu, W., & Wei, L. (2021)" Cathelicidin antimicrobial peptides suppress EV71 infection via regulating antiviral response and inhibiting viral binding 10.1016/j.antiviral.2021.105021 Anti-EV71 DRAVPe02024 NDFRSKT 7 L-P1 Synthetic Construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Influenza virus,AIV(H9N2)" Orthomyxoviridae Hemagglutination inhibition assay [Ref:19680476]Peptide P1:Inhibition of early-stage viral infection independent of virus entry.[Ref:19497129]AIV(H9N2):IC50=100 μM. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Prevent the viral replication by inhibiting the attachment or entry of the virus into the target cells 866.93 C36H58N12O13 ACQEGHILMPWYVOU RNDKFST 8.75 2 1 1 7 0 -2.014 1.3714 1.4 hours 3 min >10 hours 0 0 0 19680476##19497129 " International journal of biological sciences, 5(6), 543–548##Virology journal, 6, 74." "Rajik, M., Omar, A. R., Ideris, A., Hassan, S. S., & Yusoff, K. (2009)##Rajik, M., Jahanshiri, F., Omar, A. R., Ideris, A., Hassan, S. S., & Yusoff, K. (2009)." A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells##Identification and characterisation of a novel anti-viral peptide against avian influenza virus H9N2 10.7150/ijbs.5.543## 10.1186/1743-422X-6-74 "Anti-IAV,Anti-AIV(H9N2)" DRAVPe02022 GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE 33 CRAMP-1 Mus musculus(Mouse) P51437 Experimentally Validated 10090 CAMP(12796) U43409.1 135-172 pfam12153 CM001002.3 mRNA "Chromosome 9,(125-172)" None "HRV,AV" Picornaviridae Not Available No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Available Not Available 3750.53 C173H294N48O44 ADCHMSTWYOU K 10.22 9 3 6 16 12 -0.815 1.0286 30 hours >20 hours >10 hours 91.52 0 0 16020269##33508330 "Current eye research, 30(5), 385–394##Antiviral research, 187, 105021." "Gordon, Y. J., Huang, L. C., Romanowski, E. G., Yates, K. A., Proske, R. J., & McDermott, A. M. (2005)##Yu, J., Dai, Y., Fu, Y., Wang, K., Yang, Y., Li, M., Xu, W., & Wei, L. (2021)" "Human Cathelicidin (LL-37), a Multifunctional Peptide, is Expressed by Ocular Surface Epithelia and has Potent Antibacterial and Antiviral Activity##Cathelicidin antimicrobial peptides suppress EV71 infection via regulating antiviral response and inhibiting viral binding" 10.1080/02713680590934111##10.1016/j.antiviral.2021.105021 "Anti-HRV,Anti-AV" DRAVPe02021 LVLQTM 6 LVLQTM Derived from the very C terminus of the RBM6Δ6 protein No entry found Experimentally Validated None RBM6Δ6 protein Not Available Not Available Not Available Not Available Not Available Not Available None "HRVs,EV-71" Picornaviridae Not Available [Ref:22072773]LVLQTM peptide:Effective substrate analogue of EV-71 2A(pro) (Kd=9.6 μM);Inhibition of eIF4G cleavage activity of 2A(pro);Inhibition of EV-71 replication in HeLa cells. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Available "peptide inhibited the activity of protease 2 A, which plays several essential roles during viral replication, by coupling in the active site of this enzyme. The in vitro assay with A549 cells and the in vivo assay with mice demonstrated viral replication inhibition" 703.9 C31H57N7O9S1 ARNDCEGHIKFPSWYOU L 5.52 0 0 0 2 4 1.583 0.8067 5.5 hours 3 mins 2 mins 178.33 0 0 22072773##22865380 "Journal of virology, 86(2), 691–704;##The Journal of antimicrobial chemotherapy, 67(12), 2865–2869." "Falah, N., Violot, S., Décimo, D., Berri, F., Foucault-Grunenwald, M. L., Ohlmann, T., Schuffenecker, I., Morfin, F., Lina, B., Riteau, B., & Cortay, J. C. (2012);##Falah, N., Montserret, R., Lelogeais, V., Schuffenecker, I., Lina, B., Cortay, J. C., & Violot, S. (2012)." Ex Vivo and In Vivo Inhibition of Human Rhinovirus Replication by a New Pseudosubstrate of Viral 2A Protease;##Blocking human enterovirus 71 replication by targeting viral 2A protease  10.1128/JVI.05263-11;## 10.1093/jac/dks304 "Anti-HRVs,Anti-EV-71" DRAVPe02019 KREHGQHCEF 10 SU2 Purified from R. paludosa extract No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1(RT) Retroviridae Plaque reduction assay [Ref:17113195]HIV-1:IC50=11µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Available Not Available 1270.39 C53H79N19O16S1 ANDILPSTWVYOU EH 6.92 2 2 0 7 2 -2.04 0.924 1.3 hours 3 mins 3 mins 0 0 0 17113195 "Peptides, 28(3), 560–565." "Wang, J., Wang, H. X., & Ng, T. B. (2007)." A peptide with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Russula paludosa 10.1016/j.peptides.2006.10.004 Anti-HIV-1(RT) DRAVPe02020 IPLRGAFINGRWDSQCHRFSNGAIACA 27 Urumin Skin of the South Indian frog(Hydrophylax bahuvistara) P0DTB9 Experimentally Validated 1690667 Not Available Not Available 1 to 27 P0DTB9.1 Not Available Not Available Not Available None H1N1 Orthomyxoviridae Not Available [Ref:28423338]IC50=11.25 µg/mL²;IC50 of urumin=3.8 µM. No hemolysis information or data found in the reference(s) presented in this entry "[Ref:28423338]Urumin:TD50=2,450 μM;Therapeutic index (TI)=TD50/IC50=644.7, indicating a favorable therapeutic profile." No predicted structure available Linear Free Free None L Stalk region of H1 "Amphibian peptide that shows viricidal activity against human H1N1 influenza A virus. It specifically targets the conserved stalk region of H1 hemagglutinin, and acts by actively destroying influenza virions. It shows a reduced activity on human H3N2 influenza A virus and no activity against other viruses (HIV, SIV, HSV-II, hepatitis C, Ebola, Zika, and Dengue viruses). In vivo, the peptide also protects mice infected with mouse-adapted influenza virus from lethal influenza infection. The peptide synthesized in D-amino acids is inactive." 2961.39 C129H201N40O35S2 EKMTYVOU A 9.02 3 1 2 14 10 -0.033 1.2512 20 hours 30 mins >10 hours 72.59 5500 1.857 28423338 "Immunity, 46(4), 587–595" "Holthausen, D. J., Lee, S. H., Kumar, V. T., Bouvier, N. M., Krammer, F., Ellebedy, A. H., Wrammert, J., Lowen, A. C., George, S., Pillai, M. R., & Jacob, J. (2017)" An Amphibian Host Defense Peptide Is Virucidal for Human H1 Hemagglutinin-Bearing Influenza Viruses 10.1016/j.immuni.2017.03.018 DRAVPa0001 Anti-H1N1 DRAVPe02018 EGVKSKLNIVCNEIGLLKSLCRKFVNSHIW 30 Nk-lysin Synthetic Construct A0A1P8CXN4 Experimentally Validated 52904  SMAX5B_000299 KU705506.1 Nkl71-100 APD51552.1 KU705506 mRNA Not available None SVCV Rhabdoviridae MTT cell-viability assay [Ref:30717094]SVCV:IC50= 24.69 µg/mL² No hemolysis information or data found in the reference(s) presented in this entry [Ref:30717094]No significant toxic effect at concentrations <32 μM (84.5 ± 1.9% viability);Severe viability drop at higher concentrations. No predicted structure available Linear Free Free None L Membrane "Nkl71-100exerts strong antiviral activity against spring viremia of carp virus (SVCV) by inhibiting not only the binding of viral particles to host cells, but also the fusion of virus and cell membranes, which requires a low pH context. Such antiviral activity seems to be related to the important role that PS plays in these steps of the replication cycle of SVCV, a feature that is shared by other families of virus-comprising members with health and veterinary relevance. Consequently, Nkl71⁻100 is shown as a promising broad-spectrum antiviral candidate. it was observed that Nkl71–100 alters the binding ability of SVCV to cell membranes since virus-cell binding levels significantly decreased in the presence of peptide in comparison to what it is observed in its absence." 3429.1 C154H255N43O41S2 ADQMTOU LK 9.31 5 2 3 6 5 0.14 2.3 1 hours 30 min >10 hours 120 5625 1.64 30717094 "Marine drugs, 17(2), 87." "Falco, A., Medina-Gali, R. M., Poveda, J. A., Bello-Perez, M., Novoa, B., & Encinar, J. A. (2019)." Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion 10.3390/md17020087 Anti-SVCV DRAVPe02016 SPATAFTVYVFCFLL 15 E5-type 18 Synthetic Construct No entry found In silico None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae Not included yet No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not inlcuded yet Not Available "E5-type 18 (SPATAFTVYVFCFLL) and E7-type 45 (TLQEIVLHLEPQNELDPVDLL) peptides presented the best results for inducing the production of IFN-γ, an essential cytokine in intracellular immunity against HPV infection." 1679.01 C83H119N15O20S1 RNDQEGHIKMWOU F 5.24 0 0 0 3 10 1.693 1.69 1.9 hours >20 hours >10 hours 84.44 1740 0.887 31915962##35853393 "Biotechnology letters, 42(3), 403–418.;##Colloids and surfaces. B, Biointerfaces, 217, 112693." "Namvar, A., Panahi, H. A., Agi, E., & Bolhassani, A. (2020);##Freitas, E. D., Bataglioli, R. A., Oshodi, J., & Beppu, M. M. (2022)." "Development of HPV16,18,31,45 E5 and E7 peptides-based vaccines predicted by immunoinformatics tools;##Antimicrobial peptides and their potential application in antiviral coating agents" 10.1007/s10529-020-02792-6;## 10.1016/j.colsurfb.2022.112693 Anti-HPV DRAVPe02017 TLQEIVLHLEPQNELDPVDLL 21 E7-type 45 Synthetic Construct No entry found In silico None Not Available Not Available Not Available Not Available Not Available Not Available Not available None HPV Papillomaviridae Not included yet No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available "E5-type 18 (SPATAFTVYVFCFLL) and E7-type 45 (TLQEIVLHLEPQNELDPVDLL) peptides presented the best results for inducing the production of IFN-γ, an essential cytokine in intracellular immunity against HPV infection." 2428.76 C109H178N26O36 ARCGKMSTYOU L 3.83 0 5 -5 10 12 0.029 1.02 7.2 hours >20 hours >10 hours 157.62 0 0 31915962##35853393 "Biotechnology letters, 42(3), 403–418.;##Colloids and surfaces. B, Biointerfaces, 217, 112693." "Namvar, A., Panahi, H. A., Agi, E., & Bolhassani, A. (2020);##Freitas, E. D., Bataglioli, R. A., Oshodi, J., & Beppu, M. M. (2022)." "Development of HPV16,18,31,45 E5 and E7 peptides-based vaccines predicted by immunoinformatics tools;##Antimicrobial peptides and their potential application in antiviral coating agents" 10.1007/s10529-020-02792-6;## 10.1016/j.colsurfb.2022.112693 Anti-HPV DRAVPe02056 DHVTPDIAYNPRTMY 15 Peptide-1 Acacia catechu extract No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available 1792.98 C79H117N21O25S1 CQEGLKFWOU DPTY 5.21 2 1 -1 14 11 -0.867 1.0171 1.1 hours 3 mins >10 hours 52 2980 1.662 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13405 Anti-DENV DRAVPe02057 DHVTPDIAYNPRTYM 15 Peptide-2 Acacia catechu extract No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available 1792.98 C79H117N21O25S2 CQEGLKFWOU DPTY 5.21 2 1 -1 14 11 -0.867 1.0171 1.1 hours 4 mins >10 hours 52 2980 1.662 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13406 Anti-DENV DRAVPe02058 DHVTPDIAYNPWAFY 15 Peptide-3 Acacia catechu extract No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available 1808.97 C87H113N19O24 RCQEGLKMSOU ADPY 4.2 0 2 -2 14 11 -0.4 0.9743 1.1 hours 3 mins >10 hours 58.67 8480 4.688 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13407 Anti-DENV DRAVPe02059 DHVTPDIAYNPWAYF 15 Peptide-4 Acacia catechu extract No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay No activity information or data found in the reference(s) presented in this entry No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available 1808.97 C87H113N19O24 RCQEGLKMSOU ADPY 4.2 1 2 -2 14 11 -0.4 0.9743 1.1 hours 3 mins >10 hours 58.67 8480 4.688 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019). " Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13408 Anti-DENV DRAVPe02060 Not reported 0 Acacia catechu extract Natural Construct((isolated from digest of thai medicinal plants) ) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV Flaviviridae Foci-forming unit (FFU) assay [Ref:30225997] DENV:IC50 values of 0.18 µg/mL No hemolysis information or data found in the reference(s) presented in this entry [Ref:30225997]No toxicity was observed at the peptide concentration between 0.01 µM and 1mM. No predicted structure available Not included yet Not included yet Not included yet Not included yet Not included yet Not Available Not Available Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 30225997 "Chemical biology & drug design, 93(2), 100–109." "Panya, A., Yongpitakwattana, P., Budchart, P., Sawasdee, N., Krobthong, S., Paemanee, A., Roytrakul, S., Rattanabunyong, S., Choowongkomon, K., & Yenchitsomanus, P. T. (2019)." Novel bioactive peptides demonstrating anti-dengue virus activity isolated from the Asian medicinal plant Acacia Catechu 10.1111/cbdd.13400 Anti-DENV DRAVPe02061 CDIPIGAGICAS 12 SP-10-1  Synthetic Construct(derived from SARS-CoV S protein) P26436##P59594 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.1 648–659 Not Available CM000673.2##AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae ELISA [Ref:16337697] SARS-CoV IC50= >20µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L ACE2 Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. 1119.32 C46H78N12O16S2 RNQEHLKMFTWYVOU I 3.8 0 1 -1 9 9 1.283 0.5877 1.2 hours >20 hours >10 hours 114.17 0 0 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)" Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.002 Anti-SARS-CoV DRAVPe02062 YHTVSLLRSTSQ 12 SP-10-2 Synthetic Construct(derived from SARS-CoV S protein) P26436##P59594 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.2 660–671 Not Available CM000673.2##AY274119.4 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV8 SARS-CoV Coronaviridae ELISA [Ref:16337697] SARS-CoV IC50=6.21 ± 2.13µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L ACE2 Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. 1391.55 C60H98N18O20 ANDCEGIKMFPWOU S 8.75 1 0 1 11 11 -0.375 0.8833 2.8 hours 10 min 2 min 89.17 1490 1.071 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)" Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.003 Anti-SARS-CoV DRAVPe02063 SLLRSTSQKSIV 12 SP-10-3  Synthetic Construct(derived from SARS-CoV S protein) P26436##P59594 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.3 664–675 Not Available CM000673.2##AY274119.5 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV9 SARS-CoV Coronaviridae ELISA [Ref:16337697] SARS-CoV IC50=5.47 ± 0.41µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L ACE2 Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. 1318.54 C56H103N17O19 ANDCEGHMFPWYOU S 11 2 0 2 12 12 0.042 0.97 1.9 hours >20 hours >10 hours 121.67 0 0 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)" Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.004 Anti-SARS-CoV DRAVPe02064 KSIVAYTMSLGA 12 SP-10-4  Synthetic Construct(derived from SARS-CoV S protein) P26436##P59594 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.5 672–683 Not Available CM000673.2##AY274119.7 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV11 SARS-CoV Coronaviridae ELISA [Ref:16337697] SARS-CoV IC50=2.07 ± 1.01µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L ACE2 Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. 1240.48 C55H93N13O17S1 RNDCQEHFPWOU AS 8.59 1 0 1 12 12 0.842 0.8667 1.3 hours 3 min 3 mins 105.83 1490 1.201 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)" Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.006 Anti-SARS-CoV DRAVPe02065 AYTMSLGADSSI 12 SP-10-5 Synthetic Construct(derived from SARS-CoV S protein) P26436##P59594 Experimentally Validated 694009 S2(MAX5B_000299) AY278741.6 676–687 Not Available CM000673.2##AY274119.8 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV12 SARS-CoV Coronaviridae ELISA [Ref:16337697] SARS-CoV IC50=>20µg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L ACE2 Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. 1215.34 C51H82N12O20S1 RNCQEHKFPWVOU S 3.8 0 1 -1 12 12 0.458 0.8667 4.4 hours >20 hours >10 hours 81.67 1490 1.226 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)" Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.007 Anti-SARS-CoV DRAVPe02125 GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK 45 "Human beta defensin 3" "Skin, tonsils, oral/saliva, colonic mucosa, H. sapiens" P81534 Experimentally validated 9606 DEFB103A; DEFB103B Not Available 23-67 CAC03097.1 CM000670.2 mRNA "Chromosome 8: 7,881,392-7,882,663 forward strand." 1KJ6 HIV-1 Retroviridae Not Available "[Ref:16672548]HIV: hBD-3 inhibited infection, greater activity against X4 strains" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found " Both hBD-2 and hBD-3 inhibit R5 and X4 types of HIV-1 infection in a dose-dependent manner (Sun et al. 2005 J Virol 79: 14318-29). Its anti-HIV-1 effect may be due to a direct inactivation of cell-free virions and inhibition viral replication after cDNA formation。 (1) HIV-1 X4 and R5 phenotypes induce hBD-2 and -3 mRNA in normal human oral epithelial cells; (2) hBD-2 and -3 inhibit HIV-1 infection by both viral strains, with greater activity against X4 viruses; and (3) this inhibition is due to a direct interaction with virions and through modulation of the CXCR4 co-receptor" 5161.2 C216H377N75O59S6 DHMFOU R 10.08 13 2 11 32 24 -0.7 2.87 30 hours >20 hours >10 hours 67.11 2980 0.577 16672548 Advances in Dental Research. 2006;19(1):42-48. "Weinberg A, Quiñones-Mateu ME, Lederman MM. " Role of Human β-defensins in HIV Infection 10.1177/154407370601900109 Anti-HIV DRAVPe02124 GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP 41 "Human beta defensin 2" Homo sapiens (Human) "O15263,Q52LC0" Experimentally validated 9606 DEB4A CAA95992.1 24-64 Z71389.1 CM000670.2 mRNA "Chromosome 8: 7,414,855-7,416,863" "1FD4,1FD3 resolved by X-ray. 1FQQ resolved by NMR." HIV-1 Retroviridae Not given "[Ref:16672548]HIV: hBD-2 and hBD-3 inhibited infection, greater activity against X4 strains" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free " The 3 disulfide bonds are between residues 8-37, 15-30, and 20-38. The structure (one N-terminal helix and 3 beta strands) was found to be monomer in solution" L Not Available " Both hBD-2 and hBD-3 inhibit R5 and X4 types of HIV-1 infection in a dose-dependent manner (Sun et al. 2005 J Virol 79: 14318-29). Its anti-HIV-1 effect may be due to a direct inactivation of cell-free virions and inhibition viral replication after cDNA formation。 (1) HIV-1 X4 and R5 phenotypes induce hBD-2 and -3 mRNA in normal human oral epithelial cells; (2) hBD-2 and -3 inhibit HIV-1 infection by both viral strains, with greater activity against X4 viruses; and (3) this inhibition is due to a direct interaction with virions and through modulation of the CXCR4 co-receptor" 4334.24 C188H311N55O50S6 EMNW CG 9.3 8 1 7 17 9 -0.102 0.9 30 hours >20 hours >10 hours 64.15 1490 0.344 16672548 Advances in Dental Research. 2006;19(1):42-48. "Weinberg A, Quiñones-Mateu ME, Lederman MM. " Role of Human β-defensins in HIV Infection 10.1177/154407370601900109 anti-HIV DRAVPe02123 DHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK 36 "Human beta defensin 1" "Airway, hemofiltrates, urine, kidney; keratinocytes; skin; platelets; oral saliva; milk, mammary gland epithelium, colonic mucosa, H. sapiens" P60022 Experimentally validated 9606 DEFB1 AAC51728.1 33-68 AH006699.2 CM000670.2 Genomic DNA "Chromosome 8: 6,870,592-6,877,936 " 1E4S##1IJU IAV(H1N1) Orthomyxoviridae Plaque Assay [Ref:36678471]IAV: DEFB1 overexpression reduced viral copy number in bronchial epithelial cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found β-defensin-1 plays a key role in regulating IAV survival through STAT3 and is a potential target for antiviral drug development. 3934.57 C167H262N48O50S6 EMWOU GK 8.87 5 1 4 32 24 -0.272 1.3 1.1 hours 3 min >10 hours 46.11 4470 1.136 36678471 "Pathogens (Basel, Switzerland), 12(1), 123." "Othumpangat, S., & Noti, J. D. (2023)." β-Defensin-1 Regulates Influenza Virus Infection in Human Bronchial Epithelial Cells through the STAT3 Signaling Pathway 10.3390/pathogens12010123 Anti-IAV DRAVPe02121 DSHAKRHHGYKRKFHEKHHSHRGY 24 Human histatin 5 "Salivary glands, H. sapiens" P15516 Experimentally validated 9606 HTN3 AAA58646.1 20-43 M26665.1 CM000666.2 mRNA "Chromosome 4: 70,028,455-70,036,538" None HIV Retroviridae Peptide depletion assay [Ref:16940535]HIV: Dh-5 reduced infectivity; T20 inhibition dominant over Dhvar2 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Dh-5 inhibited HIV-1 replication 3036.33 C133H195N51O33 NCQILMPTWVOU H 10.28 7 2 5 22 18 -2.454 4.81 1.1 hours 3 min >10 hours 4.17 2980 0.981 16940535 "Journal of virology, 80(18), 9236–9243" "Groot, F., Sanders, R. W., ter Brake, O., Nazmi, K., Veerman, E. C., Bolscher, J. G., & Berkhout, B. (2006)." Histatin 5-derived peptide with improved fungicidal properties enhances human immunodeficiency virus type 1 replication by promoting viral entry 10.1128/JVI.00796-06 Anti-HIV DRAVPe02122 GIKCRFCCGCCTPGICGVCCRF 22 Hepcidin 1–5 "tilapia, Oreochromis mossambicus" No entry found Experimentally validated 106582 Not Available Not Available Not Available Not Available Not Available Not Available Not Found None NNV Nodaviridae Not Available "[Ref:20214942]Fish virus model: Hepcidin 1–5 (10 µg/fish), survival=68%" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane "The mechanism of action (MOA) of hepcidin 1-5 against the nervous necrosis virus (NNV) involves a combination of direct antiviral and immunomodulatory effects. Hepcidin 1-5 functions as a lytic peptide, disrupting the viral structure through direct interaction, as demonstrated in vitro. Additionally, treatment with hepcidin 1-5 was shown to downregulate NNV gene expression, as verified by RT-PCR, indicating its ability to inhibit viral replication or transcription. The peptide also modulates the host immune response by reducing interferon gene expression, which may help control excessive inflammation while supporting viral clearance. Importantly, hepcidin 1-5 proved effective in pretreatment, co-treatment, and post-treatment scenarios, demonstrating its versatility in preventing infection, combating active viral presence, and rescuing infected organisms" 2329.91 C94H153N29O24S8 ANDQEHLMSWYOU C 8.54 3 0 3 24 18 1 0.81 30 hours >20 hours >10 hours 48.64 0 0 20214942 "Peptides, 31(6), 1026–1033. " "Wang, Y. D., Kung, C. W., & Chen, J. Y. (2010)." Antiviral activity by fish antimicrobial peptides of epinecidin-1 and hepcidin 1–5 against nervous necrosis virus in medaka 10.1016/j.peptides.2010.02.025 Anti-NNV DRAVPe02120 ATCYCRTGR 9 HD-5(1–9) H. sapiens Q01523 Experimentally validated 9606 DEFA5(1670) AAA35754.1 63-71 M97925.1 CM000670.2 Genomic DNA chr8:7055304-7056739:- 1ZMP HCMV Herpesviridae Inhibition Assay "[Ref:32209394]HCMV: HD5(1–9) blocked infection, reduced viability at 18.75 µM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:32209394]HD5(1–9) was not cytotoxic for any of the cell types tested  No predicted structure available Linear Free Free None L Cell Membrane HD5(1–9) inhibited HCMV cellular attachment and thereby entry and was active against primary as well as a multiresistant HCMV isolate 1030.18 C40H67N15O13S2 NDQEHILKMFPSTWVOU RCT 8.96 2 0 2 9 8 -0.589 3.31 4.4 hours >20 hours >10 hours 11.11 1490 1.446 32209394 "Antiviral research, 177, 104779." "Böffert, R., Businger, R., Preiß, H., Ehmann, D., Truffault, V., Simon, C., Ruetalo, N., Hamprecht, K., Müller, P., Wehkamp, J., & Schindler, M. (2020)." The human α-defensin-derived peptide HD5(1-9) inhibits cellular attachment and entry of human cytomegalovirus 10.1016/j.antiviral.2020.104779 Anti-HCMV DRAVPe02119 KFFKRLLKSVRRAVKKFRKKPRLIGLSTLL 30 Hc-CATH "Venom gland, spleen, and lung, annulated sea snake, Hydrophis cyanocinctus" A0A0G3DRW6 Experimentally validated 8686 Not Available Not Available 158-171 Not Available Not Available Not Available Not Found None ZIKV Flaviviridae Inhibition Assay "[Ref:36089062]ZIKV: At 5 µM, reduced 70.3% CPE, 52.7% RNA, 67.4% NS3, 71.6% particles" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:36089062]MammalianCells: No cytotoxicity at 1.25, 2.5, and 5 µM" No predicted structure available Linear Free Free None L Cell Membrane "Hc-CATH can bind to ZIKV, disrupt viral membrane, induce the leakage of viral genomic RNA, and then inactivate ZIKV virions" 3628.59 C171H300N52O34 NDCQEHIMWYOU K 12.61 12 0 12 22 18 -0.273 2.28 1.3 hours 3 min 3 min 113.67 0 0 36089062 "The Journal of biological chemistry, 298(10), 102471." "Wang, J., Jiang, B., Wang, K., Dai, J., Dong, C., Wang, Y., Zhang, P., Li, M., Xu, W., & Wei, L. (2022)." A cathelicidin antimicrobial peptide from Hydrophis cyanocinctus inhibits Zika virus infection by downregulating expression of a viral entry factor 10.1016/j.jbc.2022.102471 Anti-ZIKV DRAVPe02118 VGALAVVVWLWLWLW 15 Gramicidin A "Soil bacterium, Bacillus brevis" None Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found 1MAG "HIV,HSV" Retroviridae ELISA "[Ref:9672588]HSV-1,HSV-2: IC50=0.2–0.4 mg/ml (HSV-1), 0.1–0.3 mg/ml (HSV-2)" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free "Synthesized non-ribosomally by a multienzyme complex. Both the N- and C-termini are chemically modified (CHO at the N-terminus and NHCH2CH2OH at the C-terminus). N-terminus is rich in Val, while the C-terminus is rich in Trp. Amino acids 4, 6, 8, 10, and 12 are D-amino acids." L Not Found gramicidin suppressed the replication of ACV-resistant thymidine kinase and DNA polymerase HSV mutants at doses effective against ACV-sensitive strains. 1811.25 C96H135N19O16 RNDCQEHIKMFPSTYOU LV 5.49 0 0 0 12 10 2.107 -3.31 100 hours >20 hours >10 hours 194.67 22000 12.146 9672588 "Archives of virology, 142(11), 2225–2235." "Bourinbaiar, A. S., & Coleman, C. F. (1997)." "The effect of gramicidin, a topical contraceptive and antimicrobial agent with anti-HIV activity, against herpes simplex viruses type 1 and 2 in vitro" 10.1007/s007050050237 "Anti-HIV, Anti-HSV" DRAVPe02117 ANTAFVSSAHNTQKIPAGAPFNRNLRAMLADLRQNAAFAG 40 Ginkbilobin "Seeds, Ginkgo biloba, Asia" P83171 Experimentally validated 3311 GNK1 Not Available 1-40 Not Available Not Available Not Available Not Found None HIV Retroviridae Inhibition Assay [Ref:11118300]HIV: Suppressed HIV-1 reverse transcriptase activity No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found It suppressed the activity of HIV-1 reverse transcriptase  4213.75 C183H291N59O54S1 CEWYOU A 11.71 4 1 3 32 24 -0.18 1.62 4.4 hours >20 hours >10 hours 71.25 0 0 11118300 "Biochemical and biophysical research communications, 279(2), 407–411." "Wang, H., & Ng, T. B. (2000)." "Ginkbilobin, a novel antifungal protein from Ginkgo biloba seeds with sequence similarity to embryo-abundant protein" 10.1006/bbrc.2000.3929 Anti-HIV DRAVPe02116 GLVGTLLGHIGKAILGG 17 Frenatin 2.3S "The Orinoco lime treefrog, Sphaenorhynchus lacteus, South America" L0L3V3 Experimentally validated 279984 Not Available Not Available 55-71 AGB51284.1  Not Available Not Available Not Found None YFV Flaviviridae antiviral colorimetric assay [Ref:27049440]YFV: 35% protective effect in Vero E6 cells at 20 µg/ml No hemolysis information or data found in the reference(s) presented in this entry [Ref:27049440]VeroE6: No cytotoxicity at 100 µg/ml No predicted structure available Cyclic Free Free None L Not Found Not Available 1575.91 C72H126N20O19 RNDCQEMFPSTWYOU G 8.76 1 0 1 14 12 1.176 -1.66 30 hours >20 hours >10 hours 160.59 0 0 27049440 "The Journal of antibiotics, 69(11), 783–790." "Muñoz-Camargo, C., Méndez, M. C., Salazar, V., Moscoso, J., Narváez, D., Torres, M. M., Florez, F. K., Groot, H., & Mitrani, E. (2016)." Frog skin cultures secrete anti-yellow fever compounds 10.1038/ja.2016.16 Anti-YFV DRAVPe02115 GLLGTLGNLLNGLGL 15 Frenatin-2 "White-lipped treefrog Litoria infrafrenata, Australia" P82022 Experimentally validated 61195 Not Available Not Available 1to 15 Not Available Not Available Not Available Not Found None YFV Flaviviridae antiviral colorimetric assay Not Available No hemolysis information or data found in the reference(s) presented in this entry [Ref:27049440]CMs were not cytotoxic to the CHO-K1 cell line No predicted structure available Cyclic Free Free None L Not Found Not Available 1424.7 C64H113N17O19 ARDCQEHIKMFPSWYVOU L 5.52 0 0 0 12 10 1.127 -1.55 30 hours >20 hours >10 hours 182 0 0 27049440 "The Journal of antibiotics, 69(11), 783–790." "Muñoz-Camargo, C., Méndez, M. C., Salazar, V., Moscoso, J., Narváez, D., Torres, M. M., Florez, F. K., Groot, H., & Mitrani, E. (2016)." Frog skin cultures secrete anti-yellow fever compounds 10.1038/ja.2016.16 Anti-YFV DRAVPe02114 GFSSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC 37 Esculentin-2P "North American frog, Rana pipiens" No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1 Retroviridae HIV infection and cell viability assay [Ref:16140737]HIV: Inhibited infection at a concentration also toxic to T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Envelope/outer leaflet of the membrane Highly effective in inhibiting HIV infection by disrupting the viral membrane and preventing the entry of the virus into target cells.  3870.63 C173H290N50O46S2 HPTWYOU GK 10.21 7 1 6 24 18 0.357 0.73 30 hours >20 hours >10 hours 97.57 0 0 16140737 " Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)" Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe02113 GLFSKKGGKGGKSWIKGVFKGIKGIGKEVGGDVIRTGIEIAACKIKGEC 46 Esculentin-1GN "The crawfish frog, Rana areolata, North America" No entry found Experimentally validated A0A3G6VAR4 110109 Not Available 39-87 Not Available Not Available Not Available mRNA None IAV(H1N1) Orthomyxoviridae Inhibition Assay "[Ref:33624755]H5N1,H1N1: IC50=1.29–4.59 µM for viral entry inhibition" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free "E105, N50 and the residues around them on HA2 subunit could form hydrogen bonds with amino acid on ESC-1GN" L Cell Membrane ESC-1GN disrupted membrane fusion activity of IAVs by interaction with HA2 subunit 5006.99 C225H379N63O61S2 NQHMPYOU G 9.87 11 4 7 32 24 -0.078 0.62 30 hours >20 hours >10 hours 85.51 5500 1.098 33624755 "Journal of biochemistry, 169(6), 757–765." "Yang, J., Zhang, B., Huang, Y., Liu, T., Zeng, B., Chai, J., Wu, J., & Xu, X. (2021)." Antiviral activity and mechanism of ESC-1GN from skin secretion of Hylarana guentheri against influenza A virus 10.1093/jb/mvab019 Anti-IAV DRAVPe02112 GLFPKFNKKKVKTGIFDIIKTVGKEAGMDVLRTGIDVIGCKIKGEC 46 Anti-NN+B14:B21 Rana areolata No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1 Retroviridae HIV infection and cell viability assay [Ref:16140737]HIV: Inhibited infection at a concentration also toxic to T cells [Ref:16140737]Not hemolytic HC50=120 uM No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Highly effective in inhibiting HIV infection by disrupting the viral membrane and preventing the entry of the virus into target cells.  4997.05 C226H381N59O61S3 QHSWYOU K 9.57 10 5 5 32 24 0.03 0.89 30 hours >20 hours >10 hours 95.22 0 0 16140737 " Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)" Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe02111 ALWFTMLKKLGTMALHAGKAALGAAANTISQGTQ 34 Dermaseptin-S2 "Sauvage's leaf frog, Phyllomedusa sauvagii, South America" P80278 Experimentally validated 8395 Not Available Not Available 1-34 Not Available Not Available Not Available Not Found None HSV-1 "[Ref:16672548]hBD3 inhibit HIV-1 inT2:T27fection by both viral strains, with greater activity against X4 viruses" Inhibition Assay [Ref:20718719]HSV-1: EC50=16 µg/ml No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Available 3473.11 C155H255N43O43S2 CDEPRVY A 10.3 4 0 4 10 16 0.382 5.06 4.4 hour >20 hour >10 hour 92.35 5500 166.67 20718719 " acta pathologica, microbiologica, et immunologica Scandinavica, 118(9), 674–680" "Savoia, D., Donalisio, M., Civra, A., Salvadori, S., & Guerrini, R. (2010)." In vitro activity of dermaseptin S1 derivatives against genital pathogens 10.1111/j.1600-0463.2010.02637.x Anti-HSV DRAVPe02109 GSKKPVPIIYCNRRTGKCQRI 21 SB1 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "[Ref:Not Available]HIV,HSV: EC50=13.1 µg/ml in CEM-SS cells, 64.9 µg/ml in Vero cells (HSV)" No hemolysis information or data found in the reference(s) presented in this entry "TC50:>100 µg/ml in CEM-SS Cells, >100 µg/ml in Vero Cells (HSV)" No predicted structure available Linear Not included yet Not included yet C11-C18 disulfide linkage L Not Found Not Available 2417.92 C104H181N35O27S2 ADEHLMFWOU RCGIK 10.47 6 0 6 22 16 -0.776 1.24 30 hours >20 hours >10 hours 69.52 1490 0.616 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S11" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2020" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-012 Anti-HIV DRAVPe02110 MAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAF 33 Z2 synthetic peptide derived from the stem region of ZIKV envelope protein No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None ZIKV Flaviviridae plaque reduction assay  "[Ref:28742068]ZIKV: IC50=1.75±0.13 µM in BHK21 cells, 3.69±0.27 µM in Vero cells; plaque assay IC50=2.61±0.46 µM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L E protein "The mechanism by which a peptide derived from the stem region of a flavivirus can inhibit infection by a broad spectrum of flaviviruses remains a point of controversy. It was reported that DN59, a 33-mer peptide that mimics a fragment of stem region of DENV E protein, acts like a disrupter of the DENV membrane, possibly inducing hole formation, leading to release of the viral genome. Z2 peptide could bind to the E protein of ZIKV and disrupt the integrity of ZIKV membrane, resulting in the inactivation of virions" 3308.76 C151H227N39O43S1 RCEPYOU AG 5.19 1 2 -1 25 18 0.636 1.1704 30 hours >20 hours >10 hours 91.82 5500 1.662 28742068 "Nat Commun 8, 15672 (2017)" "Yu, Y., Deng, YQ., Zou, P. et al." A peptide-based viral inactivator inhibits Zika virus infection in pregnant mice and fetuses 10.1038/ncomms15672 Anti-ZIKV DRAVPe02108 GSRRPVPIIYCNRRTGRCQRI 21 SB2 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "Ref:Not Available]HIV,HSV: EC50=3.33 µg/ml in CEM-SS cells, >100 µg/ml in Vero cells (HSV)" No hemolysis information or data found in the reference(s) presented in this entry "TC50:>100 µg/ml in CEM-SS Cells, >100 µg/ml in Vero Cells (HSV)" No predicted structure available Linear Not included yet Not included yet C11-C18 disulfide linkage L Not Found Not Available 2417.92 C104H181N35O27S2 ADEHMFWOU RK 10.47 7 0 7 22 16 -0.776 1.24 30 hours >20 hours >10 hours 69.52 1615 0.668 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S10" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2019" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-011 Anti-HIV DRAVPe02107 GCRRLLGRLLRRLGRLLCR 19 GLRC-1 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "[Ref:Not Available]HIV,HSV: EC50>100 µg/ml in CEM-SS cells, 30 µg/ml in Vero cells (HSV)" No hemolysis information or data found in the reference(s) presented in this entry "TC50:59.2 µg/ml in CEM-SS Cells, >100 µg/ml in Vero Cells (HSV)" No predicted structure available Linear Not included yet Not included yet C2-C18 disulfide linkage L Not Found Not Available 2280.88 C96H182N40O20S2 ANDQEHIKMFPSTWYVOU RL 12.13 7 0 7 17 13 -0.058 1.0824 30 hours >20 hours >10 hours 143.68 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S9" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2018" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-010 Anti-HIV DRAVPe02106 GLRCRLGRLLRRLGRCLLR 19 GLRC-2 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "[Ref:Not Available]HIV,HSV: EC50=1.81 µg/ml in CEM-SS cells, 5.43 µg/ml in Vero cells (HSV)" No hemolysis information or data found in the reference(s) presented in this entry "TC50: 17.8 µg/ml in CEM-SS cells, 31.8 µg/ml in Veo Cells" No predicted structure available Linear Not included yet Not included yet C4-C16 disulfide linkage L Not Found Not Available 2280.88 C96H182N40O20S2 ANDQEHIKMFPSTWYVOU RL 12.13 7 0 7 16 12 -0.058 1.05 30 hours >20 hours >10 hours 143.68 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S8" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2017" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-009 Anti-HIV DRAVPe02105 GLRRLCGRLGRRLCRLLLR 19 GLRC-3 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "[Ref:Not Available]HIV,HSV: EC50=6.37 µg/ml in CEM-SS cells (HIV), 15 µg/ml in Vero cells (HSV)" No hemolysis information or data found in the reference(s) presented in this entry "18.5 µg/ml in CEM-SS cells, 62.3 µg/ml in Vero Cells (HSV)" No predicted structure available Linear Not included yet Not included yet C6-C14 disulfide linkage L Not Found Not Available 2280.88 C96H182N40O20S2 ANDQEHIKMFPSTWYVOU RL 12.13 7 0 7 16 12 -0.058 1.12 30 hours >20 hours >10 hours 143.68 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S7" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2016" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-008 Anti-HIV DRAVPe02104 GCRRLCGRLGRRLCRLLCR 19 GLRC_4 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None "HIV-1IIIB, HSV-2MS" Retroviridae Anti-HIV assays "[Ref:Not Available]HSV: EC50=69.3 µg/ml in CEM-SS cells, 64.7 µg/ml in Vero cells" No hemolysis information or data found in the reference(s) presented in this entry "TC50: >100 µg/ml in CEM-SS cells, TC50: >100 µg/ml in Vero Cells (HSV)" No predicted structure available Linear Not included yet Not included yet "C2-C18, C6-C14 disulfide linkage" L Not Found Not Available 2280.88 C90H170N40O20S4 ANDQEHIKMFPSTWYVOU RL 12.13 7 0 7 16 12 -0.058 1.12 30 hours >20 hours >10 hours 143.68 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S6" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2015" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-007 Anti-HIV DRAVPe02103 GLRCRLGRLLRRLGRC 16 GLRC-5 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1IIIB Retroviridae Anti-HIV assays [Ref:Not Available]HIV: EC50>100 µg/ml in CEM-SS cells No hemolysis information or data found in the reference(s) presented in this entry TC50: 59.5 µg/ml in CEM-SS cells No predicted structure available Linear Not included yet Not included yet C4-C16 disulfide linkage L Not Found Not Available 1898.37 C78H148N34O17S2 ANDQEHIKMFPSTWYVOU RL 12 7 0 7 14 12 -0.263 1.0857 30 hours >20 hours >10 hours 121.88 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S5" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2014" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-006 Anti-HIV DRAVPe02101 GLRCLRLRGRLRLGRCLLR 19 GLRC-8 De novo designed No entry found De Novo None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1IIIB Retroviridae Anti-HIV assays [Ref:Not Available]HIV: EC50>100 µg/ml in CEM-SS cells No hemolysis information or data found in the reference(s) presented in this entry TC50:31 µg/ml in CEM-SS cells No predicted structure available Linear Not included yet Not included yet C4-C16 disulfide linkage L Not Found Not Available 2280.88 C96H182N40O20S2 ANDQEHIKMFPSTWYVOU RL 12.13 6 0 6 16 12 -0.058 1.12 30 hours >20 hours >10 hours 143.68 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S3" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2012" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-004 Anti-HIV DRAVPe02102 CRLGRLLRRLGRC 13 GLRC-7 De novo designed No entry found Experimentally validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1IIIB Retroviridae Anti-HIV assays [Ref:Not Available]HIV: EC50>100 µg/ml in CEM-SS cells No hemolysis information or data found in the reference(s) presented in this entry TC50: >100 µg/ml in CEM-SS cells No predicted structure available Linear Not included yet Not included yet C1-C13 disulfide linkage L Not Found Not Available 1571.97 C64H122N28O14S2 ANDQEHIKMFPSTWYVOU RL 11.83 8 0 8 12 10 -0.238 1.1 1.2 hours >20 hours >10 hours 120 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S4" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2013" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-005 Anti-HIV DRAVPe02100 CRLGRLLRRLGRCLLR 16 GLRC-6 De novo designed No entry found De Novo None Not Available Not Available Not Available Not Available Not Available Not Available Not Found None HIV-1IIIB Retroviridae Anti-HIV assays [Ref:Not Available]HIV: EC50=7.72 µg/ml in CEM-SS cells (T2:T27) No hemolysis information or data found in the reference(s) presented in this entry TC50:41.9 (µg/ml) in CEM-SS cells. No predicted structure available Linear Not included yet Not included yet hairpin structure with a single disulfide bond (C11-C18) between the two strands L Not Found Not Available 1954.48 C82H156N34O17S2 ANDQEHIKMFPSTWYVOU RL 12 7 0 7 13 10 0 1.0571 1.2 hours >20 hours >10 hours 146.25 0 0 Not Avaialbe "Reginald et al. J AIDS Clinic Res 2011, S2" "Wang G, Watson KM, Mishra B, Lushnikova T, Buckheit RW Jr. 2011" De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop Structures 10.4172/2155-6113.S2-003 Anti-HIV DRAVPe02099 GVSGHGQHGVHG 12 Alloferon 2 Calliphora vicina (Blue blowfly) (Calliphora erythrocephala) P83412 Experimentally Validated 7373 Not Available Not Available 2to13 Not Available Not Available Not Available Not Available None "IAV,IBV" Orthomyxoviridae Antiviral activity assay. [Ref:12235362]General antiviral activity: Stimulated antiviral and antitumoral resistance when injected in mice. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Carboxylation amidation None L Membrane "Alloferon can (i) stimulate natural cytotoxicity of human peripheral blood lymphocytes, (ii) induces IFN synthesis in mouse and human models, and (iii) enhances antiviral and antitumor resistance in mice." 1128.63 C46H69N19O15 ARNDCEILMKFPTWYOU GH 7.02 3 0 3 6 2 -0.823 -10.14 3.5 hours 10 min >10 hours 44.62 0 0 12235362 " Proceedings of the National Academy of Sciences of the United States of America, 99(20), 12628–12632." "Chernysh, S., Kim, S. I., Bekker, G., Pleskach, V. A., Filatova, N. A., Anikin, V. B., Platonov, V. G., & Bulet, P. (2002)." Antiviral and antitumor peptides from insects 10.1073/pnas.192301899 DRAVPa1832 Anti-IAV-Anti-IBV DRAVPe02098 HGVSGHGQHGVHG 13 Alloferon 1 Calliphora vicina (Blue blowfly) (Calliphora erythrocephala) P83412 Experimentally Validated 7373 Not Available Not Available 1to13 Not Available Not Available Not Available Not Available None "HHV-1,IAV" Orthomyxoviridae Antiviral activity assay. [Ref:12235362]General antiviral activity: Stimulated antiviral and antitumoral resistance when injected in mice. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Carboxylation Amidation "The three imidazoles of H1, H6, and H9 participate in the coordination of Zn(II)" L Membrane "Alloferon can (i) stimulate natural cytotoxicity of human peripheral blood lymphocytes, (ii) induces IFN synthesis in mouse and human models, and (iii) enhances antiviral and antitumor resistance in mice." 1265.15 C52H76N22O16 ARNDCEILMKFPTWYOU GH 7.1 4 0 4 4 2 0.9 -14.8 20 hours 30 min >10 hours 209.29 0 0 21766388##12235362 "Journal of peptide science : an official publication of the European Peptide Society, 17(11), 715–719##Proceedings of the National Academy of Sciences of the United States of America, 99(20), 12628–12632." "Kuczer, M., Midak-Siewirska, A., Zahorska, R., Luczak, M., & Konopińska, D. (2011)##Chernysh, S., Kim, S. I., Bekker, G., Pleskach, V. A., Filatova, N. A., Anikin, V. B., Platonov, V. G., & Bulet, P. (2002)." Further studies on the antiviral activity of alloferon and its analogues##Antiviral and antitumor peptides from insects 10.1002/psc.1388##10.1073/pnas.192301899 DRAVPa1831 "Anti-HHV-1,Anti-IAV" DRAVPe02097 INLKILARLAKKIL 14 "[I5, R8]Mastoparan" "Venom, Vespula lewisii" P01514 Experimentally Validated 7452 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 6DUL##1D7N HSV-1 Herpesviridae  Plaque Assay [Ref:38932240]Human alphaherpesvirus 1 (HSV-1): Inhibited entry (EC50 = 6.22 µM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref:38932240]CC50 > 50 µg.mL−1. Mastoparan showed no cytotoxicity even at higher concentrations (LC50 > 200 µM).However, in THP-1-derived macrophages, LC50 ranged between 24.5~12.9 µM." No predicted structure available Linear Free Amination None L Membrane "Mastoparan can be classified as entry inhibitors, for which characteristics such as cationicity and hydrophobicity play a significant role, primarily against enveloped viruses. Nevertheless, further assays with other enveloped and non-enveloped viruses are needed to address this matter.mastoparan, it is inferred that this peptide may also affect lipid vesicles mimicking the viral envelope" 1607.1 C76H143N21O16 DCQEGHMFPSTUQYOV KLI 11.26 4 0 4 5 9 1.157 0.01 20 hours 30 min >10 hours 195.71 0 0 38932240 Viruses. 2024 Jun 12;16(6) "Vilas Boas LCP, Buccini DF, Berlanda RLA, Santos BPO, Maximiano MR, Lião LM, Gonçalves S, Santos NC, Franco OL." Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1  10.3390/v16060948 Anti-HSV-1 DRAVPe02096 INLKALAALAKKIL 14 Mastoparan-L "Venom, Vespula lewisii" P01514 Experimentally Validated 7452 Not Available Not Available 1to14 Not Available Not Available Not Available Not Available 6DUL##1D7N HSV-1 Herpesviridae  Plaque Assay [Ref:38932240]No significant inhibition. No hemolysis information or data found in the reference(s) presented in this entry [Ref:38932240]CC50 > 200 µg.mL−1 No predicted structure available Linear Free Amination None L Membrane "Mastoparan can be classified as entry inhibitors, for which characteristics such as cationicity and hydrophobicity play a significant role, primarily against enveloped viruses. Nevertheless, further assays with other enveloped and non-enveloped viruses are needed to address this matter.mastoparan, it is inferred that this peptide may also affect lipid vesicles mimicking the viral envelope" 1479.91 C70H130N18O16 RDCQEGHMFPSTWYVOU AILK 10.3 3 0 3 4 10 1.157 -0.96 20 hours 30 min >10 hours 195.71 0 0 38932240 Viruses. 2024 Jun 12;16(6) "Vilas Boas LCP, Buccini DF, Berlanda RLA, Santos BPO, Maximiano MR, Lião LM, Gonçalves S, Santos NC, Franco OL." Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1  10.3390/v16060948 Anti-HSV-1 DRAVPe02095 EKYTEAPEYI 10 Ala-6-fenycin Bacillus sp. strain P34 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "EAV, FHV-1" Arteriviridae Antiviral assay. "[Ref:25477947]Equine arteritis virus (EAV): P34 peptide inhibited replication by 99.9%, and Feline herpesvirus-1 (FHV-1) by 94.4%." No hemolysis information or data found in the reference(s) presented in this entry "[Ref:25477947]MDCK cells: CC50 = 2.11 µg/mL,CRFK cells: CC50 = 2.5 µg/mL,RK13 cells: CC50 = 3.92 µg/mL,MDCK cells: No cytotoxicity observed at 1.37 µg/mL of peptide P34,CRFK cells: No cytotoxicity obs" No predicted structure available Linear Free Carboxylation None L Membrane This peptide inactivates the virus through an interaction with a non-lipidic structural component. 1242.35 C57H83N11O20 RNDCQLMFSWVOU E 4.25 1 3 -2 5 5 -1.3 2.21 1 hour 30 min >10 hours 49 2980 2.399 25477947##28083516 "Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 45(3), 1089–1094##Frontiers in cellular and infection microbiology, 6, 194" "Scopel e Silva, D., de Castro, C. C., da Silva e Silva, F., Sant'anna, V., Vargas, G. D., de Lima, M., Fischer, G., Brandelli, A., da Motta, A.deS., & Hübner, S.deO. (2014)##Mahlapuu, M., Håkansson, J., Ringstad, L., & Björn, C. (2016)" Antiviral activity of a Bacillus sp: P34 peptide against pathogenic viruses of domestic animals##Antimicrobial Peptides: An Emerging Category of Therapeutic Agents 10.1590/s1517-83822014000300043##10.3389/fcimb.2016.00194 "Anti-EAV,Anti-FHV-1" DRAVPe02094 GIGAVLKYLTTGLPALISWIKRKROQ 26 Melittin of bee venom Bee Venom No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae MTT assay/ RT-qPCR Assay [Ref:33652894]SARS-CoV-2: Sitagliptin and melittin-nanoconjugates complex exhibited significant antiviral activity (IC50 = 8.439 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref:34261542]C654 cells: Melittin CC50 = 6.45 µg/mL. No predicted structure available Linear Free Free None L Membrane "Melittin disrupts viral membranes, activates Toll-like receptors to reduce inflammatory cytokines, suppresses metabolic regulators like transketolase, and activates host RNA-binding proteins," 3020.7 C142H239N39O33 NDCHMFU ARGILKT 11.17 5 0 5 10 16 0.196 2.21 30 hours >20 hours >10 hours 123.85 6990 2.314 35236909 "Scientific reports, 12(1), 3446" "Enayathullah, M. G., Parekh, Y., Banu, S., Ram, S., Nagaraj, R., Kumar, B. K., & Idris, M. M" Gramicidin S and melittin: potential anti-viral therapeutic peptides to treat SARS-CoV-2 infection 10.1038/s41598-022-07341-x Anti-SARS-CoV-2 DRAVPe02093 GAICHPVFCPRRYKQIGTCGLPGTKCCKKP 30 4H30 human beta-defensin 2 (HBD2) O15263 Experimentally Validated 9606 DEFB4A(100289462) AF040153.1 20-64 pfam00711 CM000670.2 mRNA "Chromosome 8:7,894,677-7,896,716" 1FD3 SARS-CoV-2 Coronaviridae plaque reduction assay/ [Ref:35768416]SARS-CoV-2: 4H30 significantly inhibited infection (IC50 = 0.59 µg/mL or 44 nM). No hemolysis information or data found in the reference(s) presented in this entry "[Ref:35768416]Vero E6, Calu-3: TC50 > 400 µg/mL." No predicted structure available Linear Free Free None L Lipid Bilayer "4H30 can inhibit three distinct steps of the SARS-CoV-2 life cycle. Specifically, 4H30 blocks viral entry by clustering SARS-CoV-2 virions; prevents membrane fusion by inhibiting endosomal acidification; and inhibits the release of virions by cross-linking SARS-CoV-2 with cellular glycosaminoglycans." 1973.46 C87H157N23O24S2 ARNDQEHIMFPTWYOU GLV 8.9 7 0 7 8 11 -1.36 1.12 30 hours >20 hours >10 hours 152.86 125 0.063 35768416 Cell Discov. 2022 Jun 30;8(1):62 "Zhao H, To KK, Lam H, Zhang C, Peng Z, Meng X, Wang X, Zhang AJ, Yan B, Cai J, Yeung ML, Chan JF, Yuen KY" A trifunctional peptide broadly inhibits SARS-CoV-2 Delta and Omicron variants in hamsters 10.1038/s41421-022-00428-9 DRAVPa2313 Anti-SARS-CoV-2 DRAVPe02092 GADFQECMKEHSQKQHQHQG 20 Alpha-basrubrin isolated from seeds of the Ceylon spinach Basella rubra P83186 Experimentally Validated 3589 Not Available Not Available 1to20 Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA "[Ref:11688973]HIV-1: Alpha-Basrubrin inhibited reverse transcriptase activity (79.4 ± 7.8% at 400 µM, 10.6 ± 0.9% at 40 µM)." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Free None L Not given Inhibits HIV-1 reverse transcriptase and cell-free translation 2353.53 C96H145N33O33S2 RNILTWYVOU Q 6.27 2 3 -1 0 0 -1.9 3.41 30 hours >20 hours >10 hours 5 0 0 11688973 "Biochemical and biophysical research communications, 288(4), 765–770." "Wang, H., & Ng, T. B. (2001)" Novel antifungal peptides from Ceylon spinach seeds 10.1006/bbrc.2001.5822 Anti-HIV DRAVPe02091 LNCYWPLNDYGFYTTTGIGYK 21 S5 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae SARS-CoV-2 inhibition assay [Ref:38917689]SARS-CoV: S5 peptide targeted the binding site of SARS.-CoV-1 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given " All peptides (S2, S4, and S5) in this study bound to the ACE2 receptor and established a competitive inhibitory relationship with the RBD" 2489.78 C118H161N25O33S1 ARQEHMSVOU Y 5.83 1 1 0 8 13 -0.381 0.55 5.5 hours 3 min 2 min 55.71 11460 4.603 38917689 "Virology, 597, 110149." "Liang, Z., Wang, J., Zhang, H., Gao, L., Xu, J., Li, P., Yang, J., Fu, X., Duan, H., Liu, J., Liu, T., Ma, W., & Wu, K." Peptide S4 is an entry inhibitor of SARS-CoV-2 infection 10.1016/j.virol.2024.110149 Anti-SARS-CoV-2 DRAVPe02090 YNYLYRLFC 9 S2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae SARS-CoV-2 inhibition assay [Ref:38917689]SARS-CoV-2: S2 and S4 peptides targeted the binding site of SARS-CoV-2 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given " All peptides (S2, S4, and S5) in this study bound to the ACE2 receptor and established a competitive inhibitory relationship with the RBD" 1254.47 C61H83N13O14S1 ADQEGHIKMPSTWVOU Y 8.17 1 0 1 3 6 0.111 0.87 2.8 hours 10 min 3 min 86.67 4470 3.563 38917689 "Virology, 597, 110149." "Liang, Z., Wang, J., Zhang, H., Gao, L., Xu, J., Li, P., Yang, J., Fu, X., Duan, H., Liu, J., Liu, T., Ma, W., & Wu, K." Peptide S4 is an entry inhibitor of SARS-CoV-2 infection 10.1016/j.virol.2024.110151 Anti-SARS-CoV-2 DRAVPe02089 FNCYFPLQSYGFQPTNGVGYK 21 S4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae SARS-CoV-2 inhibition assay "[Ref:38917689] PT (Vero E6): EC50 = 4.40 µM (TI = 163.68), BA.2 (Vero E6): EC50 = 4.87 µM (TI = 147.88), EG.5 (Vero E6): EC50 = 8.44 µM (TI = 85.33), XBB.1.16 (Vero E6): EC50 = 9.59 µM (TI = 75.10)" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:38917689]PT(Vero E6): CC₅₀=720.20 µM,BA.2 (Vero E6): CC₅₀=720.20 µM,EG.5 (Vero E6): CC₅₀= 720.20 µM,XBB.1.16 (Vero E6): CC₅₀= 720.20 µM,HEK293T: CC₅₀=730.20 µM,HEK293T/ACE2: CC₅₀=714.0 µM" No predicted structure available Linear Free Free None L Not given peptide S4 inhibited the ACE2 receptor and competed with the HCoV-NL63 virus for binding while exhibiting good inhibitory activity against HCoV-NL63 infection. 2430.72 C115H156N26O31S1 ARDEHIMWOU GFY 8.15 1 0 1 13 8 -0.419 0.68 1.1 hours 3 min 2 min 32.38 4470 1.839 38917689 "Virology, 597, 110149." "Liang, Z., Wang, J., Zhang, H., Gao, L., Xu, J., Li, P., Yang, J., Fu, X., Duan, H., Liu, J., Liu, T., Ma, W., & Wu, K." Peptide S4 is an entry inhibitor of SARS-CoV-2 infection 10.1016/j.virol.2024.110150 Anti-SARS-CoV-2 DRAVPe02088 CYCRIPACIAGERRYGTCIYQGRLWAFCC 29 HNP-1 Synthetic construct P59665 Experimentally Validated 9606 DEFA1; DEFA1B M21130.1 59-74 pfam00323##smart00048 CM000670.2 mRNA Chromosome 8:6996766-6999198 1DFN##2KHT##3GNY IAV(H3N2) Orthomyxoviridae Antiviral activity assay. [Ref:17703413]IAV: Inhibited replication and viral protein synthesis No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given " HNP-1 treatment inhibited protein kinase C (PKC) activation in infected cells, suggesting the involvement of the PKC pathway" 17703413 "The Journal of infectious diseases, 196(6), 835–843" "Mirella Salvatore 1, Adolfo Garcia-Sastre, Piotr Ruchala, Robert I Lehrer, Theresa Chang, Mary E Klotman" alpha-Defensin inhibits influenza virus replication by cell-mediated mechanism(s) 10.1086/521027 DRAVPe00300 Anti-IAV DRAVPe02087 ESGRIKKEEFAEIMKICSTIEELGRQK 27 PB1731–757 Synthetic construct (derived from the C-terminus of PB1) Q9Q0V0 Experimentally Validated 93838##384505 PB1(3654616)  AAD51923.1 731-757 Not Available AF144301.1 Genomic RNA "Chromosome:25 - 2,298" 3J9B##8H69 IAV(H5N1) Orthomyxoviridae BiFC disruption assay [Ref:23279951]IAV: PB1731–757 effectively blocked the replication of human influenza virus A/WSN/33 (H1N1) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given PB1(731-757) is capable of inhibiting viral polymerase activity and viral replication. 3153.66 C135H230N38O44S2 NDHPWYVOU E 6.46 6 6 0 2 9 -0.793 2.7 1 hour 30 min >10 hours 75.93 0 0 23279951##23340380 "The FEBS journal, 280(4), 1139–1149##Viruses, 5(1), 352–373" "Li, C., Ba, Q., Wu, A., Zhang, H., Deng, T., & Jiang, T. (2013)##Jie Yang 1, Minmin Li, Xintian Shen, Shuwen Liu" A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly##Influenza A virus entry inhibitors targeting the hemagglutinin 10.1111/febs.12107##10.3390/v5010352 Anti-IAV DRAVPe02086 MERIKELRDLMSWSRTREILTKTTVDHMAIIKKYTSG 37 PB21-37 Synthetic construct No entry found In silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "IAV(H1N1,H5N1)" Orthomyxoviridae ELISA [Ref:21867756]H1N1: IC50 = 375 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free "The N-terminus of PB2 consists of 3 alpha-helices, one of which binds to 3 alpha-helices in the C-terminus of PB1 " L Membrane Inhibit Viral Replication 4439.23 C193H326N56O57S3 NCQFPOU REDIKMST 9.82 8 5 3 1 13 -0.586 2.62 "30 hours (mammalian reticulocytes, in vitro)" >20 hours >10 hours 84.32 6990 1.575 21867756 "Methods (San Diego, Calif.), 55(2), 188–191." "Chase, G., Wunderlich, K., Reuther, P., & Schwemmle, M. (2011). I" Identification of influenza virus inhibitors which disrupt of viral polymerase protein-protein interactions 10.1016/j.ymeth.2011.08.007 Anti-IAV DRAVPe02085 ACYCRIPACIAGERRYGTCIYQGRLWAFCC 30 Defensins Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "IAV(H1N1,H3N2)" Orthomyxoviridae Antiviral assay. [Ref:19494312]No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus Attachment and Virus-Cell Membrane Fusion 3448.09 C150H228N44O38S6 NDHKMSVOU ARCGIY 8.68 4 1 3 20 13 0.3 1.1704 4.4 hours >20 hours >10 hours 65.33 10345 3 19494312 "Journal of immunology (Baltimore, Md. : 1950), 182(12), 7878–7887." "Doss, M., White, M. R., Tecle, T., Gantz, D., Crouch, E. C., Jung, G., Ruchala, P., Waring, A. J., Lehrer, R. I., & Hartshorn, K. L. (2009)." "Interactions of alpha-, beta-, and theta-defensins with influenza A virus and surfactant protein D" 10.4049/jimmunol.0804049 Anti-IAV DRAVPe02084 FLPIIINLKALAALAKKIL 19 Mastoparan-MO "Venom, Vespula lewisii" P01514 Experimentally Validated 7452 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 6DUU) HSV-1 Herpesviridae  Plaque Assay [Ref:38932240]Human alphaherpesvirus 1 (HSV-1): Inhibited entry (EC50 = 6.68 µM). No hemolysis information or data found in the reference(s) presented in this entry [Ref:38932240]:CC50=>200 µg.mL−1 No predicted structure available Linear Free Amidation None L Membrane "Mastoparan-MO exhibited over 80% HSV-1 inhibition, with up to 99% viral replication inhibition, particularly in the early infection stages." 2063.68 C102H179N23O21 RDCEQGHMSTWYVOU L 10.03 3 0 3 4 15 1.589 0.8211 1.1 hours 3 min 2 min 205.79 0 0 38932240 Viruses. 2024 Jun 12;16(6) "Vilas Boas LCP, Buccini DF, Berlanda RLA, Santos BPO, Maximiano MR, Lião LM, Gonçalves S, Santos NC, Franco OL." Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1  10.3390/v16060948 Anti-HSV-1 DRAVPe02083 GFWFKGKWRFKKYRGGRYKKFRWKGKFWFG 30 PEP 19-8D Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "H7N7,H3N2,H1N2" Orthomyxoviridae Hemagglutination assay [Ref:24486207]Influenza virus: SALPs PEP 19-8D inhibited virus hemagglutination up to 75% depending on virus subtype and dilution No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus Attachment and Virus-Cell Membrane Fusion 3964.73 C200H276N54O33 ANDCQEHILMPSTVOU RGKFWY 11.64 12 0 12 10 17 -1.367 1.1 30 hours ">20 hours (yeast, in" >10 hours 0 24980 6.301 24486207 "Antiviral research, 104, 23–33. " "Hoffmann, J., Schneider, C., Heinbockel, L., Brandenburg, K., Reimer, R., & Gabriel, G. (2014). " A new class of synthetic anti-lipopolysaccharide peptides inhibits influenza A virus replication by blocking cellular attachment 10.1016/j.antiviral.2014.01.016 Anti-IAV DRAVPe02082 GKKYRRFRWKFKGKWFWFG 19 PEP 19-4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "IAV(H7N7,H3N2,H1N1)" Orthomyxoviridae Hemagglutination assay [Ref:24486207]Influenza virus: SALPs inhibited virus hemagglutination up to 75% depending on virus subtype and dilution. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus Attachment and Virus-Cell Membrane Fusion 2609.13 C132H182N36O21 ANDCQEHILMPSTVOU RGKFWY 11.76 8 0 8 3 7 -1.421 2.68 30 hours ">20 hours (yeast, in" >10 hours 0 17990 6.895 24486207 "Antiviral research, 104, 23–33. " "Hoffmann, J., Schneider, C., Heinbockel, L., Brandenburg, K., Reimer, R., & Gabriel, G. (2014). " A new class of synthetic anti-lipopolysaccharide peptides inhibits influenza A virus replication by blocking cellular attachment 10.1016/j.antiviral.2014.01.015 Anti-IAV DRAVPe02081 GLLASLGKVFGGYLAEKLKPK 21 Dahlein 5.6 "Litoria dahlii, Australia" P84272 Experimentally Validated 299727 Not Available Not Available 1to21 Not Available Not Available Not Available Not Available None HIV Retroviridae HIV infection and cell viability assay. [Ref:16140737]HIV: This peptide could inhibit HIV infection at a specific concentration. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Cell Membrane inhibit HIV infection at significantly lower concentrations than those required to affect the viability of the T cells. 2189.67 C104H173N25O26 RNDCQHIMTWOU L 9.83 4 1 3 22 16 0.248 -0.3 30 hours >20 hours >10 hours 116.19 1490 0.68 16140737 "Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)." Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV-1 DRAVPe02080 CGESCVFIPCITTVLGCSCSIKVCYKNGSIP 31 Cycloviolacin VY1 Viola yedoensis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None IAV Orthomyxoviridae In vitro assay [Ref:25212039]Influenza A virus (H1N1): IC50 = 2.27 µg/mL. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Found 3225.88 C138H226N34O42S6 ARDQMWOU C 7.77 2 1 1 24 18 0.874 -0.21 1.2 hours >20 hours >10 hours 90.97 1490 0.462 25212039 "Yao xue xue bao = Acta pharmaceutica Sinica, 49(6), 905–912." "Liu, M. Z., Yang, Y., Zhang, S. X., Tang, L., Wang, H. M., Chen, C. J., Shen, Z. F., Cheng, K. D., Kong, J. Q., & Wang, W. (2014)." [A cyclotide against influenza A H1N1 virus from Viola yedoensis] Not Available Anti-IAV DRAVPe02078 SPIHACRYQRGVCIPGPCRWPYYRVGSCGSGLKSCCVRNRWA 42 Chicken AvBD6 "G. gallus domestic; duck, A. platyrhynchos" Q6QLR3 Experimentally Validated 9031 GAL6 Not Available 26-67 Not Available Not Available Not Available Not Available None IBRV Orthomyxoviridae ELISA Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Found 4744.55 C205H317N67O52S6 DEFTOU C 9.61 7 0 7 32 24 -0.343 1.86 1.9 hours >20 hours >10 hours 53.33 15470 3.261 26142390 "Applied microbiology and biotechnology, 99(21), 9011–9024." "Xu, Y., Zhang, T., Xu, Q., Han, Z., Liang, S., Shao, Y., Ma, D., & Liu, S. (2015)." Differential modulation of avian β-defensin and Toll-like receptor expression in chickens infected with infectious bronchitis virus 10.1007/s00253-015-6786-8 Anti-IBrV DRAVPe02079 EQCREEEDDR 10 Coconut antifungal peptide Cocos nucifera No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Not Found "[Ref:16308082]HIV-1 reverse transcriptase: IC50 = 52.5 µM; Inhibition at 8 and 80 µM coconut antifungal peptide = 20.1% and 68.4%, respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found  It lowered the HIV-1 reverse transcriptase activity 1308.3 ANGHILKMNFPSTWYVOU E 4.08 2 6 -4 10 0 -3.1 7.87 1 hour 30 min >10 hours 0 0 0 16308082 "Peptides, 26(12), 2392–2396" "Wang, H. X., & Ng, T. B. (2005)" An antifungal peptide from the coconut 10.1016/j.peptides.2005.05.009 Anti-HIV-1 DRAVPe02077 GLPQDCERRGGFCSHKSCPPGIGRIGLCSKEDFCCRSRWYS 41 Chicken AvBD5 Gallus gallus domestic Q6IV26 Experimentally Validated 9031 GAL5 Not Available 26-66 Not Available Not Available Not Available Not Available None IBV Orthomyxoviridae ELISA Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Found 4593.25 C193H300N62O57S6 ANMVOU CG 8.67 7 4 3 32 24 -0.663 2.5 30 hours >20 hours >10 hours 38.05 6990 1.603 26142390 "Applied microbiology and biotechnology, 99(21), 9011–9024." "Xu, Y., Zhang, T., Xu, Q., Han, Z., Liang, S., Shao, Y., Ma, D., & Liu, S. (2015)." Differential modulation of avian β-defensin and Toll-like receptor expression in chickens infected with infectious bronchitis virus 10.1007/s00253-015-6786-8 Anti-IBV DRAVPe02076 KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK 37 Cecropin A "Giant silk moth, Hyalophora cecropia" P01507 Experimentally Validated 7123 Not Available Not Available 27-63 Not Available Not Available Not Available Not Available 1D9L HIV Retroviridae Transient transfection assays [Ref:9568968]HIV: Cecropin ID50 = 2–3 µM; HIV LTR activity reduced in cells with retroviral expression of cecropin No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found cecropin is capable of inhibiting cell-associated production of HIV-1 by suppressing HIV-1 gene expression. 4004.82 C184H312N52O47 CHMSYOU K 10.39 8 2 6 32 24 -0.073 0.84 1.3 hours 3 min 3 min 108.11 5500 1.373 9568968 "The Journal of general virology, 79 ( Pt 4), 731–740." "Wachinger, M., Kleinschmidt, A., Winder, D., von Pechmann, N., Ludvigsen, A., Neumann, M., Holle, R., Salmons, B., Erfle, V., & Brack-Werner, R. (1998)." Antimicrobial peptides melittin and cecropin inhibit replication of human immunodeficiency virus 1 by suppressing viral gene expression 10.1099/0022-1317-79-4-731 Anti-HIV DRAVPe02075 GLWQKIKSAAGDLASGIVEGIKS 23 Caerin 4.1 "Green tree frog Litoria caerula, Australia" P56242 Experimentally Validated 30344 Not Available Not Available 1to23 Not Available Not Available Not Available Not Available None HIV Retroviridae HIV infection and cell viability assay. [Ref:16140737]HIV: This peptide could inhibit HIV infection at a specific concentration No hemolysis information or data found in the reference(s) presented in this entry [Ref:16140737]Toxic to T cells No predicted structure available Linear Free Amination None L T cells inhibit HIV infection at significantly lower concentrations than those required to affect the viability of the T cells. 2328.69 C104H174N28O32 RNCHMFPTYOU G 8.5 3 2 1 22 16 0.157 0.33 30 hours >20 hours >10 hours 110.43 5500 2.362 16140737 "Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)." Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe02073 GLLSVLGSVAQHVLPHVVPVIAEHL 25 Caerin 1.3 L. caerulea P56228 Experimentally Validated 30344 Not Available Not Available 1to25 Not Available Not Available Not Available Not Available None HIV Retroviridae HIV infection and cell viability assay. [Ref:26026377]HIV: Less effective inhibitor of infection. No hemolysis information or data found in the reference(s) presented in this entry [Ref:26026377]Non-toxic or only modestly toxic at the concentrations tested No predicted structure available Linear Free Amination None L Membrane The disruption of the viral envelope and release p24 core protein 2585.09 C120H198N32O31 RNDCKMFTWYOU V 6.26 0 1 -1 22 16 1.204 -1.04 30 hours >20 hours >10 hours 171.2 0 0 26026377 "Peptides, 71, 296–303." "VanCompernolle, S., Smith, P. B., Bowie, J. H., Tyler, M. J., Unutmaz, D., & Rollins-Smith, L. A. (2015)." Inhibition of HIV infection by caerin 1 antimicrobial peptides 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe02074 GLLSSLSSVAKHVLPHVVPVIAEHL 25 Caerin 1.4 Australian frog Litoria caerula P62544##P62545 Experimentally Validated 30344 Not Available Not Available 1to25 Not Available Not Available Not Available Not Available None HIV Retroviridae HIV infection and cell viability assay. [Ref:26026377]HIV: Less effective inhibitor of infection No hemolysis information or data found in the reference(s) presented in this entry [Ref:26026377]Non-toxic or only modestly toxic at the concentrations tested No predicted structure available Linear Free Amination None L Cell Membrane The disruption of the viral envelope and release p24 core protein 2603.1 C120H200N32O32 RNDCKMFTWYOU V 7.02 1 1 0 22 16 0.972 -0.57 30 hours >20 hours >10 hours 159.6 0 0 26026377 "Peptides, 71, 296–303." "VanCompernolle, S., Smith, P. B., Bowie, J. H., Tyler, M. J., Unutmaz, D., & Rollins-Smith, L. A. (2015)." Inhibition of HIV infection by caerin 1 antimicrobial peptides 10.1016/j.peptides.2015.05.004 Anti-HIV DRAVPe02072 FLPVLAGIAAKVVPALFCKITKKC 24 Brevinin-1 "Frog, Rana brevipoda porsa, Japan, Asia" P32423 Experimentally Validated 88447 Not Found Not Available 1to24 Not Available Not Available Not Available Not Available None "HSV-1,HSV-2" Herpesviridae Inhibition assay [Ref:10795591]HSV-1: IC50 = 93.4 µg/mL; HSV-2: IC50 = 89.8 µg/m [Ref:10795591]EC50:13.4 µg/ml [Ref:10795591]CC50=14.4µg/ml No predicted structure available Linear Free Free Brevinin-1 was reduced and alkylated L Cell Membrane "Brevinin-1 has demonstrated antiviral activity against herpes simplex virus (HSV), primarily by targeting the viral envelope and interfering with viral entry" 2527.5 C121H204N28O26S2 RNDQEQMSWYOU AK 99.7 4 0 4 20 14 1.288 -1.19 1.1 hours 3 mins 2 miins 134.17 0 0 10795591 "European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology, 19(3), 187–194." "Yasin, B., Pang, M., Turner, J. S., Cho, Y., Dinh, N. N., Waring, A. J., Lehrer, R. I., & Wagar, E. A. (2000)" Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides 10.1007/s100960050457 Anti-HSV DRAVPe02071 SDSVVSDIICTTFCSVTWCQSNCC 24 Brevicillin Brevibacillus J2FTU4 Experimentally Validated 2825881 PMI05_05757 EJL20520.1 20-43 Not Available AKIX01000128 Genomic DNA Not Available None SARS-CoV-2 Coronaviridae Cell Culture-based Assay [Ref:36914211]SARS-CoV-2: Peptide inhibited ~99% virus growth at 10 µg/mL in cell culture-based assay. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Found 2601.93 C106H165N27O39S5 AREGHLKMPYOU CS 3.56 0 2 -2 24 18 0.662 0.86 1.9 hours >20 hours >10 hours 68.75 5500 2.114 36914211 "Journal of applied microbiology, 134(3), lxad054." "Singh, S. S., Sharma, D., Singh, C., Kumar, S., Singh, P., Sharma, A., Das, D. K., Pinnaka, A. K., Thakur, K. G., Ringe, R. P., & Korpole, S. (2023)" "Brevicillin, a novel lanthipeptide from the genus Brevibacillus with antimicrobial, antifungal, and antiviral activity" 10.1093/jambio/lxad054 Anti-SARS-CoV-2 DRAVPe02070 FIGAIARLLSKIF 13 BmKn2 "venom, Buthus martensii Karsch" No entry found Experimentally Validated 34649 Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Antiviral effect assay [Ref:22536342]HIV-1: BmKn2 and Kn2-7 decreased infectivity of HIV-1 clade B b12-resistant pseudotyped virus CAAN5342 "[Ref22536342] human RBC, HC50 12.5 ug/ml, hemolytic" No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free "While deletions of 1 to 4 residues from the peptide (Kn2-1 to Kn2-6) reduced its activity against S. aureus, peptide Kn2-7 (changes of G3, A4, and S10 to cationic K/R) showed increased activity due to an increase in cationicity. However, C-terminally truncated or cyclic BmKn2 lost activity against N. gonorrhoeae, indicating both the linear and intact sequence are important for peptide activity. " L Not Found "BmKn2 aggregates and inserts into viral envelope so that the hydrophobic peptide region aligns with the lipid core region and the hydrophilic peptide regions form the interior region of the pore, with the help of positive charge of peptide somehow" 1448.81 C71H117N17O15 NDCQEHMPTWYVOU I 11 3 0 3 13 10 1.592 -0.86 1.1 hours 3 mins 2 miins 165.38 0 0 22536342 "PloS one, 7(4), e34947." "Chen, Y., Cao, L., Zhong, M., Zhang, Y., Han, C., Li, Q., Yang, J., Zhou, D., Shi, W., He, B., Liu, F., Yu, J., Sun, Y., Cao, Y., Li, Y., Li, W., Guo, D., Cao, Z., & Yan, H. (2012)." Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7 10.1371/journal.pone.0034947 Anti-HIV-1 DRAVPe02069 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 40 "Beta-amyloid peptide (1–40)" Homo sapiens A0A0A0MRG2##P05067 Experimentally Validated 9606 APP(351) Y00264 672-711 pfam03494 CM000683.2 Genomic DNA "Chromosome21:25,881,673 - 26,112,098" 1AML##1AMC##1BA4 "HSV-1, IAV(H3N1,H1N1)" Orthomyxoviridae inhibition assay [Ref:25376108]HSV-1: Aβ 1-40 and Aβ 1-42 caused 82% and 91% decreases in HSV-1 DNA replication in MRC-5 cells.[Ref:24988208]Influenza A virus (H3N2 - Phil82): βA40 at 16 µg/mL reduced infectivity to 29±12% of control; Cal09 strain: 47±15% of control. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Aβ 1-40 acted directly on HSV-1 in a cell-free system and prevented viral entry into cells.The sequence homology between Aβ and a proximal transmembrane region of HSV-1 glycoprotein B suggested that Aβ interference with HSV-1 replication could involve its insertion into the HSV-1 envelope. 4329.86 C194H295N53O58S1 CPTWOU GV 5.31 3 6 -3 32 24 0.057 0.98 1.1 hours 3 mins >10 hours 90 1490 0.344 25376108##24988208 "Biogerontology, 16(1), 85–98## PloS one, 9(7), e101364." "Bourgade, K., Garneau, H., Giroux, G., Le Page, A. Y., Bocti, C., Dupuis, G., Frost, E. H., & Fülöp, T., Jr (2015)##White, M. R., Kandel, R., Tripathi, S., Condon, D., Qi, L., Taubenberger, J., & Hartshorn, K. L. (2014)." β-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1##Alzheimer's associated β-amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytes 10.1007/s10522-014-9538-8 "Anti-HSV,Anti-IAV" DRAVPe02068 GLFDIIKKIAESF 13 Aurein 1.2 "Southern bell frog Litoria aurea and Litoria raniformis, Australia" P82387  Experimentally Validated 116057 Not Available Not Available 1to13 Not Available Not Available Not Available Not Available 1VM5 HIV-1 Retroviridae Inhibition assay [Ref:9568968]HIV-1: Aurein 1.2 EC₅₀ = 7.7 µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Amidation F13  L Membrane "Aurein 1.2 interacts with membranes and can induce curvature and disintegration, which is crucial for its antimicrobial activity .This mechanism could theoretically be effective against viral membranes, although this has not been extensively studied in the context of HIV" 1480.77 C71H113N15O19 RNCQHMPTWYVOU I 6.07 2 2 0 13 10 0.669 0.12 30 hours >20 hours >10 hours 127.69 0 0 20086159##9568968 "Antimicrobial agents and chemotherapy, 54(3), 1343–1346##The Journal of general virology, 79 ( Pt 4), 731–740" "Wang, G., Watson, K. M., Peterkofsky, A., & Buckheit, R. W., Jr (2010)##Wachinger, M., Kleinschmidt, A., Winder, D., von Pechmann, N., Ludvigsen, A., Neumann, M., Holle, R., Salmons, B., Erfle, V., & Brack-Werner, R. (1998)" Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database##Antimicrobial peptides melittin and cecropin inhibit replication of human immunodeficiency virus 1 by suppressing viral gene expression 10.1128/AAC.01448-09##10.1099/0022-1317-79-4-731 Anti-HIV-1 DRAVPe02067 GRFKRFRKKFKKLFKKLSPVIPLLHLG 27 BMAP-27 "Cattle, Bos taurus" P54228 Experimentally Validated 9913 CATHL6(317651) X97608.1 132-158 Not Available X97608 mRNA "Chromosome 22(NC_037349.1 (51663351..51665275, complement))" 2KET HIV-1 Retroviridae Inhibition assay [Ref:18591279]HIV-1: BMAP-27 blocks HIV-1 infection "[Ref:18591279]HC50>100 uM to hRBC (3.5% hemolysis at 3 uM; 32.7% hemolysis at 100 uM), but not hemo.lytic to bovine RBC even at 100 uM. Thus, hemolysis is related to cell sources, indicating the need " No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Carboxylation Amidation  a 26mer was mad with a hydrophobic tail L Membrane inhibit viral replication 3283.15 C160H265N45O29 ANDCQEMTWYOU K 12.32 10 0 10 20 14 -0.367 1.64 30 hours >20 hours >10 hours 97.41 0 0 18591279 "Antimicrobial agents and chemotherapy, 52(9), 3438–3440." "Wang, G., Watson, K. M., & Buckheit, R. W., Jr (2008)." Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins 10.1128/AAC.00452-08 Anti-HIV-1 DRAVPe02066 GFGCPLDQMQCHNHCQSVRYRGGYCTNFLKMTCKCY 36 Av-LCTX-An1a venom gland of the A. nagpag spider A0A5Q1NCA8 Experimentally Validated 2664917 Not Found QGD15041.1 25-60 NF038042##pfam01097 MN319466 mRNA Not Available None "DENV-2,ZIKV" Flaviviridae protease inhibition assay [Ref:31658707]Dengue virus-2 (DENV2): An1a showed ~10 µM 50% inhibition in Vero cells.Zika virus (ZIKV):An1a showed ~2 µM 50% inhibition in Vero cells. It acts as a competitive inhibitor of ZIKV NS2B–NS3 protease (Ki = 12.54 ± 1.88 µM). Inhibited replication in HUVEC and A549 cells.DENV2 and ZIKV NS2B–NS3 protease: Ki = 9.47 µM for DENV2; Ki = 12.54 µM for ZIKV. [Ref:31658707]hemolytic: no hemolysis of hRBC below 20 uM No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free "Gly4–Ser–Gly4 linker," L Protease An1a suppresses DENV2 replication and infectious virus production.Also An1a may inhibit DENV2 replication and particle production by interacting with the NS2B–NS3 protease. 4193.919 C177H269N51O50S8 AEIWOU C 8.65 4 1 3 24 18 -0.481 1.71 30 hours >20 hours >10 hours 29.72 4845 1.55 31658707 "Toxins, 11(10), 584. " "Ji, M., Zhu, T., Xing, M., Luan, N., Mwangi, J., Yan, X., Mo, G., Rong, M., Li, B., Lai, R., & Jin, L. (2019)." An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B-NS3 Protease of Flaviviruses 10.3390/toxins11100584 "Anti-DENV-2,ANTi-ZIKV" DRAVPe02126 XYXTAGXAXLXPXQXKXVXGX 11 Mirabamide G  sponge Stelletta clavosa No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Neutralization Assays. [Ref:21280591]HIV-1:IC50=68±13μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic "The N-terminal is blocked by the Dhtda-like moiety," Free "X at position 1 is β-O-methyltyrosine (β-OMeTyr).X at position 2 is N-methylthreonine (NMeThr).X at position 5 is 3-O-methylalanine (3-OMeAla).X at position 6 is 3-hydroxyleucine (3-OHLeu).X at position 7 is 4 chlorohydroxyproline (4-ClHpr).X at position 8 is 3,4-dimethylglutamine (3,4-DiMeGln).X at position 9 is diaminobutyric acid (Dab).X at position 10 is aminobutyric acid (Aba)" L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 1104.27 C66H103ClN13O20 RNDCEIMFSWOU A 8.59 1 0 1 6 6 -0.018 0.92 2.8 hours 10 min 2 min 80 1490 1.349 21280591 J Nat Prod. 2011 Feb 25;74(2):185-93. "Lu Z, Van Wagoner RM, Harper MK, Baker HL, Hooper JN, Bewley CA, Ireland CM." "Mirabamides E-H, HIV-Inhibitory Depsipeptides from the Sponge Stelletta clavosa" 10.1021/np100613p Anti-HIV-1 DRAVPe02127 XYXTAGXAXLXPXQXKXVXG 11 Mirabamide H  sponge Stelletta clavosa No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Neutralization Assays. [Ref:21280591]HIV-1:IC50=42±5μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic "The N-terminal is blocked, likely due to structural truncation involving the Dhtda-like group." Free "X at position 1: β-O-methyltyrosine (β-OMeTyr).X at position 2: N-methylthreonine (NMeThr).X at position 5: 3-O-methylalanine (3-OMeAla).X at position 6: 3-hydroxyleucine (3-OHLeu).X at position 7: 4-chlorohydroxyproline (4-ClHpr) .X at position 8: 3,4-dimethylglutamine (3,4-DiMeGln).X at position 9: Diaminobutyric acid (Dab).X at position 10: Aminobutyric acid (Aba) " L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 1104.27 C66H103ClN13O19 RNDCEIMFSWOU A 8.59 1 0 1 6 6 -0.018 0.92 2.8 hours 10 min 2 min 80 1490 1.349 21280591 J Nat Prod. 2011 Feb 25;74(2):185-93. "Lu Z, Van Wagoner RM, Harper MK, Baker HL, Hooper JN, Bewley CA, Ireland CM." "Mirabamides E-H, HIV-Inhibitory Depsipeptides from the Sponge Stelletta clavosa" 10.1021/np100613p Anti-HIV-1 DRAVPe02128 XAXYXQLGXATXQXKXQXNH 12 Stellettapeptin A  Isolated from Stelletta sponge No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV integrase inhibition assay [Ref:26139946]HIV-1:EC50=23nM No hemolysis information or data found in the reference(s) presented in this entry [Ref:26139946]CC50: 367 nM No predicted structure available Cyclic "The N-terminal residue in both peptides is Hdna (3-hydroxy-6,8-dimethylnon-4-enoic acid), a unique polyketide moiety. This polyketide is linked to the peptide chain through the 3-OHAsn residue in Stel" "C-terminal is esterified to a threonine hydroxyl group, forming a cyclic structure. This ester bond is a defining feature of these cyclic depsipeptides." "Contains 3-OHGln and 3-OHAsn residues, rarely found in peptides.Macrocycle closure via esterification.X at position 1: N-methylalanine (NMeAla) → A (Alanine with an additional methyl group on the nitrogen),X at position 2: β-O-methyltyrosine (β-OMeTyr) → Y (Tyrosine with a methyl group on the hydroxyl group),X at position 3: N-methylglutamine (NMeGln) → Q (Glutamine with an additional methyl group on the nitrogen),X at position 4: Leucine (Unmodified),X at position 5: Glycine (Unmodified),X at p" L Viral entry (Viral membrane) "The cyclic structure and amphipathic nature of these peptides likely enable interaction with the lipid bilayer of viral or host cell membranes.This interaction may disrupt the membrane integrity, inhibiting viral entry or replication.The peptides may interact with HIV-1 envelope proteins, preventing the virus from attaching or fusing with host cells.Some depsipeptides are known to inhibit the reverse transcriptase enzyme of HIV-1, disrupting the viral replication process.By binding to host or viral targets, the peptides may alter immune responses to enhance antiviral effects" 1358.48 C58H91N19O19 RDCEIMFPSWVOU Q 8.64 1 0 1 10 8 -1.342 1.04 4.4 hours >20 hour >10 hours 49.17 1490 1.097 26139946 2015 Jul 8;56(28):4215-4219. "Shin HJ, Rashid MA, Cartner LK, Bokesch HR, Wilson JA, McMahon JB, Gustafson KR. " "Stellettapeptins A and B, HIV-inhibitory cyclic depsipeptides from the marine sponge Stelletta sp" 10.1016/j.tetlet.2015.05.058 Anti-HIV-1 DRAVPe02129 XAXYXTLGGXATTXQXKXH 12 Stellettapeptin B  Isolated from Stelletta sponge No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV integrase inhibition assay [Ref:26139946]HIV-1:EC50=27nM No hemolysis information or data found in the reference(s) presented in this entry [Ref:26139946]CC50: 367nM No predicted structure available Cyclic "The N-terminal residue in both peptides is Hdna (3-hydroxy-6,8-dimethylnon-4-enoic acid), a unique polyketide moiety. This polyketide is linked to the peptide chain through the 3-OHAsn residue in Stel" "C-terminal is esterified to a threonine hydroxyl group, forming a cyclic structure. This ester bond is a defining feature of these cyclic depsipeptides." "Replaces NMeGln, 3-OHGln, and 3-OHAsn from A with NMeThr, Thr, and Gly, respectively. Similar macrocycle.X at position 1: N-methylalanine (NMeAla) → A,X at position 2: β-O-methyltyrosine (β-OMeTyr) → Y,X at position 5: 3-O-methylalanine (3-OMeAla) → A,X at position 6: Threonine (Thr) → T,X at position 8: 3,4-dimethylglutamine (3,4-DiMeGln) → Q,X at position 9: Diaminobutyric acid (Dab) → K,X at position 10: Histidine (Hdna) → H" L Viral entry (Viral membrane) "The cyclic structure and amphipathic nature of these peptides likely enable interaction with the lipid bilayer of viral or host cell membranes.This interaction may disrupt the membrane integrity, inhibiting viral entry or replication.The peptides may interact with HIV-1 envelope proteins, preventing the virus from attaching or fusing with host cells.Some depsipeptides are known to inhibit the reverse transcriptase enzyme of HIV-1, disrupting the viral replication process.By binding to host or viral targets, the peptides may alter immune responses to enhance antiviral effects" 1247.37 C54H86N16O18 RNDCEIMFPSWVOU T 8.44 1 0 1 9 7 -0.617 1 4.4 hours >20 hour >10 hours 49.17 1490 1.195 26139946 2015 Jul 8;56(28):4215-4219. "Shin HJ, Rashid MA, Cartner LK, Bokesch HR, Wilson JA, McMahon JB, Gustafson KR. " "Stellettapeptins A and B, HIV-inhibitory cyclic depsipeptides from the marine sponge Stelletta sp" 10.1016/j.tetlet.2015.05.058 Anti-HIV-1 DRAVPe02130 XFPSLTCLSTXC 10 Mollamide E Tunicate Didemnum molle PNG07-2-050 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV integrase inhibition assay and cytoprotective cell-based assay [Ref:22845329]HIV-1:No inhibition at78μM;NoHIV integrase inhibition at 100μg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Phenylalanine (Phe) Thiazoline (Cys-derived residue) "The cysteine residue forms a thiazoline ring, contributing to the rigidity and cyclic nature of the peptide.Attached to the threonine residue, this modification is a unique structural feature.Contains d-Phe and d-thiazoline, resulting from thermodynamic relaxation under constrained peptide geometry.X at position 1: D-Phenylalanine (D-Phe) → Mirror image of L-Phe, not commonly found in natural peptides, X at position 7: D-Cysteine in thiazoline ring → Modified residue, involved in heterocyclic st" L Viral integrase "Mollamide E does not exhibit significant HIV inhibition activity in cytoprotective or integrase assays. Its mechanism of action remains uncharacterized but may involve steric or structural features that prevent integrase binding, unlike its analog Mollamide F" 1071.27 C35H50N6O7S ARNDQEGHIKMWYVOU CLST 5.51 0 0 0 8 8 1.08 0.96 1.1hours 3 min 2 min 78 0 0 22845329 J Nat Prod. 2012 Aug 24;75(8):1436-40. "Lu Z, Harper MK, Pond CD, Barrows LR, Ireland CM, Van Wagoner RM." Thiazoline Peptides and a Tris-Phenethyl Urea from Didemnum molle with Anti-HIV Activity 10.1021/np300270p Anti-HIV-1 DRAVPe02131 XFPPVIXC 6 Mollamide F Tunicate Didemnum molle PNG07-2-050 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV integrase inhibition assay and cytoprotective cell-based assay [Ref:22845329]HIV-1:IC50=78μM;HIV integrase IC50=39μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Phenylalanine (Phe) Thiazoline (Cys-derived residue) "Similar to Mollamide E, it contains a thiazoline ring derived from cysteine.The sequence includes two proline residues, with a cis geometry at the Pro-Pro peptide bond.Contains d-Phe and d-thiazoline, similar to Mollamide E, due to stereochemical lability. Unlike Mollamide E, the reversed isoprene group is missing, which impacts its structural dynamics and activity.X at position 1: D-Phenylalanine (D-Phe) → This is a D-isomer, which is not naturally common in ribosomally synthesized peptides.X a" L Viral integrase "Mollamide F inhibits HIV-1 integrase with an IC50 value of 39 µM, suggesting it interacts with integrase's active site. Residues in the ""southern region"" of the peptide are crucial for binding. The thiazoline moiety likely contributes to molecular rigidity and facilitates integrase interaction." 674.86 C33H46N6O5S ARNDQEGHLKMSTWTOU P 5.52 0 0 0 6 6 1.8 0.88 1.1 hours 3 min 2 min 113.33 0 0 22845329 J Nat Prod. 2012 Aug 24;75(8):1436-40. "Lu Z, Harper MK, Pond CD, Barrows LR, Ireland CM, Van Wagoner RM." Thiazoline Peptides and a Tris-Phenethyl Urea from Didemnum molle with Anti-HIV Activity 10.1021/np300270p Anti-HIV-1 DRAVPe02132 EISKINTTLLDLSDEMAMLQQEVVKQLNDSYIDLKEL 37 HKU4-HR2P2 HR2 domain of bat No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MERS-CoV , SARS-CoV." Coronaviridae Time-of-addition assay "[Ref:30646495]MERS-CoV,SARS-CoV:IC50=0.38μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Linear Free Free None L HR2  HKU4-HR2 peptides could cross-target the MERS-CoV HR1 region. 4281.9 C186H311N45O65S2 RCGHFPWOU L 4.07 3 8 5 22 18 -0.222 0.9185 1 hour 30 min >10 hours 123.78 1490 0.348 30646495 "Viruses, 11(1), 56." "Xia, S., Lan, Q., Pu, J., Wang, C., Liu, Z., Xu, W., Wang, Q., Liu, H., Jiang, S., & Lu, L. (2019). " Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4 10.3390/v11010056 "Anti-MERS-CoV,Anti-SARS-CoV" DRAVPe02133 XCXCVXLL 6 Malformin C marine-derived fungus Aspergillus niger SCSIO Jcsw6F30 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV integrase inhibition assay [Ref:26711143]HIV-1:IC50=1.4±0.06μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:26711143]No cytotoxicity No predicted structure available Cyclic Free Free "X1 at position 1: D-Cys → Cysteine in D-configuration (mirror image of natural L-Cys),X2 at position 2: D-Cys → D-isomer of Cysteine,X at position 4: D-Leu → Leucine in D-form,Cyclic structure: The peptide is cyclized, forming a closed ring via peptide bonds, often enhancing stability and bioactivity." L Not found Not Available 529.2392 C23H39N5O5S2 CL 0 0 0 0 5 5 3.36 0.72 1.2 hours >20 hour >10 hours 214 0 0 26711143 "Bioorganic & medicinal chemistry letters, 26(2), 361–365." "Zhou, X., Fang, W., Tan, S., Lin, X., Xun, T., Yang, B., Liu, S., & Liu, Y. (2016)" Aspernigrins with anti-HIV-1 activities from the marine-derived fungus Aspergillus nigerSCSIO Jcsw6F30 10.1016/j.bmcl.2015.12.005 Anti-HIV-1 DRAVPe02134 GENFAISKINTTLLDISDEMAMIQEVVKQLNDSYI 35 HKU4-HR2P1 HR2 domain of bat No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref:30646495]SARS-CoV:IC50=1.09μM No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Linear Free Free None L HR2  These peptides target the viral fusion and entry stages. 3944.48 C172H280N42O59S2 RCHPWOU I 4.02 2 6 -4 22 18 0.02 0.9185 30 hours >20 hour >10 hours 111.43 1490 0.378 30646495 "Viruses, 11(1), 56." "Xia, S., Lan, Q., Pu, J., Wang, C., Liu, Z., Xu, W., Wang, Q., Liu, H., Jiang, S., & Lu, L. (2019). " Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU6 10.3390/v11010058 Anti-MERS-CoV DRAVPe02135 ECASTCSFGIVTIVCDGTTK 20 Divamide A TunicateDidemnum molle E11-036 A0A2H4GZ80 Experimentally Validated 1216 divA ARD09202.1 72-91 Not Available KY115608 Genomic DNA Not Available None HIV-1 Retroviridae HIV assay [Ref:29291350]HIV-1:IC50=0.225μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:29291350]CC50=2.63µm No predicted structure available Cyclic Free Free the tertiary structure conferred by the cyclic lysinoalanine residue is necessary to block infection L PE binding " duramycin inhibits entry of Ebola and Dengue viruses, indicating that TIM proteins also interact with PE.Thus, lipid binding appears a likely mechanism for the anti-HIV activity of the divamides. However, the stark differences in potency and toxicity between individual divamides and 4 may reflect additional interactions with non-membrane components, potentially including TIM proteins, that are substantially affected by the peptide sequence. " 2035.33 C84H139N21O31S3 RNQHMWYOU T 4.37 1 2 -1 16 14 0.671 0.9576 1 hour 3 min >10 hours 73 0 0 29291350 Nat Chem Biol. 2018 Feb;14(2):179-185. "Smith TE, Pond CD, Pierce E, Harmer ZP, Kwan J, Zachariah MM, Harper MK, Wyche TP, Matainaho TK, Bugni TS, Barrows LR, Ireland CM, Schmidt EW." Accessing chemical diversity from the uncultivated symbionts of small marine animals 10.1038/nchembio.2537 Anti-HIV-1 DRAVPe02136 2Abz-A-xiIle-N(Me)Phe(bS-OH) 3 Asperterrestide A marine-derived fungus Aspergillus terreus SCSGAF0162. No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None H1N1/H3N2 Orthomyxoviridae HIV assay "[Ref:23806112]H1N1:IC50=20.2μM,H3N2:IC50=0.41μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:23806112]Negligible cytotoxicity No predicted structure available Cyclic Free Free 2Abz at position 1: 2-Aminobenzoyl (Aromatic modification).D-Ala at position2:D-Alanine (Natural enantiomer of alanine).D-xiIle at position 3:D-X-isoleucine (Modified or non-standard isoleucine).D-N(Me)Phe at position 4:D-N-Methylphenylalanine (Methyl group added to the nitrogen of phenylalanine).bS-OH at position5:b-Sulfhydroxyphenylalanine (Phenylalanine derivative with a hydroxyl group attached to a sulfur atom. L Not found Not Available 480.6 g/mol C12H15N5O2 RNDECQMFPSTWYVOU A 6 0 0 0 1 4 2.65 -0.67 4 hours >20 hour >10 hours 85 0 0 23806112 "Journal of natural products, 76(6), 1182–1186." "He, F., Bao, J., Zhang, X. Y., Tu, Z. C., Shi, Y. M., & Qi, S. H. (2013)." "Asperterrestide A, a cytotoxic cyclic tetrapeptide from the marine-derived fungus Aspergillus terreus SCSGAF0162" 10.1021/np300897v "Anti-H1N1,Anti-H3N2" DRAVPe02137 VXYXYXYP 5 Aspergillipeptide D Endophytic fungus Aspergillus sp. SCSIO 41501 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae plaque reduction assay. "[Ref:32192525]HSV-1:IC50=9.5μM,HSV-1:IC50=12.5μM(ACV-HSV-1)" No hemolysis information or data found in the reference(s) presented in this entry [Ref:32192525]Negligible cytotoxicity No predicted structure available Cyclic Free Free "X at position 2: N-methyltyrosine (N-Me-Tyr) → Y (Tyrosine with a methyl group on the nitrogen),X at position 3: O-methyltyrosine (O-Me-Tyr) → Y (Tyrosine with a methyl group on the hydroxyl group),X at position 4: O-methyltyrosine (O-Me-Tyr) → Y (Tyrosine with a methyl group on the hydroxyl group)" L Glycoprotein. " Aspergillipeptide D did not affect HSV-1 early infection events, including viral inactivation, attachment and penetration. Interestingly, Aspergillipeptide D dramatically reduced both the gene and protein levels of viral late protein gB, and suppressed its location in the endoplasmic reticulum and Golgi apparatus.n contrast, overexpression of gB restored viral production. Finally, proteomic analysis revealed that the numbers of cellular proteins that interacted with gB protein was largely decreased by Aspergillipeptide D. These results suggested that Aspergillipeptide D inhibited gB function to affect HSV-1 intercellular spread." 727.859 g/mol C40H49N5O8 ARNDCQWMFSTWOU Y 5.49 0 0 0 5 5 -0.26 0.84 100 hours >20 hour >10 hours 58 1470 6.351 32192525 "Virology journal, 17(1), 41. " "Wang, Z., Jia, J., Wang, L., Li, F., Wang, Y., Jiang, Y., Song, X., Qin, S., Zheng, K., Ye, J., Ren, Z., Wang, Y., & Qi, S. (2020). " Antiviral peptides from marine gorgonian-derived fungus Aspergillus sp. SCSIO 41501 10.1186/s12985-020-01315-z Anti-HSV-1 DRAVPe02138 YWV 3 Aspergillipeptide E Endophytic fungus Aspergillus sp. SCSIO 41501 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae plaque reduction assay. [Ref:32192525]HSV-1:IC50=19.8μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:32192525]Negligible cytotoxicity No predicted structure available Linear Free Free "The configurations of Tyr and Val have been determined as D-Tyr and D-Val, while Trp is speculated to be L-Trp based on the precursor added." L Glycoprotein. Not Available Not inlcuded yet C26H36N4O7 ARNDCQEMFPSVOU Y 0 0 0 0 3 3 0 0.56 0 0 0 0 0 0 32192525 "Virology journal, 17(1), 41. " "Wang, Z., Jia, J., Wang, L., Li, F., Wang, Y., Jiang, Y., Song, X., Qin, S., Zheng, K., Ye, J., Ren, Z., Wang, Y., & Qi, S. (2020). " Antiviral peptides from marine gorgonian-derived fungus Aspergillus sp. SCSIO 41501 10.1186/s12985-020-01315-z Anti-HSV-1 DRAVPe02139 XIXYQPXAXTX 6 Simplicilliumtide J Fungus Simplicillium obclavatum EIODSF 0210 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Anti-HSV-Assay [Ref:28578573]HSV-1:IC50=14.1μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free "X at position 1: allo-Ile,X at position 2: D-Tyr,X at position 5: D-Ala,X at position 6: D-allo-Thr,X at position 7: 5(S)-HTA (non-standard residue)" L Not found Not Available 691.78 C25H30N4O5 RNDCEGHLKMFSVOU A 5.52 0 0 0 6 6 -0.133 0.92 20 hour 30 min >10 hours 81.67 1490 2.154 28578573 "Journal of agricultural and food chemistry, 65(25), 5114–5121." "Liang, X., Nong, X. H., Huang, Z. H., & Qi, S. H. (2017)." Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020  10.1021/acs.jafc.7b01238 Anti-HSV-1 DRAVPe02140 SAPQYV 6 Verlameline A Fungus Simplicillium obclavatum EIODSF 0210 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Anti-HSV-Assay [Ref:28578573]HSV-1:IC50=16.7μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic A 5-hydroxytetradecanoic acid (HTDA) is attached to the N-terminus — this makes the compound a lipopeptide. Free "Macrocyclic lactone ring:The hydroxyl group at C-5 of HTDA is ester-linked to the C-terminal carboxyl of Val, forming a cyclic structure." L Not found Not Available 663.73 C45H71N7O11 RNDCEGHLKMFSVOU Q 5.24 0 0 0 6 6 -0.2 92 1.9 hours >20 hour >10 hours 65 1490 2.254 28578573 "Journal of agricultural and food chemistry, 65(25), 5114–5121" "Liang, X., Nong, X. H., Huang, Z. H., & Qi, S. H. (2017)" Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020 10.1021/acs.jafc.7b01238 Anti-HSV-1 DRAVPe02141 FLSX₃ 3 Acremonpeptide A Fungus Acremonium persicinum SCSIO 115 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HSV-1,HSV-2" Herpesviridae Vitro Bioassay "[Ref:31503476]HSV-1:IC50=16μM,HSV-1:EC50=8.7μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free "X = Modified ornithine (specifically N5-acetyl-N5-hydroxy-Orn, repeated three times)" L Cell membrane Viral Replication 365.19 C39H61N9O13 ARNDCQEMPWVOU FLS 5.9 0 0 0 1 2 1.93 0.46 1.1 hours 20 mins 10 mins 81.6 0 0 31503476 "Journal of natural products, 82(9), 2594–2600." "Luo, M., Zang, R., Wang, X., Chen, Z., Song, X., Ju, J., & Huang, H. (2019)." Natural Hydroxamate-Containing Siderophore Acremonpeptides A-D and an Aluminum Complex of Acremonpeptide D from the Marine-Derived Acremonium persicinum SCSIO 115 10.1021/acs.jnatprod.9b00545 "Anti-HSV-1,Anti-HSV-2" DRAVPe02142 FLWXOX 4 Al(III)-acremonpeptide D Fungus Acremonium persicinum SCSIO 115 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Anti-HSV-Assay [Ref:31503476]HSV-1:IC50=14μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free X = AcN(OH)Orn L Cell membrane Viral replication 578.3 C47H63AlN10O12 ARNDCQEMPSVOU FLW 9.9 1 0 1 2 2 1.18 1.95 30 hours >20 hours >10 hours 87.5 0 0 31503476 "Journal of natural products, 82(9), 2594–2600." "Luo, M., Zang, R., Wang, X., Chen, Z., Song, X., Ju, J., & Huang, H. (2019)." Natural Hydroxamate-Containing Siderophore Acremonpeptides A-D and an Aluminum Complex of Acremonpeptide D from the Marine-Derived Acremonium persicinum SCSIO 115 10.1021/acs.jnatprod.9b00545 Anti-HSV-1 DRAVPe02143 QSVACRSYYCSKFCGSAGCSLYGCYLLHPGKICYCLHCSR 40 Myticin C Mollusk Mytilus galloprovincialis A7DWR7 Experimentally Validated 29158 mync_MYTGA Not Available 21-60 Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Anti-HSV-Assay "[Ref:27307570]HSV-1:IC50=7.69–8.21μM,HSV-1:IC50=8.32–10.5μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not found The intracellular phase of viral replication 4432.2 C191H289N53O53S8 NDEMTWOU C 8.71 4 0 4 12 18 0.227 0.9185 0.8 hours 10 min 10 hours 61 7450 1.681 27307570 "Journal of virology, 90(17), 7692–7702." "Novoa, B., Romero, A., Álvarez, Á. L., Moreira, R., Pereiro, P., Costa, M. M., Dios, S., Estepa, A., Parra, F., & Figueras, A. (2016)." Antiviral Activity of Myticin C Peptide from Mussel: an Ancient Defense against Herpesviruses 10.1128/JVI.00591-16 Anti-HSV-1 DRAVPe02144 HTASDAAAAAALTAANAAAAAAASMA 26 Pa-MAP polar fish Pleuronectes americanus No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Anti-HSV-Assay "[Ref:27161201]HSV-1:IC50=82%(45μM),HSV-1:IC50=90%(23μM)" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:27161201]Pa-MAP did not reach the concentrations that allowed 50% of cellular viability (CC50), since there were already 80% of viable cells in the first dilution. Even though some peptides showe" No predicted structure available Cyclic Free Free None L Membrane "Pa-MAP could possible interact with the viral envelope and the phospholipids of the viral surface, due to the presence of hydrophobic amino acid residues.22 According to such data, further tests were performed in this study to define Pa-MAP’s antiviral mechanism of action. It was verified that this peptide has a virucidal action,like most antiviral peptides described in the literature,13 inhibiting the virus’ action before adsorption, at a percentage above 80%, reinforcing the theory presented by Migliolo et al.,22 and the SI was higher than 5 considering the CC50 at 400 mg." 2213.41 C90H149N29O34S1 RCQEGIKFPWYVOU A 5.08 0 1 -1 22 18 0.888 0.9185 3.5 hours 10 min >10 hours 80.38 0 0 27161201 "Biopolymers, 108(2), 10.1002/bip.22871." "Vilas Boas, L. C., de Lima, L. M., Migliolo, L., Mendes, G. D., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2017)." Linear antimicrobial peptides with activity against herpes simplex virus 1 and Aichi virus 10.1002/bip.22871 Anti-HSV-1 DRAVPe02145 YP 2 Cyclo(l-Tyr-l-Pro) diketopiperazine Endophytic fungus Aspergillus versicolor No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Herpesviridae Anti-HSV-Assay [Ref:Not Available]HCV:IC50: 8.2 μg mL−1 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L NS3-4A protease interact with the viral envelope and the phospholipids of the Not inlcuded yet Not includedd yet Not included ye Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet 2 2 Not inlcuded yet 0.8 Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not inlcuded yet Not Available "Applied Biochemistry and Microbiology, 53(1), 101-106." "Ahmed, Eman; Rateb, Mostafa; El-Kassem, L.T. Abou ; Hawas, Usama" Anti-HCV protease of diketopiperazines produced by the Red Sea sponge-associated fungus Aspergillus versicolor 10.1134/S0003683817010021 Anti-HCV DRAVPe02146 AVVVDAVVVDAVVVDAVVVD 20 Valinomycin; streptodepsipeptides P11A and SV21 Bacterial symbiont Streptomyces sp. SV21 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Herpesviridae Anti-HCV assay [Ref:33540548]HCV:IC50=0–5% No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not found "viral surface, due to the presence of hydrophobic amino acid" 1952.28 C54H90N6O18 RNCQEGHHILKMFPSTWYOU V 3.32 0 4 -4 12 10 2.18 0.96 4.4 hours >20 hours >10 hours 194 0 0 33540548 " Marine drugs, 19(2), 81." "Wibowo, J. T., Kellermann, M. Y., Köck, M., Putra, M. Y., Murniasih, T., Mohr, K. I., Wink, J., Praditya, D. F., Steinmann, E., & Schupp, P. J. (2021). " "Anti-Infective and Antiviral Activity of Valinomycin and Its Analogues from a Sea Cucumber-Associated Bacterium, Streptomyces sp. SV 21" 10.3390/md19020081 Anti-HCV DRAVPe02147 SITQINTTLLDTTYEMISIQQVVKALNESYIDLKEL 36 MERS-HR2P HR2 domain of bat No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Cell–Cell Fusion Assay [Ref:30646495]SARS-CoV:IC50=1.07μM No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Linear Free Free None L HR2  These peptides target the viral fusion and entry stages. 4129.73 C183H303N43O62S1 RCGHFPWOU ILT 4.18 2 5 -3 22 18 0.064 0.9185 1.9 hours >20 hour >10 hours 127.22 2980 0.722 33082259 "mBio, 11(5), e01935-20." "Outlaw, V. K., Bovier, F. T., Mears, M. C., Cajimat, M. N., Zhu, Y., Lin, M. J., Addetia, A., Lieberman, N. A. P., Peddu, V., Xie, X., Shi, P. Y., Greninger, A. L., Gellman, S. H., Bente, D. A., Moscona, A., & Porotto, M. (2020)." Inhibition of Coronavirus Entry In Vitro and Ex Vivoby a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain 10.1128/mBio.01935-20 Anti-MERS-CoV DRAVPe02148 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSGSGCTEG 45 SARS-CoV-2 HRC C-terminal HR domain of SARS-CoV-2 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "SARS-CoV-2 ,MERS-CoV" Coronaviridae cell-cell fusion assay [Ref:20032190]SARS-CoV:IC50≈3nM and ~6nM No hemolysis information or data found in the reference(s) presented in this entry [Ref:20032190]No toxicity was observed for the SARS-CoV-2 lipopeptide at its IC90 concentration No predicted structure available Cyclic Free Chlo None L Not found Not Available 4744.22 C198H333N57O75S1 MFPWTOU NILS 4.12 3 8 -5 22 18 -0.251 0.9185 1.1 hours 3 min >10 hours 110.44 0 0 20032190 "Journal of virology, 84(5), 2511–2521." "O'Keefe, B. R., Giomarelli, B., Barnard, D. L., Shenoy, S. R., Chan, P. K., McMahon, J. B., Palmer, K. E., Barnett, B. W., Meyerholz, D. K., Wohlford-Lenane, C. L., & McCray, P. B., Jr (2010)" Broad-spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae 10.1128/JVI.02322-09 Anti-SARS-CoV-2 DRAVPe02149 LDLSDEMAMIEVVKQLNDSYIDLKELSNYTYYNKW 35 HKU4-HR2P3  HR2 domain of bat No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae Time-of-addition assay [Ref:30646495]SARS-CoV:IC50=0.55μM No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Cyclic Free Free None L HR2  These peptides target the viral fusion and entry stages. 4245.78 C191H291N43O62S2 RCGHFPOU L 4.14 3 7 -4 22 18 -0.497 0.91 5.5 hours 3 min 2 min 97.43 11460 2.699 30646495 "Viruses, 11(1), 56." "Xia, S., Lan, Q., Pu, J., Wang, C., Liu, Z., Xu, W., Wang, Q., Liu, H., Jiang, S., & Lu, L. (2019). " Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU5 10.3390/v11010057 Anti-MERS-CoV DRAVPe02150 GVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQ 40 NP-1 HR1 region of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 892-931 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" "1WYY, 5WRG, 5X58, 5X5B, 5XLR, 5ZVM, 6ACC, 6ACD" SARS-CoV Coronaviridae antiviral Assay [Ref:15043961]SARS-CoV:Marginal activity at 50μmol/L No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Glycoprotein. Gp41 "like most antiviral peptides described in the literature,13 inhibi-" 4408.93 C191H316N54O65 RDCHMPWOU LN 8.43 3 2 1 22 18 -0.497 0.918 30 hours >20 hour >10 hours 90.25 1490 0.338 15043961 "Lancet (London, England), 363(9413), 938–947." "Liu, S., Xiao, G., Chen, Y., He, Y., Niu, J., Escalante, C. R., Xiong, H., Farmar, J., Debnath, A. K., Tien, P., & Jiang, S. (2004). " Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors 10.1016/S0140-6736(04)15788-7 Anti-SARS-CoV DRAVPe02151 SGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 34 N/A HR segment of SARS-CoV P0DTC2 Experimentally Validated 2697049 S2(43740568) QHD43416.1 1170-1203 Not Available MN908947.3 Genomic RNA "Chromosome:21,563 - 25,384" 6LVN##6LXT##6LZG SARS-CoV-2 Coronaviridae antiviral Assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic N-terminal leucine/isoleucine zipper-like sequence C-terminal heptad repeat located upstream None L Glycoprotein. Gp41 "ting the virus’ action before adsorption, at a percentage above" 3780.25 C162H276N46O57 RDCHMPWOU NL 4.36 3 6 -3 22 18 -0.218 0.9 1.9 hours >20 hour >10 hours 134.71 0 0 14499001 "BMC microbiology, 3, 20." "Kliger, Y., & Levanon, E. Y. (2003)." Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy 10.1186/1471-2180-3-20 Anti-SARS-CoV DRAVPe02152 PTTFMLKYDENGTITDAVDC 20 P2 S1 subunit of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 259-278 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" None SARS-CoV-2 Coronaviridae antiviral Assay [Ref:15918330]SARS-CoV:IC50=112.5±26.3μg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not found "80%, reinforcing the theory presented by Migliolo et al.,22 and" 2234.48 C96H148N22O35S2 RQSWOU T 3.84 1 4 -3 16 14 -0.3 0.95 >20 hour >20 hour Unknown 58.5 1490 0.667 15918330 "Antiviral therapy, 10(3), 393–403." "Zheng, B. J., Guan, Y., Hez, M. L., Sun, H., Du, L., Zheng, Y., Wong, K. L., Chen, H., Chen, Y., Lu, L., Tanner, J. A., Watt, R. M., Niccolai, N., Bernini, A., Spiga, O., Woo, P. C., Kung, H. F., Yuen, K. Y., & Huang, J. D. (2005)." Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus Not Available Anti-SARS-CoV DRAVPe02153 YQDVNCTDVSTAIHADQLTP 20 P6 S1 subunit of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 598-617 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" None SARS-CoV-2 Coronaviridae antiviral Assay [Ref:15918330]SARS-CoV:IC50=113.0±27.6μg/mL No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not found the SI was higher than 5 considering the CC50 at 400 mg. 2191.35 C92H143N25O35S1 RQSWOU DT 3.93 0 3 -3 16 14 -0.36 0.9576 2.8 hours 10 min 2 min 78 1490 0.68 15918330 "Antiviral therapy, 10(3), 393–403." "Zheng, B. J., Guan, Y., Hez, M. L., Sun, H., Du, L., Zheng, Y., Wong, K. L., Chen, H., Chen, Y., Lu, L., Tanner, J. A., Watt, R. M., Niccolai, N., Bernini, A., Spiga, O., Woo, P. C., Kung, H. F., Yuen, K. Y., & Huang, J. D. (2005)." Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus Not Available Anti-SARS-CoV DRAVPe02154 STSQKSIVAYTM 12 SP-10 S protein of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 668-679 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" "1WYY, 5WRG, 5X58, 5X5B, 5XLR, 5ZVM, 6ACC, 6ACD" SARS-CoV Coronaviridae Biotinylated enzyme-linked immunosorbent assay [Ref:16337697]SARS-CoV:IC50=1.88±0.52nmol No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L S protein to ACE2  Significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay.SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. 1315.5 C56H94N14O20S1 RNDCEGHLFPWOU S 8.31 1 0 1 12 10 -0.008 0.96 1.9 hours >20 hour >10 hours 65 1490 1.113 16337697 "Antiviral research, 69(2), 70–76." "Ho, T. Y., Wu, S. L., Chen, J. C., Wei, Y. C., Cheng, S. E., Chang, Y. H., Liu, H. J., & Hsiang, C. Y. (2006)." Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction 10.1016/j.antiviral.2005.10.005 Anti-SARS-CoV DRAVPe02155 GGGYSKAQKAQAKQAKQAQKAQKAQAKQAKQAQKAQKAQAKQAKQ 45 P5 +14 S1 subunit of SARS-CoV-2 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae antiviral Assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Not Found Not Available 4766.45 C202H351N71O62 RNDCEGHLFPWOU A 10.74 12 0 12 22 18 -1.642 0.9185 30 hours >20 hour >10 hours 31.11 1490 0.313 32913137 "Molecular pharmacology, 98(5), 612–619." "Tavassoly, O., Safavi, F., & Tavassoly, I. (2020)." Heparin-binding Peptides as Novel Therapies to Stop SARS-CoV-2 Cellular Entry and Infection 10.1124/molpharm.120.000098 Anti-SARS-CoV DRAVPe02156 QYGSFCTQLNRALSGIAAEQ 20 P8 S2 subunit of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 737-756 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" "1WYY, 5WRG, 5X58, 5X5B, 5XLR, 5ZVM, 6ACC, 6ACD" SARS-CoV Coronaviridae antiviral Assay [Ref:15918330]SARS-CoV:IC90=24.9±6.2μg/mL No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Cyclic Free Free None L Not Found Not Available 2157.39 C92H145N27O31S1 DHKMPWVOU AQ 5.99 1 1 0 16 14 -0.18 0.95 0.8 hours 10 mins 10 hours 73.5 1490 0.69 15918330 "Antiviral therapy, 10(3), 393–403." "Zheng, B. J., Guan, Y., Hez, M. L., Sun, H., Du, L., Zheng, Y., Wong, K. L., Chen, H., Chen, Y., Lu, L., Tanner, J. A., Watt, R. M., Niccolai, N., Bernini, A., Spiga, O., Woo, P. C., Kung, H. F., Yuen, K. Y., & Huang, J. D. (2005)." Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus Not Available Anti-SARS-CoV DRAVPe02157 IQKEIDRLNEVAKNLNESLI 20 P10 HR2 region of SARS-CoV P59594 Experimentally Validated 694009 S2 AAP13441.1 1161-1180 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" "1WYY, 5WRG, 5X58, 5X5B, 5XLR, 5ZVM, 6ACC, 6ACD" SARS-CoV Coronaviridae antiviral Assay [Ref:15918330]SARS-CoV:IC90=73.5±15.7μg/mL No hemolysis information or data found in the reference(s) presented in this entry [Ref: 30646495]No cytotoxicity No predicted structure available Cyclic Free Free None L Not Found Not Available 2339.67 C101H175N29O34 CGHMFPTWYOU NIL 4.87 3 4 -1 16 14 -0.51 0.9576 20 hour 30 min >10 hours 136.5 0 0 15918330 "Antiviral therapy, 10(3), 393–403." "Zheng, B. J., Guan, Y., Hez, M. L., Sun, H., Du, L., Zheng, Y., Wong, K. L., Chen, H., Chen, Y., Lu, L., Tanner, J. A., Watt, R. M., Niccolai, N., Bernini, A., Spiga, O., Woo, P. C., Kung, H. F., Yuen, K. Y., & Huang, J. D. (2005)." Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus Not Available Anti-SARS-CoV DRAVPe02158 GGRGGGGSGGSGGSGGRGGGGSGGSGG 27 MERS-5HB S2 subunit of MERS-CoV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MERS-CoV Coronaviridae ELISA "[Ref:28906430]MERS-CoV:IC50=The 50% inhibitory concentration (IC50) for the inhibition by MERS-5HB of a MERS-CoV infection was about 1 μM, " "[Ref:28906430]The calculated 50% effective concentration (EC50) of binding of MERS-5HB to MERS-HR2P is 5.4 nM.To confirm the binding, the ELISA assay was performed in the reverse way. MERS-5HB was coa" [Ref: 30646495]No cytotoxicity No predicted structure available Cyclic Free Free None L HR2   The absence of one HR2 may reserve a hydrophobic groove in MERS-5HB for binding to a native HR2 in the MERS-CoV S protein.It could bind to HR2 in MERS-CoV S2 to inhibit viral entry as well as S protein-mediated syncytial formation. 1906.82 C67H111N33O33 ANDCQEHIKLMFPWYVOU G 12 2 0 2 12 10 -0.778 0.96 30 hours >20 hour >10 hours 0 0 0 28906430 Viruses. 2017 Sep 14;9(9):255. "Sun Y, Zhang H, Shi J, Zhang Z, Gong R." Identification of a Novel Inhibitor against Middle East Respiratory Syndrome Coronavirus 10.3390/v9090255 Anti-MERS-CoV DRAVPe02159 VVEQYNQTILNLTSEISTLENKSAELNYTVQKLQTLIDNINSTLVDLKWL 50 229E-HR2P S2 subunit of HCoV-229E P15423 Experimentally Validated 11137 S2 CAA34723.1 1056-1105 Not Available AF304460.1 Genomic RNA "Chromosome:20,570 - 24,091" 5ZHY##5YL9##5ZUV SARS-CoV Coronaviridae cell-cell fusion assay "[Ref:29415501]SARS-CoV,IC50=0.3μM,1.96μM" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:29415501]Neither 229E-HR1P nor 229E-HR2P had significant cytotoxicity to these cells at concentrations up to 1,000 μM" No predicted structure available Linear Free Free None L Spike Protein Fusion Inhibitor 5752.51 C256H418N64O85 RCGHMFPOU L 4.36 3 6 -3 32 24 -0.156 1.1 100 hours >20 hour >10 hours 126.6 8480 1.474 29415501 "International journal of molecular sciences, 19(2), 487." "Xia, S., Xu, W., Wang, Q., Wang, C., Hua, C., Li, W., Lu, L., & Jiang, S. (2018)" Peptide-Based Membrane Fusion Inhibitors Targeting HCoV-229E Spike Protein HR1 and HR2 Domains 10.3390/ijms19020487 Anti-SARS-CoV DRAVPe02160 AVLQSGFR 8 Octapeptide Structure of SARS-CoV Mpro P0C6U8 Experimentally Validated 694009 1a Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Cell–Cell Fusion Assay "[Ref:16242214]HCoV-229E,IC50=0.5μM(pseudotyped),1.7μM(livevirus)" No hemolysis information or data found in the reference(s) presented in this entry [Ref:16242214]no detectable toxicity is observed on Vero cells .100 No predicted structure available Linear Free Free None L Not Found It inhibits replication 877.01 C39H64N12O11 NDCEHIKMPTWYOU ARQGLFSV 9.79 1 0 1 6 8 0.425 1.1 4.4 hours >20 hour >10 hours 97.5 0 0 16242214 "Peptides, 27(4), 622–625." "Gan, Y. R., Huang, H., Huang, Y. D., Rao, C. M., Zhao, Y., Liu, J. S., Wu, L., & Wei, D. Q. (2006)." Synthesis and activity of an octapeptide inhibitor designed for SARS coronavirus main proteinase 10.1016/j.peptides.2005.09.006 Anti-SARS-CoV DRAVPe02161 LQQFMK 6 6a Cleavage site of SARS-CoV Mpro No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Cell–Cell Fusion Assay "[Ref:16451084]SARS-CoV,EC50=0.027μg/mL" No hemolysis information or data found in the reference(s) presented in this entry [Ref16451084]low toxicity in cells No predicted structure available Linear Free Free None L Not Found Not Available 793.98 C36H59N9O9S1 ARNDCEGHIPSTWYVOU Q 8.75 1 0 1 6 6 8.75 1.08 5.5 hours 3 mins 2 mins 65 0 0 16451084 "J. Med. Chem. 2006, 49, 3, 1198–1201" "Zhang, H. Z., Zhang, H., Kemnitzer, W., Tseng, B., Cinatl, J., Jr, Michaelis, M., Doerr, H. W., & Cai, S. X. (2006)." Design and synthesis of dipeptidyl glutaminyl fluoromethyl ketones as potent severe acute respiratory syndrome coronovirus (SARS-CoV) inhibitors 10.1021/jm0507678 Anti-SARS-CoV DRAVPe02162 AVLQ 4 Protected tetrapeptide Cleavage site of the main proteases No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Peptide cleavage assay "[Ref:25224114]SARS-CoV,IC50=2.5μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear carboxybenzyl nitrile None L Not Found Not Available 432.53 C19H36N6O6 NDCFPSTWYVOUMGK Q 6.02 0 0 0 1 3 0.875 0.37 4.4 hours >20 hour >10 hours 117.5 0 0 25224114 " Hong Kong medical journal = Xianggang yi xue za zhi, 20 Suppl 4, 22–25." "Chuck, C. P., Ke, Z. H., Chen, C., Wan, D. C., Chow, H. F., & Wong, K. B. (2014). " Profiling of substrate-specificity and rational design of broad-spectrum peptidomimetic inhibitors for main proteases of coronaviruses 10.1021/jm0507678 Anti-SARS-CoV DRAVPe02163 ESTLQ 5 Peptide aldehyde 1 Analyses of the SARS-CoV Mpro No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Peptide cleavage assay "[Ref:21854807]SARS-CoV,IC50=8.27±1.52μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Acetylation Hydogenation None L Not Found tight-binding inhibitors 576.6 C23H40N6O11 ANDCFPWYVOU QELST 4 0 1 -1 5 5 -0.94 1.152 1 hours 30 mins >10 hours 78 0 0 21854807 "Antiviral research, 92(2), 204–212." "Vilas Boas, L. C., de Lima, L. M., Migliolo, L., Mendes, G. D., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2017)." Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease  10.1016/j.antiviral.2011.08.001 Anti-SARS-CoV DRAVPe02164 NSFSQ 5 Peptide aldehyde 2 Analyses of the SARS-CoV Mpro No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Peptide cleavage assay "[Ref:21854807]SARS-CoV,IC50=40.98±2.63μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Acetylation Hydogenation None L Not Found tight-binding inhibitors 581.58 C24H35N7O10 ARDCEGHILMPTWYVOU S 5.52 0 0 0 5 5 -1.16 1.152 1.4 hours 3 mins >10 hours 0 0 0 21854807 "Antiviral research, 92(2), 204–212." "Vilas Boas, L. C., de Lima, L. M., Migliolo, L., Mendes, G. D., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2017)." Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease  10.1016/j.antiviral.2011.08.001 Anti-SARS-CoV DRAVPe02165 DSFDQ 5 Peptide aldehyde 3 Analyses of the SARS-CoV Mpro No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Peptide cleavage assay "[Ref:21854807]SARS-CoV,IC50=41.24±2.25μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Acetylation Hydogenation None L Not Found tight-binding inhibitors 610.58 C25H34N6O12 ARNCEGHILKMPTWYVOU D 3.56 0 2 -2 5 5 -1.7 1.27 1.1 hours 3 mins >10 hours 0 0 0 21854807 "Antiviral research, 92(2), 204–212." "Vilas Boas, L. C., de Lima, L. M., Migliolo, L., Mendes, G. D., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2017)." Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease  10.1016/j.antiviral.2011.08.001 Anti-SARS-CoV DRAVPe02166 NSTSQ 5 Peptide aldehyde 4 Analyses of the SARS-CoV Mpro No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Peptide cleavage assay "[Ref:21854807]SARS-CoV,IC50=72.73±3.60μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Acetylation Hydogenation None L Not Found tight-binding inhibitors 535.51 C19H33N7O11 ARNCEGHILKMPTWYVOU S 5.52 0 0 0 5 5 -1.86 1.24 1.4 hours 3 mins >10 hours 0 0 0 21854807 "Antiviral research, 92(2), 204–212." "Vilas Boas, L. C., de Lima, L. M., Migliolo, L., Mendes, G. D., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2017)." Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease  10.1016/j.antiviral.2011.08.001 Anti-SARS-CoV DRAVPe02167 TVFH 4 Tetrapeptide aldehyde Analyses of the SARS-CoV 3CL protease No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Cell–Cell Fusion Assay "[Ref:22014094]SARS-CoV,IC50=8nM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 522.61 C25H37N5O6 ARNDCEGILMSPTWYOU TVFH 7.52 1 0 1 1 2 0.425 0.79 3.5 hours >20 hours >10 hours 97.5 0 0 22014094 "Journal of medicinal chemistry, 54(23), 7962–7973." "Akaji, K., Konno, H., Mitsui, H., Teruya, K., Shimamoto, Y., Hattori, Y., Ozaki, T., Kusunoki, M., & Sanjoh, A. (2011)." "Structure-based design, synthesis, and evaluation of peptide-mimetic SARS 3CL protease inhibitors" 10.1021/jm200870n Anti-SARS-CoV DRAVPe02168 VIQY 4 Oligopeptide 1 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 523.61 C25H41N5O7 ARNCEGHILKMPWOU Q 6.03 0 0 0 2 2 -0.2 0.48 100 hours >20 hours >10 hours 112.5 1490 0.054 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV DRAVPe02169 ICIY 4 Oligopeptide 2 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 522.65 C25H41N5O6S ARNCEGHILKMPTWYVOU C 6.02 0 0 0 2 2 -0.95 -0.27 20 hours >20 hour >10 hours 137.5 1490 0.054 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV DRAVPe02170 PISQF 5 Oligopeptide 3 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 590.68 C28H42N6O8 ARNDEGHLKMTWVOU QIFPS 5.96 0 0 0 5 5 0.28 0.944 > 20 hours >20 hours Unknown 78 0 0 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV DRAVPe02171 VISAW 5 Oligopeptide 4 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 574.68 C28H42N6O7 RNDCQEGHLKMFPTYOU ISWV 5.49 0 0 0 5 5 1.76 0.73 100 hours >20 hours >10 hours 156 5500 9.571 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV DRAVPe02172 AIPAW 5 Oligopeptide 5 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 556.66 C28H40N6O6 RNDCQEGHLKMFSTOU A 5.57 0 0 0 5 5 1.12 0.82 4.4 hours >20 hours >10 hours 118 500 980 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV DRAVPe02173 PVSQF 5 Oligopeptide 6 Marine fish proteins No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV-2 Coronaviridae Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Not Found Not Available 576.65 C27H40N6O8 RNDCGHLMKTSYOU QEFPSV 5.96 0 0 0 5 5 0.22 0.94 >20 hours >20 hours Unknown 58 0 0 32520031 "Food & function, 11(6), 5565–5572." "Yao, Y., Luo, Z., & Zhang, X. (2020)." In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients 10.1039/d0fo00530d Anti-SARS-CoV-2 DRAVPe02174 GGASCCLYCRCH 12 K12 Sequence of nsp 10 of SARS-CoV P0C6U8 Experimentally Validated 694009 1a Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Not Available "[Ref:22659295]SARS-CoV,IC50=160μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Available 1272.5 C49H77N17O15S4 NDQEIKMFPTWVOU C 7.9 1 0 1 12 10 0.417 0.633 30 hours >20 hours >10 hours 40.83 1490 1.171 22659295 "Virus research, 167(2), 322–328." "Ke, M., Chen, Y., Wu, A., Sun, Y., Su, C., Wu, H., Jin, X., Tao, J., Wang, Y., Ma, X., Pan, J. A., & Guo, D. (2012)." Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex 10.1016/j.virusres.2012.05.017 Anti-SARS-CoV DRAVPe02175 FGGASCCLYCRCHIDHPNPKGFCDLKGKY 29 K29 Sequence of nsp 10 of SARS-CoV P0C6U8 Experimentally Validated 694009 1a Not Available Not Available Not Available Not Available Not Available Not Available None SARS-CoV Coronaviridae Not Available "[Ref:22659295]SARS-CoV,IC50=160μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found Not Available 3233.76 C141H210N40O38S5 QEMWVOU C 8.4 4 2 2 22 18 -0.321 0.918 1.1 hours 3 min 2 min 43.78 2980 0.922 22659295 "Virus research, 167(2), 322–328." "Ke, M., Chen, Y., Wu, A., Sun, Y., Su, C., Wu, H., Jin, X., Tao, J., Wang, Y., Ma, X., Pan, J. A., & Guo, D. (2012). " Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex  10.1016/j.virusres.2012.05.017 Anti-SARS-CoV DRAVPe02176 ILPWKWPWWPWRR 13 APB-13 Cattle P33046  A3KN14  Experimentally Validated 9913 CATHL4 CAA47755.1 131-143 282166 CM008189.2 mRNA "Primary_assembly 22: 51,592,817-51,594,193 reverse strand." 1G8C##1G89  TGEV Coronaviridae TCID50 assay. "[Ref:33016025]TGEV,IC50=62.5μg/mL" No hemolysis information or data found in the reference(s) presented in this entry "The results showed that the APB-13 concentrations from 0 to 62.5 µg/mL were relatively non-toxic to the cells, and the cell states and mean OD values of the ST cells treated with APB-13 for these conc" No predicted structure available Linear Free Amidation None L N Protein "APB-13 inhibited TGEV replication, and within a certain range, the mRNA and protein expression levels of the N protein increased gradually as the APB-13 concentration decreased." 1907.3 C100H131N25O14 ANDCQEGHMFSTYVOU P 12.01 3 0 3 12 10 -1.069 0.9 20 hours 30 mins >10 hours 60 27500 14.418 33016025 "Journal of veterinary science, 21(5), e80." "Liang, X., Zhang, X., Lian, K., Tian, X., Zhang, M., Wang, S., Chen, C., Nie, C., Pan, Y., Han, F., Wei, Z., & Zhang, W. (2020). " Antiviral effects of Bovine antimicrobial peptide against TGEV in vivo and in vitro 10.4142/jvs.2020.21.e80 Anti-TGEV DRAVPe02177 FKPSSPPSITLW 12 F S protein of TGEV (synthetic Construct) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None TGEV Coronaviridae ELISA "[Ref:21176936]TGEV,IC50=20μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L S protein "The peptides showed an effective binding to pAPN and inhibition to TGEV infection, although their sequences are not completely identical to the homologous regions in the S1 protein" 1359.59 C66H98N14O17 ARNDCQEGHMYVOU PS 8.75 1 0 1 12 10 -0.133 0.9 1.1 hours 3 min 2 min 65 5500 4.045 21176936 "Virology, 410(2), 299–306." "Ren, X., Liu, B., Yin, J., Zhang, H., & Li, G. (2011)." Phage displayed peptides recognizing porcine aminopeptidase N inhibit transmissible gastroenteritis coronavirus infection in vitro 10.1016/j.virol.2010.11.014 Anti-TGEV DRAVPe02178 HVTTTFAPPPPR 12 H S protein of TGEV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None TGEV Coronaviridae ELISA "[Ref:21176937]TGEV,IC50=" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L S protein "The peptides showed an effective binding to pAPN and inhibition to TGEV infection, although their sequences are not completely identical to the homologous regions in the S1 protein" 1320.51 C61H93N17O16 NDCQEGILKMOUW T 9.76 1 0 1 12 10 -0.617 0.99 3.5 hours 10 min >10 hours 32.5 0 0 21176936 "Virology, 410(2), 299–306." "Ren, X., Liu, B., Yin, J., Zhang, H., & Li, G. (2011)." Phage displayed peptides recognizing porcine aminopeptidase N inhibit transmissible gastroenteritis coronavirus infection in vitro 10.1016/j.virol.2010.11.015 Anti-TGEV DRAVPe02179 SVVPSKATWGFA 12 S S protein of TGEV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None TGEV Coronaviridae ELISA "[Ref:21176936]TGEV,IC50=20μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L S protein "The peptides showed an effective binding to pAPN and inhibition to TGEV infection, although their sequences are not completely identical to the homologous regions in the S1 protein" 1249.43 C59H88N14O16 RNDCQEHILMYOU ASV 8.47 1 0 1 12 10 0.475 0.906 1.9 hurs >20 hour >10 hours 65 5500 4.402 21176936 "Virology, 410(2), 299–306." "Ren, X., Liu, B., Yin, J., Zhang, H., & Li, G. (2011)." Phage displayed peptides recognizing porcine aminopeptidase N inhibit transmissible gastroenteritis coronavirus infection in vitro 10.1016/j.virol.2010.11.016 Anti-TGEV DRAVPe02180 HDAISWTHYHPW 12 PM1 porcine aminopeptidase N (rpAPN-C) protein No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None TGEV Coronaviridae MTT assay Not Avaialble No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 1549.67 C74H92N20O18 RNCQEILKFMSTVOU H 6.25 0 1 -1 12 10 -1.083 0.99 3.5 hours 10 min >10 hours 40.83 12490 8.06 24111863 "Monoclonal antibodies in immunodiagnosis and immunotherapy, 32(5), 326–329." "Guo, D., Zhu, Q., Feng, L., & Sun, D. (2013)." Screening and antiviral analysis of phages that display peptides with an affinity to subunit C of porcine aminopeptidase 10.1089/mab.2013.0038 Anti-TGEV DRAVPe02181 LMQINPTYYQIM 12 L S1 protein of PEDV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque-reduction assay "[Ref:26292945]PEDV,IC50=50μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Cell surface Two peptides derived from phage display libraries were identified with sequence homology to a specific region of the PEDV S1 protein and that affect binding of the PEDV to the cell surface 1514.82 C69H107N15O19S2 ARDCEGHKFSWVOU QIM 5.52 0 0 0 12 10 0.1 0.99 5.5 hours 3 mins 2 min 97.5 2980 1.967 26292945 "Virus genes, 51(2), 217–224." "Cao, L., Ge, X., Gao, Y., Zarlenga, D. S., Wang, K., Li, X., Qin, Z., Yin, X., Liu, J., Ren, X., & Li, G. (2015)." Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity 10.1007/s11262-015-1234-5 Anti-PEDV DRAVPe02182 WSFNPSTYTIAG 12 W S1 protein of PEDV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None PEDV Coronaviridae Plaque-reduction assay "[Ref:26292945]PEDV,IC50=50μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Cell surface Two peptides derived from phage display libraries were identified with sequence homology to a specific region of the PEDV S1 protein and that affect binding of the PEDV to the cell surface 1343.46 C63H86N14O19 RDCQEHKMOU ST 5.52 0 0 0 12 10 -0.133 0.99 2.8 hours 3 mins 2 min 40.83 6990 5.203 26292945 "Virus genes, 51(2), 217–224." "Cao, L., Ge, X., Gao, Y., Zarlenga, D. S., Wang, K., Li, X., Qin, Z., Yin, X., Liu, J., Ren, X., & Li, G. (2015)." Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity  10.1007/s11262-015-1234-5 Anti-PEDV DRAVPe02183 HALTPIKYIPPG 12 TGEV-M7 M protein of TGEV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None TGEV Coronaviridae Plaque-reduction assay "[Ref:23830854]TGEV,IC50=62.5μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L rTGEV-M protein pepTGEV-M7 binding to the surface of the virus and either interfering with the ability of the virus to invade the cell or generate progeny virus.  1306.57 C63H99N15O15 RNDCQEMFSWVOU P 8.06 1 0 1 12 10 0.025 0.99 3.5 hours 10 mins >10 hours 105.83 1490 1.14 23830854 "Antiviral research, 99(3), 383–390." "Zou, H., Zarlenga, D. S., Sestak, K., Suo, S., & Ren, X. (2013)." Transmissible gastroenteritis virus: identification of M protein-binding peptide ligands with antiviral and diagnostic potential 10.1016/j.antiviral.2013.06.015 Anti-TGEV DRAVPe02184 YGFWTIAYTNYTDVMVDVNG 20 I-S1-9 S1 protein of FIPV A0A1Z2WU95 Experimentally Validated 12663 S Not Available 477-496 Not Available Not Available Not Available Not Available None FIPV Coronaviridae plaque reduction assay. "[Ref:25896976]FIPV,IC50=100μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 2329.57 C108H149N23O33S1 RCQEHLKPSOU TYV 3.56 0 2 -2 22 18 0.095 0.9185 2.8 hours 10 min 2 min 68 9970 4.28 25896976 "Virus research, 204, 13–20." "Doki, T., Takano, T., Koyama, Y., & Hohdatsu, T. (2015)." Identification of the peptide derived from S1 domain that inhibits type I and type II feline infectious peritonitis virus infection 10.1016/j.virusres.2015.04.011 Anti-FIPV DRAVPe02185 YHWMNVTLHVVLNDTEKKYD 20 I-S1-16 S1 protein of FIPV Q66951 Experimentally Validated 11135 S Not Available 541-560 Not Available Not Available Not Available Not Available None FIPV Coronaviridae plaque reduction assay. "[Ref:25896976]FIPV,IC50=100μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 2505.83 C114H169N29O33S1 ARCQGIFPSOU V 6 2 3 -1 22 18 -0.725 0.9185 2.8 hours 10 min 2 min 82.5 8480 3.384 25896976 "Virus research, 204, 13–20." "Doki, T., Takano, T., Koyama, Y., & Hohdatsu, T. (2015)." Identification of the peptide derived from S1 domain that inhibits type I and type II feline infectious peritonitis virus infection 10.1016/j.virusres.2015.04.011 Anti-FIPV DRAVPe02186 LFYKYTSLQGLYTYSNLVEL 20 I-S1-22 S1 protein of FIPV A0A0C5CJL1 Experimentally Validated 12663 S Not Available 603-622 Not Available Not Available Not Available Not Available None FIPV Coronaviridae plaque reduction assay. "[Ref:25896976]FIPV,IC50=~60μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 2415.77 C116H171N23O33 ARDCHIMWOU L 6 1 1 0 22 18 0.15 0.9185 5.5 hours 3 min 2 min 112 5960 2.467 25896976 "Virus research, 204, 13–20." "Doki, T., Takano, T., Koyama, Y., & Hohdatsu, T. (2015)." Identification of the peptide derived from S1 domain that inhibits type I and type II feline infectious peritonitis virus infection 10.1016/j.virusres.2015.04.012 Anti-FIPV DRAVPe02187 VNFSISSVEEYGFWTIAYTN 20 I-S1-8 S1 protein of FIPV Q66951 Experimentally Validated 11135 S Not Available 461-480 Not Available Not Available Not Available Not Available None FIPV Coronaviridae Plaque-reduction assay "[Ref:25896976]FIPV,IC50=~50μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 2327.53 C109H151N23O34 RDCQQHLKMPOU NEI 3.79 0 2 -2 22 18 0.155 0.9185 100 hours >20 hour >10 hours 73 8480 3.643 25896976 "Virus research, 204, 13–20." "Doki, T., Takano, T., Koyama, Y., & Hohdatsu, T. (2015)." Identification of the peptide derived from S1 domain that inhibits type I and type II feline infectious peritonitis virus infection 10.1016/j.virusres.2015.04.013 Anti-FIPV DRAVPe02188 YTDVMVDVNGTAITRLFYCD 20 I-S1-10 S1 protein of FIPV Q66951 Experimentally Validated 11135 S Not Available 481-500 Not Available Not Available Not Available Not Available None FIPV Coronaviridae Plaque-reduction assay "[Ref:25896976]FIPV,IC50=~60μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 2296.59 C101H154N24O33S2 QEHPSWOU DTV 3.93 1 3 -2 22 18 0.315 0.9185 2.8 hours 10 min 2 min 87.5 2980 1.298 25896976 "Virus research, 204, 13–20." "Doki, T., Takano, T., Koyama, Y., & Hohdatsu, T. (2015)." Identification of the peptide derived from S1 domain that inhibits type I and type II feline infectious peritonitis virus infection 10.1016/j.virusres.2015.04.014 Anti-FIPV DRAVPe02189 GSHHRHVHSPFV 12 Peptide 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None IBV Coronaviridae Plaque-reduction assay "[Ref:16704119]IBV,IC50=8.3μg/mL" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not given Not Available 1396.53 C62H89N23O15 ANDCQEILKMTWYOU H 9.78 1 0 1 10 10 -0.808 0.988 30 hours >20 hour >10 hours 48.33 0 0 16704119 "Science in China. Series C, Life sciences, 49(2), 158–163." "Peng, B., Chen, H., Tan, Y., Jin, M., Chen, H., & Guo, A. (2006). " Identification of one peptide which inhibited infectivity of avian infectious bronchitis virus in vitro 10.1007/s11427-006-0158-7 Anti-IBV DRAVPe02190 CRPYGYRCDGVINQCCDPYHCTPPLIGICL 30 Alstotide As1 Alstonia scholaris plant A0A0S0ZR07 Experimentally Validated 52822 As1 Not Available 63-92 Not Available Not Available Not Available Not Available 2MM6 IBV Coronaviridae Antiviral Activity Assay "[Ref:26546678]IBV,EC50=35μM" No hemolysis information or data found in the reference(s) presented in this entry Cytotoxicity assay showed that As1 and As3 did not induce significant cytotoxicity in Vero cells at concentrations up to 100 μm No predicted structure available Linear Free Free None L S protein "We first determined the stage(s) in viral replication cycle which alstotides could inhibit using a time of drug addition assay. As1 (50 and 100 μm) was introduced to synchronized infected cells at different time points during preincubation at 4 °C and the infection at 37 °C As1 was identified as a moderate early acting anti-IBV drug, as supported by three lines of evidence. First, the time of drug addition assay revealed a significant drop of activity when As1 was added at 3 hpi, implicating an antiviral mechanism upstream of genomic replication and gene expression. Second, in transfection assay when the genetic material was electroporated into the host cells to bypass the attachment and entry steps, no inhibition over gene replication within 18 hpi was observed. In contrast, parallel As1-treated samples collected at 40 hpi showed a clear inhibition, probably because of inhibitory activity during the early stage of secondary infection. Third, As1 binds to IBV fusion glycoprotein, S protein, which plays a vital role during viral entry by attaching to Vero cell receptors and triggering membrane fusion between enveloped virus and host cells. In this assay, As1 added during attachment (at 4 °C) or entry (after transfer to 37 °C) exhibited comparable positive effects. As1 significantly lost its activity when added during later stages from 3 hpi onward. Comparable intensities of the endogenous control actin bands for both the treated and untreated samples excluded the effect of As1 on cellular protein synthesis, thus suggesting that As1 acts during an early stage of the viral infection." 3373.96 C145H222N40O41S6 AEKMFWOU C 6.7 2 2 0 32 24 0.063 0.9576 1.2 hours >20 hour >10 hours 74.67 4470 1.35 26546678 "The Journal of biological chemistry, 290(52), 31138–31150." "Nguyen, P. Q., Ooi, J. S., Nguyen, N. T., Wang, S., Huang, M., Liu, D. X., & Tam, J. P. (2015). " Antiviral Cystine Knot α-Amylase Inhibitors from Alstonia scholaris  10.1074/jbc.M115.654855 Anti-IBV DRAVPe02191 CVPRFGRCDGIINOCCDPYLCTPPLVGICT 30 Alstotide As3 Alstonia scholaris plant No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None IBV Coronaviridae Antiviral Activity Assay "[Ref:26546678]IBV,EC50=55μM" No hemolysis information or data found in the reference(s) presented in this entry Cytotoxicity assay showed that As1 and As3 did not induce significant cytotoxicity in Vero cells at concentrations up to 100 μm No predicted structure available Linear Free Free None L S protein The putative antiviral mechanism of As1 is through its interference with S protein function during IBV entry. 3367.05 C146H233N39O40S6 AEKMFWOU C 5.92 2 2 0 32 24 0.583 0.9576 1.2 hours >20 hour >10 hours 84.33 1490 0.443 26546678 "The Journal of biological chemistry, 290(52), 31138–31150." "Nguyen, P. Q., Ooi, J. S., Nguyen, N. T., Wang, S., Huang, M., Liu, D. X., & Tam, J. P. (2015). " Antiviral Cystine Knot α-Amylase Inhibitors from Alstonia scholaris  10.1074/jbc.M115.654855 Anti-IBV DRAVPe02192 SLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKE 39 HR2 HR2 region of MHV No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MHV Coronaviridae Cell-cell fusion assay. "[Ref:2885899]MHV,IC90=50μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Spike Protein "Using biological assays, the HR2 peptide was shown to be a potent inhibitor of virus entry into the cell, as well as of cell-cell fusion" 4616.3 C206H337N51O66S1 CGHPWOU L 4.71 5 7 -2 32 24 -0.356 1.1 1.9 hours >20 hours >10 hours 120 2980 0.646 12885899 "Journal of virology, 77(16), 8801–8811." "Bosch, B. J., van der Zee, R., de Haan, C. A., & Rottier, P. J. (2003)." The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex 10.1128/jvi.77.16.8801-8811.2003 Anti-MHV DRAVPe01810 ARLPRKKWK 9 C20-Jp-Hp Synthetic construct None Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Orthomyxoviridae Cytopathic effect inhibition [Ref:26952867]IAV:IC50=0.53 ± 0.25ug/ml No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear C20 Free None L Hemagglutinin protein "The ARLPR is a sialic acid mimic, the compound was demonstrated to bind the fusogenic region of HA, as indicated by CD spectra registered for the fusion peptide alone or in presence of C20-Jp-Hp" 1182.48 C55H95N19O10 NDCQEGHIMFSTYVOU K 12.02 5 0 5 0 3 -1.956 4.15 4.4 hours >20 hours >10 hours 54.44 5500 4.651 26952867 "Scientific reports, 6, 22790. " "Lin, D., Li, F., Wu, Q., Xie, X., Wu, W., Wu, J., Chen, Q., Liu, S., & He, J. (2016). " A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities 10.1038/srep22790 Anti-HIV DRAVPe02329 YYTRWQGGLRYIRPCG 16 eVpeD2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:28574091]EBOV:IC50=9 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Acetylation "In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration" L VP24 "The macrocyclic peptide eVpeD2 exhibits potent binding to immobilized Zaire Ebola virus VP24, with a dissociation constant (KD) in the single-digit nanomolar range. Studies show that eVpeD2 disrupts the protein-protein interaction between eVP24 and KPNA5, confirmed through assays like the AlphaLISA-based binding assay. This inhibition suggests eVpeD2's potential as a modulator of a crucial interaction in Ebola virus pathogenesis." 1989.28 C91H133N27O22S1 ADEFHKMNOSUV GRY 9.78 3 0 3 9 3 -0.906 2.31 2.8hours 10min 2min 48.75 9970 5.012 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02328 YIVPWNGGSRLIRNSRCG 18 eVpeD1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:28574091]EBOV:IC50=28 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Acetylation "In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration.)" L VP24 "eVpeD1 works against the Ebola virus by inhibiting the protein-protein interaction (PPI) between the viral protein VP24 and the host protein karyopherin alpha 5 (KPNA5). VP24 interferes with the host's immune response by binding to KPNA5, which is crucial for transporting antiviral signaling proteins into the nucleus. By binding to VP24, eVpeD1 prevents its interaction with KPNA5, thereby restoring the normal function of the immune signaling pathway. This inhibition was demonstrated in vitro using an AlphaLISA-based binding assay, where eVpeD1 disrupted the VP24-KPNA5 interaction. Consequently, eVpeD1 and similar peptides have potential as novel antiviral agents against Ebola virus by targeting and blocking this critical PPI." 2048.35 C89H142N30O24S1 ADEFHKMOQTU GR 10.76 3 0 3 9 5 -0.422 2.2 2.8hours 10min 2min 81.11 6990 3.413 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02326 RWLRGLLSGLLR 12 DFTavP3 Designed In-silico (Ab-initio) by using database filtering technology No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A "[Ref:35631348]EBOV:IC50:2.5, 5, or 10 microM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "DFTavP3 likely inhibits Ebola virus infection by targeting specific parameters designed to disrupt viral entry or replication. Its mechanism of action may involve interference with viral attachment, fusion, or replication processes, ultimately reducing viral infectivity. This inhibition could occur through direct interaction with viral components or through modulation of host cell factors essential for viral propagation, leading to decreased viral replication and infection in Vero cells." 1439.77 C66H114N22O14 ACDEFHIKMNOPQTUVY L 12.3 3 0 3 4 6 0.25 1.61 1hours 2min 2min 162.5 5500 3.82 35631348  Pharmaceuticals (Basel). 2022;15(5). "Ripperda T, Yu Y, Verma A, et al." Improved Database Filtering Technology Enables More Efficient Ab Initio Design of Potent Peptides against Ebola Viruses. 10.3390/ph15050521 Anti-EBOV DRAVPe02327 GLRCRLGRLLRRLGRCLLR 19 DDIP1 Designed In-silico (Ab-initio) by using database filtering technology No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A Not Available "The hemolytic activity of DDIP1 was assessed using murine red blood cells, where the HC50 (concentration causing 50% hemolysis) was greater than 160 microM, indicating low hemolytic activity." "[Ref:35631348]DDIP1 was evaluated for its cytotoxicity using various cell lines, including Vero cells and Calu3 cells. The results indicated that DDIP1 had a TC50 (toxic concentration at 50% cell deat" No predicted structure available Linear Free Free None L glycoprotein. " DDIP1, a database-designed inhibitory peptide, against Ebola virus. In experiments using an Ebola virus pseudo-type system, DDIP1 effectively inhibited the entry of pseudo-Ebola virus (VSV-eGP) into Vero cells at an early stage of infection. These findings suggest DDIP1's potential as a novel treatment for Ebola by targeting viral entry." 2280.88 C96H182N40O20S2 ADEFHIKMNOPQSTUVWY LR 12.13 7 0 7 9 7 -0.058 3.4 30hours >20hours >10hours 143.68 125 0.055 35631348  Pharmaceuticals (Basel). 2022;15(5). "Ripperda T, Yu Y, Verma A, et al." Improved Database Filtering Technology Enables More Efficient Ab Initio Design of Potent Peptides against Ebola Viruses. 10.3390/ph15050521 Anti-EBOV DRAVPe02325 RWLRGLLSGLLRRLLS 16 DFTavP2 Designed In-silico (Ab-initio) by using database filtering technology No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:35631348]EBOV:IC33=5 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "DFTavP2 likely combats the Ebola virus by interacting with viral glycoproteins or host cell receptors, thereby inhibiting viral entry into host cells. It may disrupt viral membranes, compromising the virus's structural integrity and function. The peptide could also interfere with the virus's replication machinery by binding to viral RNA or essential proteins. Overall, these mechanisms highlight DFTavP2's potential in blocking critical stages of the Ebola virus lifecycle" 1909.35 C87H153N29O19 ACDEFHIKMNOPQTUVY L 12.48 4 0 4 6 8 0.331 1.73 1hours 2min 2min 170.62 5500 2.881 35631348  Pharmaceuticals (Basel). 2022;15(5). "Ripperda T, Yu Y, Verma A, et al." Improved Database Filtering Technology Enables More Efficient Ab Initio Design of Potent Peptides against Ebola Viruses. 10.3390/ph15050521 Anti-EBOV DRAVPe02324 RWLRGLLSGLLRRLLSGLLL 20 DFTavP1 Designed In-silico (Ab-initio) by using database filtering technology No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:35631348]EBOV:IC50= 2.5 microM "[Ref:35631348]DFTavP1 displayed hemolytic activity, with an HC50 (the concentration that caused 50% hemolysis) below 12.5 microM. In contrast, DDIP1, another designed peptide, showed a higher HC50 val" "[Ref:35631348]DFTavP1 showed cytotoxic effects on Vero cells, with a TC50 (the peptide concentration that killed 50% of cells) of 2.4 microM. The peptide also exhibited cytotoxicity to Calu3 cells, wi" No predicted structure available Linear Free Free None L Viral envelopes. "DFTavP1 is a designed peptide that inhibits Ebola virus by blocking viral entry and disrupting viral envelopes, crucial steps in infection. Studies show DFTavP1 and similar peptides effectively inhibit pseudo-Ebola virus (VSV-eGP) in Vero cells, exhibiting dose-responsive inhibition even post-infection." 2305.88 C107H189N33O23 ACDEFHIKMNOPQTUVY L 12.48 4 0 4 6 11 0.815 0.6 1hours 2min 2min 195 5500 2.385 35631348  Pharmaceuticals (Basel). 2022;15(5). "Ripperda T, Yu Y, Verma A, et al." Improved Database Filtering Technology Enables More Efficient Ab Initio Design of Potent Peptides against Ebola Viruses. 10.3390/ph15050521 Anti-EBOV DRAVPe02323 SGWIYWAV 8 CP3 Designed In-silico on VEGAZZ software No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:32998394]EBOV:IC50 = 25.8 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L VP40. "CP3, a cyclic peptide inhibitor, can inhibit Ebola virus budding by preventing the binding of UEV domain proteins to the P6 motif. CP3 forms hydrogen bonds with UEV domain proteins through its Tyr147 and Trp148 residues. Additionally, its Trp145, Tyr147, Ile146, and Trp148 residues engage in nonbonding interactions with UEV domain proteins. These interactions suggest that CP3 effectively disrupts the protein-protein interactions essential for the budding of both Ebola viruses." 981.12 C50H64N10O11 CDEFHKLMNOPQRTU W 5.24 0 0 0 2 5 0.775 -1.6 1.9hours >20hours >10hours 97.5 12490 12.37 32998394 Polymers (Basel). 2020;12(10) "Lin WW, Wang YJ, Ko CW, et al" Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations 10.3390/polym12102235 Anti-EBOV DRAVPe02322 SGWIAWNV 8 CP2 Designed In-silico on VEGAZZ software No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:32998394]EBOV:IC50=296.3 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L VP40. "CP2, a cyclic peptide inhibitor, has a weaker binding affinity for UEV domain proteins compared to CP1. Consequently, CP1 and CP3 are more effective at preventing UEV domain proteins from binding to the P6 motif, thereby inhibiting Ebola virus budding. In contrast, CP2's weaker binding suggests it is less potent in disrupting the necessary protein-protein interactions for virus budding inhibition." 932.05 C45H61N11O11 CDEFHKLMOPQRTUY W 5.24 0 0 0 2 5 0.5 -0.79 1.9hours >20hours >10hours 97.5 11000 11.802 32998394 Polymers (Basel). 2020;12(10) "Lin WW, Wang YJ, Ko CW, et al" Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations 10.3390/polym12102235 Anti-EBOV DRAVPe02321 SGWIYWNV 8 CP1 Designed In-silico on VEGAZZ software No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:32998394]EBOV:IC50=48.6 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L VP40. "The cyclic peptide CP1 works against Ebola virus by inhibiting the binding of the UEV domain protein to the Ebola Vp40 protein. This interference prevents the budding of the Ebola virus, thereby hindering its replication and spread. The specific residues Trp145, Tyr147, and Trp148 of CP1 play essential roles in the interactions between CP1 and the UEV domain protein, contributing to its inhibitory effect. By disrupting these protein-protein interactions crucial for virus budding, CP1 shows promise as a potential therapeutic agent against Ebola virus infections." 1024.14 C51H65N11O12 ACDEFHKLMOPQRTU W 5.24 0 0 0 3 4 0.113 -0.54 1.9hours >20hours >10hours 85 12490 12.196 32998394 Polymers (Basel). 2020;12(10) "Lin WW, Wang YJ, Ko CW, et al" Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations 10.3390/polym12102235 Anti-EBOV DRAVPe02320 CTVALPGGYVRVC 13 pep42 Designed In-silico [Pep42 cyclic peptide (CTVALPGGYVRVC) model was built using I-TASSER web server] No entry found In-Silico None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Cell-surface HSPA5 "Pep42 works against the Ebola virus by selectively targeting cell-surface HSPA5, also known as GRP78, which interacts with viral glycoproteins GP1 and GP2. By disrupting the interaction between HSPA5 and viral glycoproteins, Pep42 potentially inhibits viral entry into host cells, thereby reducing viral infection" 1337.62 C58H96N16O16S2 DEFHIKMNOQSUW V 8.06 1 0 1 5 5 1.1 -0.43 1.2hours >20hours >10hours 104.62 1615 1.207 32291698 Cell Stress Chaperones. 2020;25(3):541-548 "Elfiky AA, Elfiky AA" Ebola virus glycoprotein GP1-host cell-surface HSPA5 binding site prediction. 10.1007/s12192-020-01106-z Anti-EBOV DRAVPe02319 IGIEDLSKNIKDKIDKIIHDFVDKTLPDQG 30 EBOV-8 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A [Ref:31473342]EBOV:EC50=18.47 plusminus 4.64 microM;EC90=69.49 microM.EBOV-GP EC50=4.02 plusminus 1.13 microM;EBOV-GP EC90=20.22 microM.ma-EBOV EC50=19.80 plusminus 1953 microM;ma-EBOV EC90=142 microM.GP =>GlycoProtein;ma =>Mouse-Adapted No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342]EBOV-8 show cytotoxicity (CC50) at greater than 30 microM.EBOV-5 show cytotoxicity (CC50) at >= 25 microM (when tested for EBOV-GP).EBOV-5 show cytotoxicity (CC50) at >= 44.0 microM (whe No predicted structure available Cyclic cholesterylation PEG12 "In the peptide sequence, the cysteine residue at position 31 is modified with a PEG12-cholesterol (PEG12-Chol) moiety" L Glycoprotein. "Exact MoA explicitly not available (EBOV-8 likely inhibits Ebola virus by targeting viral entry and fusion processes. It may interfere with viral glycoproteins, preventing the virus from attaching to and entering host cells. Additionally, EBOV-8 could disrupt the fusion between the viral envelope and host cell membrane, blocking the release of viral genetic material. By targeting these critical steps, the peptide effectively halts infection and viral replication. The specific antiviral mechanisms of EBOV-8 involve interactions with viral proteins essential for these processes. Detailed studies and assays in the full research paper would provide further insights into these mechanisms.)." 3408.9 C152H251N39O49 ACMORUWY DI 4.89 5 7 -2 17 10 -0.55 2.04 20hours 30min >10hours 113.67 None None 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02318 IEPHDWTKNIKDKIDKIIHDFVDKTLPDQG 30 EBOV-7 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:31473342]EBOV:EC50=1.90 plusminus 0.28;EC90=9.44 microM.EBOV-GP EC50=0.60 plusminus 0.20 microM;EBOV-GP EC90=6.15 microM.ma-EBOV EC50=0.50 plusminus 0.09 microM;ma-EBOV EC90=3.45 microM.GP =>GlycoProtein;ma =>Mouse-Adapted No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342]EBOV-7 show cytotoxicity (CC50) at greater than 30 microM.EBOV-5 show cytotoxicity (CC50) at >= 25 microM (when tested for EBOV-GP).EBOV-5 show cytotoxicity (CC50) at >= 42.6 microM (whe No predicted structure available Cyclic cholesterylation PEG12 "In the peptide sequence, the cysteine residue at position 31 is modified with a PEG4-cholesterol (PEG4-Chol) moiety" L Glycoprotein. "EBOV-7 works against Ebola virus by targeting its entry and replication processes. It likely prevents the virus from binding to host cell receptors or fusing with cellular membranes, thus inhibiting viral entry. The peptide stabilizes an alpha-helical structure, enhancing its ability to interact with viral components critical for these processes. With a potency of 0.5 microM, EBOV-7 effectively disrupts the viral life cycle. In vivo studies in mice have shown that EBOV-7 has robust antiviral activity against Ebola virus, further confirming its efficacy. Overall, EBOV-7 interferes with viral entry and stabilizes essential structures, making it a strong candidate for therapeutic use against Ebola." 3560.02 C161H252N42O49 ACMORSUY D 5.37 5 7 -2 18 9 -1 2.45 20hours 30min >10hours 87.67 5500 1.545 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02317 DWTKNIKDKIDKIIHDFVDKTLPDQGC 26 EBOV-6 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available "[Ref:31473342]EBOV:EC50=1.90 plusminus 0.39 microM, 3.67 plusminus 0.89 microM, 5.44 plusminus 0.85 microM; EBOV EC90 = 9.84 microM, 15.33 microM, 25.75 microM.EBOV-GP EC50 = 1.82 plusminus 0.55 microM; EBOV-GP EC90 = 29.46 microM.ma-EBOV EC50 = 7.95 plusminus 28.30 microM; ma-EBOV EC90 = 211 microM.GP => GlycoProtein; ma => Mouse-Adapted" No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342]EBOV-6 show cytotoxicity (CC50) at greater than 30 microM.EBOV-5 show cytotoxicity (CC50) at >= 25 microM (when tested for EBOV-GP).EBOV-5 show cytotoxicity (CC50) at >= 47.4 microM (whe No predicted structure available Cyclic cholesterylation PEG12 "In the peptide sequence, the cysteine residue at position 27 is modified with a PEG4-cholesterol (PEG4-Chol) moiety.)" L Glycoprotein. "EBOV-6 works against the Ebola virus by targeting the fusion process required for the virus to enter host cells. Specifically, it binds to the C-terminal heptad-repeat (HR2) domain of the Ebola virus glycoprotein GP2. This binding disrupts the formation of the fusion complex, a critical structure that facilitates the merging of the viral and host cell membranes. By interfering with this fusion process, EBOV-6 prevents the virus from entering and infecting the host cells. Consequently, this inhibition leads to a reduction in viral replication and spread, making EBOV-6 a potential antiviral agent against Ebola virus infection" 3186.63 C142H225N37O44S1 AEMORSUY D 5.46 5 6 -1 17 8 -0.878 2.44 1.1hours 3min >10hours 82.96 5500 1.726 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02316 DWTKNIKDKIDKIIHDFVDKTLPDQG 26 EBOV-5 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae N/A "[Ref:31473342]EBOV:EC₅₀= 3.88 ± 0.67 μM, 3.89 ± 0.61 μM; EBOV EC₉₀=17.27 μM, 16.86 μM; EBOV-GP EC₅₀=2.45 ± 1.09 μM; EBOV-GP EC₉₀= 29.46 μM; ma-EBOV EC₅₀= 2.34 ± 0.69 μM; ma-EBOV EC₉₀=16.2 μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342}EBOV:CC₅₀ > 30 μM; EBOV-5 CC₅₀ ≥ 25 μM (EBOV-GP); EBOV-5 CC₅₀ ≥ 51.7 μM (ma-EBOV). No predicted structure available Cyclic cholesterylation PEG4 "In the peptide sequence, the cysteine residue at position 27 is modified with a PEG4-cholesterol (PEG4-Chol) moiety.)" L Glycoprotein. "Exact MoA explicitly not available (may interfere with the binding of the Ebola virus glycoprotein to host cell receptors, thereby preventing viral entry into host cells)." 3083.49 C139H220N36O43 ACEMORSUY D 5.46 5 6 -1 16 8 -1.008 2.58 1.1hours 3min >10hours 86.15 5500 1.784 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02315 DWTKNIKDKIDKIIHDFVDK 20 EBOV-4 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available "[Ref:31473342]EBOV:EC50 = 6.29 plusminus 0.66 microM, 8.10 plusminus 0.63 microM, 6.67 plusminus 0.89 microM, 9.04 plusminus 1.23 microM; EC90 = 19.41 microM, 24.79 microM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342]EBOV-4 show cytotoxicity (CC50) at greater than 30 microM. No predicted structure available Cyclic cholesterylation PEG4 "In the peptide sequence, the cysteine residue at position 21 is modified with a PEG4-cholesterol (PEG4-Chol) moiety." L Glycoprotein. "Exact MoA explicitly not available (may interfere with the binding of the Ebola virus glycoprotein to host cell receptors, thereby preventing viral entry into host cells)." 2471.84 C113H179N29O33 ACEGLMOPQRSUY DK 6.75 5 5 0 13 7 -1.015 2.8 1.1hours 3min >10hours 92.5 5500 2.225 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02314 IEPHDWTKNITDKIDQIIHDFVDKTLPDQG 30 EBOV-3 Cholesterol-conjugated synthetic peptide No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available "[Ref:31473342]EBOV:EC50 = 12.89 plusminus 1.59 microM, 11.94 plusminus 2.59 microM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:31473342]EBOV-3 show cytotoxicity (CC50) at greater than 30 microM. No predicted structure available Cyclic cholesterylation PEG4 "In the peptide sequence, the cysteine residue at position 31 is modified with a PEG4-cholesterol (PEG4-Chol) moiety." L Glycoprotein. "EBOV-3 is an elongated peptide with five residues downstream of the helical domain. This modification likely contributes to the peptide's potency in inhibiting EBOV infection. By targeting specific regions of the EBOV glycoprotein, EBOV-3 interferes with viral entry and replication processes, ultimately inhibiting the virus's ability to infect host cells" 3532.91 C158H243N41O51 ACMORSUY D 4.52 3 7 -4 18 9 -0.88 2.35 20hours 30min >10hours 87.67 5500 1.557 31473342 Antiviral Res. 2019;171:104592.  "Pessi A, Bixler SL, Soloveva V, et al" Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo 10.1016/j.antiviral.2019.104592 Anti-EBOV DRAVPe02313 SGSWNFFDWFSGLMSWFGGPL 21  RVFV-10  Rift Valley fever virus (RVFV) Gc stem region P03518##P21401 Experimentally Validated 11588 GP Not Available 1137-1157 Not Available Not Available Not Available Not Available 6EGT EBOV Filoviridae Not Available [Ref:24069485]EBOV:IC50=50 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L DII domain of the E protein (RVFV-10 may interact with a specific region of the Ebola virus (EBOV) d "RVFV-10, a fusion-inhibiting peptide derived from the RVFV Gc stem region, displayed inhibitory effects against Ebola virus (EBOV) in a plaque-reduction assay, albeit less effectively than RVFV-6. Despite demonstrating weaker inhibition compared to RVFV-6, RVFV-10's efficacy against EBOV prompted further evaluation, ultimately leading to the selection of RVFV-6 for subsequent studies due to its superior inhibitory activity." 2425.7 C119H149N25O29S1 ACEHIKOQRTUVY FGS 3.8 0 1 -1 6 10 0.219 -0.28 1.9hours >20hours >10hours 37.14 16500 6.802 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR" "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02312 YGRKKRRQRRRGSGIEPHDWTKNITCKIOQIIHDFVDK 38 5-Link Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC50=15 microM No hemolysis information or data found in the reference(s) presented in this entry "[Ref:23962564]Vero cells incubated with concentrations of 5-Link exceeding 15 microM showed signs of toxicity by visual inspection, which prevented assessment of antiviral activity at higher concentra" No predicted structure available Linear Free Acetylation "The peptide sequence features N-terminal acetylation (Ac-), which enhances stability by protecting it from enzymatic degradation and making it more resistant to proteolysis. To further enhance the peptide's structure and function, alpha-helical stabilization can be introduced through covalent side chain-side chain cross-links. This is achieved by linking Cys at position 26 (C) with another suitable residue i.e., Ornithine (Orn) Ornithine (Orn) at position 29 (i.e., i and i+3). These cross-links " L Glycoprotein. "5-Link displayed antiviral activity against vesicular stomatitis virus particles containing the Ebola virus glycoprotein (VSV-GP), inhibiting infection at concentrations below 15 microM. It exhibited broad antiviral activity against both VSV-GP and VSV-G at lower concentrations, but induced toxicity in Vero cells at concentrations exceeding 15 microM, limiting further assessment. The peptide's specificity towards VSV-GP over VSV-G suggests a mechanism involving interference with viral entry, similar to its action against VSV-GP particles, thereby inhibiting Ebola virus infection. This indicates 5-Link's potential as a therapeutic agent targeting viral entry mediated by the Ebola virus glycoprotein." 4774.54 C210H343N71O55S1 ALMU R 10.6 11 4 7 25 8 -1.384 None 2.8hours 10min 2min 58.95 6990 1.464 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. "Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02311 YGRKKRRQRRRGSGIEPHDWTKCITOKIDQIIHDFVDK 38 4-Link Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC50=40 microM No hemolysis information or data found in the reference(s) presented in this entry "[Ref:23962564]Non-toxic (At 40 microM concentration, peptide 4-Link demonstrated good tolerance by Vero cells, as evaluated through visual examination and a commercial viability assay. At the same con" No predicted structure available Linear Free Acetylation "In the peptide sequence, N-terminal acetylation (Ac-) blocks the free amine group, protecting the peptide from exopeptidase degradation and increasing stability. To promote an alpha-helical conformation, side chain-side chain cross-links were introduced, particularly between Cys (C) at position 23 and an Ornithine (O) residue replacing Lys (K), positioned for cross-linking (at i and i + 3). These modifications help stabilize the helical structure, especially in regions predisposed to alpha-helix" L Glycoprotein. "Peptide 4-Link demonstrated strong neutralization of vesicular stomatitis virus particles carrying the Ebola virus glycoprotein (VSV-GP), resulting in a notable decrease in infection at a concentration of 40 microM. Its effectiveness against Ebola virus was evaluated by measuring the reduction in infection events induced by VSV-GP in its presence. Additionally, 4-Link displayed inhibitory effects on VSV particles bearing their native glycoprotein G (VSV-G), a lesser extent than VSV-GP, suggesting a degree of specificity towards the Ebola virus glycoprotein. These findings suggest that 4-Link likely targets the viral entry process common to both viruses, with a higher affinity for the Ebola virus glycoprotein, thereby inhibiting infection." 4775.52 C210H342N70O56S1 ALMNU R 10.28 11 5 6 25 8 -1.384 None 2.8hours 10min 2min 58.95 6990 1.464 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. "Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02310 KKKKGSGC 8 3-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC90=20 microM No hemolysis information or data found in the reference(s) presented in this entry "[Ref:23962564]Exceeding 15 microM, concentrations of 3-Chol caused observable toxicity in Vero cells, hindering the evaluation of its antiviral activity at higher doses." No predicted structure available Linear cholesterylation Free "In the peptide sequence, the cysteine residue at position 8 is modified with a cholesterol (Chol) moiety. HIV-1 C-peptide conjugated to cholesterol contain covalent side chain-side chain crosslinks to promote an alpha-helical conformation. The cholesterol-conjugated C-peptides proved to be potent inhibitors of Ebola virus glycoprotein (GP)-mediated cell entry (~10^3-fold reduction in infection at 40 microM" L Glycoprotein. "3-Chol, comprising a tetralysine segment linked to cholesterol, effectively inhibits both VSV-GP and VSV-G viral entry, with over 90% inhibition at higher concentrations. Despite lacking the GP CHR sequence, its activity against VSV-GP suggests a potential dependency on the native C-heptad repeat sequence. The study underscores the non-specific inhibitory role of cholesterol-conjugated peptides like 3-Chol against VSV-GP entry, implicating a mechanism involving both peptide and cholesterol components in inhibiting Ebola virus glycoprotein-mediated cell entry." 835.03 C34H66N12O10S1 ADEFHILMNOPQRTUVWY K 10.04 4 0 4 6 0 -1.837 2.8 1.3 hours 3min 3min 0 0 0 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. "Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02309 IEPHDWTKNITDKIDQIIHDFVDKGSGKKKKC 32 2-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC50=40 microM No hemolysis information or data found in the reference(s) presented in this entry [Ref:23962564]2-Chol showed only modest cell toxicity under certain conditions (see MoA). No predicted structure available Linear cholesterylation Free "In the peptide sequence, the cysteine residue at position 32 is modified with a cholesterol (Chol) moiety. HIV-1 C-peptide conjugated to cholesterol contain covalent side chain-side chain crosslinks to promote an alpha-helical conformation. The cholesterol-conjugated C-peptides proved to be potent inhibitors of Ebola virus glycoprotein (GP)-mediated cell entry (~10^3-fold reduction in infection at 40 microM" L Glycoprotein. "2-Chol was evaluated for its effectiveness against Ebola virus. The assay involved assessing the capacity of 2-Chol to inhibit GP-mediated viral entry using a vesicular stomatitis virus particle bearing the Ebola virus GP (VSV-GP) in place of the native glycoprotein G. The primary infection events were quantified by fluorescence confocal microscopy. Results showed that 2-Chol resulted in potent inhibition of VSV-GP entry, with approximately a 10^3-fold reduction in infection at 40 microM peptide concentrations. This level of inhibition was significantly higher than previously reported VSV-GP inhibition by Tat-Ebo at higher peptide concentrations. Notably, 2-Chol also exhibited potent activity for inhibiting VSV bearing its native envelope glycoprotein G (VSV-G), with over 90% reduction at 10 microM peptide concentration and more than 99% reduction at higher concentrations. Importantly, 2-Chol showed only modest cell toxicity under these conditions . Therefore, 2-Chol demonstrated potent inhibition of Ebola virus glycoprotein-mediated cell entry, suggesting a non-specific mechanism of neutralization that may involve a combination of peptide and cholesterol moieties." 3738.28 C166H266N46O50S1 ALMORUY K 8.12 7 6 1 21 8 -1.1 2.56 20hours 30min >10hours 70 5500 1.471 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. "Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02308 KKKKGSGIEPHDWTKNITDKIDQIIHDFVDK 32 1-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC50=50 microM No hemolysis information or data found in the reference(s) presented in this entry "[Ref:23962564]At certain concentrations, 1-Chol, a cholesterol-conjugated peptide inhibitor, demonstrates only a slight cell toxicity of approximately 20%, indicating a low level of toxicity within th" No predicted structure available Linear cholesterylation Free "In the peptide sequence, the cysteine residue at position 1 is modified with a cholesterol (Chol) moiety. This HIV-1 C-peptide conjugated to cholesterol contain covalent side chain-side chain crosslinks to promote an alpha-helical conformation. The cholesterol-conjugated C-peptides proved to be potent inhibitors of Ebola virus glycoprotein (GP)-mediated cell entry (~10^3-fold reduction in infection at 40 microM)" L Glycoprotein. "1-Chol, a cholesterol-conjugated C-peptide inhibitor, disrupts Ebola virus cell entry by targeting the glycoprotein-mediated fusion process. Specifically, it binds to the GP2 C-heptad repeat region (CHR), hindering the formation of the six-helix bundle crucial for membrane fusion. Effective at a concentration of 40 microM, 1-Chol's cholesterol conjugation enhances its alpha-helical structure independently of concentration, contributing to its broad inhibitory activity against Ebola virus. The combined peptide and cholesterol components of 1-Chol play a vital role in its inhibition of viral entry" 3635.14 C163H261N45O49 ACLMORUY K 8.32 7 6 1 20 8 -1.216 2.69 1.3 hours 3min 3min 72.26 5500 1.513 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. " Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking. 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02307 YGRKKRRQRRRGSGIEPHDWTKNITDKIDQIIHDFVDK 38 Tat-Ebo Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Not Available [Ref:23962564]EBOV:IC50=75 microM No hemolysis information or data found in the reference(s) presented in this entry [Ref:23962564]Low cytotoxicity (cytotoxicity assays indicated that Tat-Ebo was well tolerated by Vero cells at concentrations up to 75 microM). No predicted structure available Linear Free Free None L Viral membrane. " Tat-Ebo, a peptide combining HIV-1 Tat Arg-rich sequence with Ebola virus GP2 residues 610 - 633, combats Ebola virus within cells. It impedes viral membrane fusion by binding to a GP2 fusion intermediate, particularly targeting the extended conformation during fusion. Tat-Ebo enhances its antiviral efficacy by promoting internalization into cells and accumulating in endosomes. Its mode of action involves sequestering the extended intermediate, crucial for its effectiveness. Tat-Ebo's specificity lies in inhibiting filovirus GP proteins, including various strains, through sequestration. Demonstrating broad-spectrum inhibition, it effectively hampers infection mediated by diverse Ebola virus strains." 4664.27 C203H329N69O58 ACLMOU R 10.27 11 6 5 26 8 -1.634 4.38 2.8hours 10min 2min 58.95 6990 1.499 21454542## 23962564 J Biol Chem. 2011;286(18):15854-61;##Bioorg Med Chem Lett. 2013;23(19):5356-60. "Miller EH, Harrison JS, Radoshitzky SR;##Higgins CD, Koellhoffer JF, Chandran K," Inhibition of Ebola virus entry by a C-peptide targeted to endosomes;##C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1074/jbc.M110.207084;##10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02305 FFGSVLKLIPKIL 13 Temporin-PTa "Hylarana picturata, Asia" P0C8U2 Experimentally Validated 395594 Temporin-Pta(protein) Not Available 1 to 13 Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Antiviral Activity Assay "[Ref:30669255]HIV-1:EC50=0.63 uM,Tb inhibited viral replication at 5 μM,HSV-1:EC50=40 μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:30669255]Tb was tested at concentrations ranging from 5 (7 µg/mL) to 60 µM (84 µg/mL) [21]. Significant cytotoxicity was only observed at the highest concentration used (60 μM) with a cell viabil No predicted structure available Linear Free Free None L Membrane Inhibit Viral replication 1474.89 C75H123N15O15 ACDEHMNOQRTUWY L 10 2 0 2 3 8 1.508 -1.61 1.1hours 3min 2min 172.31 0 0 30669255 "Viruses, 11(1), 77." "Roy, M., Lebeau, L., Chessa, C., Damour, A., Ladram, A., Oury, B., Boutolleau, D., Bodet, C., & Lévêque, N. (2019)." Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1 10.3390/v11010077 Anti-HIV DRAVPe02306 QKKCPGRCTLKCGKHERPTLPYNCGKYICCVPVKVK 36 TEWP Red sea turtle Caretta caretta P0CAP0 Experimentally Validated 8467 TEWP Not Available 1-36 Not Available Not Available Not Available Not Available None CHAV Rhabdoviridae Viral Inhibition Assays [Ref:16700051]CHAV:IC50=10^5mM.Viral infection leads to shrinkage of cell volume by about 80% and addition of TEWP leads to recovery of the cell volume No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Pyroglutamatation Carboxylation "The N-terminal Q is pyroglutamate. There are three disulfide bonds: C1-C6; C2-C5; C3-C4, different from those of the vertebrate beta-defensins." L Not Found Antiviral action may occur because of inhibition of viral replication and/or transcription 4079.99 C177H297N53O45S6 ADFMOSUW K 9.54 9 1 8 23 6 -0.608 1.67 0.8hours 10min 10hours 56.67 3355 0.822 16700051 "Proteins, 64(2), 524–531." "Chattopadhyay, S., Sinha, N. K., Banerjee, S., Roy, D., Chattopadhyay, D., & Roy, S. (2006)." Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity 10.1002/prot.20963 Anti-CHAV DRAVPe02304 GMKCKFCCNCCNLNGCGVCCRF 22 SmHep2P "Turbot, Scophthalmus maximus" Q5CAP7##Q5CAJ5 Experimentally Validated 52904 "thp,TAPP" Not Available 52-73 Not Available Not Available Not Available Not Available None MV Paramyxoviridae Antiviral Assay [Ref:24647314]Significantly inhibit the megalocytivirus No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found These peptides inhibit viral propagation by disruption of the viral envelope and/or capsid 2406.97 C94H152N30O26S9 ADEHIOPQSTUWY C 8.53 3 0 3 14 5 0.523 0.7 30hours >20hours >10hours 30.91 500 0.208 24647314 "Fish & shellfish immunology, 38(1), 127–134." "Zhang, J., Yu, L. P., Li, M. F., & Sun, L. (2014)." Turbot (Scophthalmus maximus) hepcidin-1 and hepcidin-2 possess antimicrobial activity and promote resistance against bacterial and viral infection 10.1016/j.fsi.2014.03.011 Anti-MV DRAVPe02303 QSHISLCRWCCNCCKANKGCGFCCKF 26 SmHep1P "Turbot, Scophthalmus maximus" Q52PA0 Experimentally Validated 52904 hamp AAX92670.1 65-90 Not Available CM023543.1 mRNA "Primary_assembly 1: 14,423,721-14,424,529 forward strand." None MV Paramyxoviridae Antiviral Assay [Ref:24647314]Significantly inhibit the megalocytivirus No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found These peptides inhibit viral propagation by disruption of the viral envelope and/or capsid 2943.54 C121H188N38O32S8 DEMOPTUVY C 8.75 4 0 4 18 6 0.096 1.14 0.8hours 10min 10hours 33.85 6000 2.038 24647314 "Fish & shellfish immunology, 38(1), 127–134." "Zhang, J., Yu, L. P., Li, M. F., & Sun, L. (2014)." Turbot (Scophthalmus maximus) hepcidin-1 and hepcidin-2 possess antimicrobial activity and promote resistance against bacterial and viral infection 10.1016/j.fsi.2014.03.011 Anti-MV DRAVPe02302 CLGIGSCNDFAGCGYAIVCFW 21 Siamycin II Streptomyces strains AA3891 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae Antiviral Assay [Ref:7787424]Active against HIV-1 virus (replication inhibitor) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Amidation Free "It differs from Siamycin I only by one amino acid. Siamycin I has a valine residue at position 4. In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus (XXJ)." L Not Found "These peptides act by preventing oligomerization of the HIV transmembrane glycoprotein gp41, or by interfering with interactions between gp41 and the envelope glycoprotein gp120, the cell membrane or membrane-bound proteins.binding siamycin II or siamycin I may play a crucial role in blocking interactions between HIV and the T-cell surface, an essential step in the fusion process." 2199.56 C98H139N23O27S4 EHKMOPQRTU CG 3.8 0 1 -1 8 9 1.171 -0.98 1.2hours >20hours >10hours 79.05 7240 3.292 7787424 "ournal of biomolecular NMR, 5(3), 271–286. " "Constantine, K. L., Friedrichs, M. S., Detlefsen, D., Nishio, M., Tsunakawa, M., Furumai, T., Ohkuma, H., Oki, T., Hill, S., & Bruccoleri, R. E. (1995)." High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion 10.1007/BF00211754 Anti-HIV DRAVPe02301 CLGVGSCNDFAGCGYAVVCFW 21 Siamycin I Streptomyces strain AA6532 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV-1,HIV-2" Retroviridae Antiviral Assay "[Ref:8787894]HIV-1 RF (CEM-SS, CPE XTT) ED₅₀ = 0.35 ± 0.26 mM, HIV-1 IIIB (CEM-SS, CPE XTT) ED₅₀ = 0.6 ± 0.10 mM, HIV-2 CBL-20 (CEM-SS, CPE XTT) ED₅₀ = 0.45 ± 0.25 mM, HIV RF (MT-2, p24) ED₅₀ = 0.05 ± 0.02 mM, HIV-1 NL4-3 (MT-2, p24) ED₅₀ = 0.26 ± 0.29 mM, HIV-1 Y181C/NL4-3 (MT-2, p24) ED₅₀ = 0.16 ± 0.09 mM, HIV-1 A71T/V82A/NL4-3 (MT-2, p24) ED₅₀ = 0.45 ± 0.22 mM, HIV-1 A018A (MT-2, p24) ED₅₀ = 0.89 ± 0.09 mM, HIV-1 A018C (MT-2, p24) ED₅₀ = 0.89 ± 0.12 mM, SIV mac 251 (MT-2, p24) ED₅₀ = 3.2 ± 0.48 mM, HIV-1 008-PRE-D4T SI (1) (PBMC, p24) ED₅₀ = 4.3 ± 1.9 mM, HIV-1 008-POST-D4T SI (111) (PBMC, p24) ED₅₀ = 5.7 ± 2.1 mM, HIV-1 002-PRE-D4T NSI (PBMC, p24) ED₅₀ = 3.6 ± 0.9 mM, HIV-1 002-POST-D4T SI (1/2) (PBMC, p24) ED₅₀ = 2.0 ± 1.1 mM." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Amidation Free  disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19 L Not Found "Siamycin I acts as an HIV fusion inhibitor, specifically inhibiting the fusion between the HIV-1 gp160 envelope glycoprotein and CD4-expressing cells. It disrupts syncytium formation (fusion of infected cells with uninfected ones), which is a hallmark of HIV cytopathicity.In fusion assays, siamycin I at 0.08 µM reduced syncytium formation by 50% in a 4-hour coculture of HIV-1 RF-infected cells with uninfected T cells. It showed minimal effect on non-HIV fusion processes, indicating retrovirus-specific fusion inhibition." 2171.51 C96H135N23O27S4 EHIKMOPQRTU CG 3.8 0 1 -1 8 9 1.143 -0.9 1.2hours >20hours >10hours 69.52 7240 3.334 8557614 "The Journal of antibiotics, 48(12), 1515–1517." "Detlefsen, D. J., Hill, S. E., Volk, K. J., Klohr, S. E., Tsunakawa, M., Furumai, T., Lin, P. F., Nishio, M., Kawano, K., & Oki, T. (1995)" "Siamycins I and II, new anti-HIV-1 peptides: II. Sequence analysis and structure determination of siamycin I" 10.7164/antibiotics.48.1515 Anti-HIV DRAVPe02300 KTCENLADTY 10 Sesquin "Seeds, Vigna sesquipedalis, ground beans." P84868 Experimentally Validated 138955 Not Available Not Available 1 to 10 Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV reverse transcriptase inhibitory activity Assay "[Ref:15949629]HIV-1:(% inhibition at 50 μM) = 35 ± 3%,(% inhibition at 100 μM) = 45 ± 5%,(% inhibition at 200 μM) = 61 ± 2%." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found it inhibits HIV-1 reverse transcriptase. 1157.26 C48H76N12O19S1 FGHIMOPQRSUVW T 4.37 1 2 -1 8 2 -0.9 2.49 1.3 hours 3min 3min 49 1490 1.288 15949629 " Peptides, 26(7), 1120–1126." "Wong, J. H., & Ng, T. B. (2005). " "Sesquin, a potent defensin-like antimicrobial peptide from ground beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase" 10.1016/j.peptides.2005.01.003 Anti-HIV DRAVPe02299 NPAGCRFCCGCCPNMIGCGVCCRF 24 SA-hepcidin2 "Liver, spotted scat, Scatophagus argus" A0A142LQX2 Experimentally Validated None Hepcidin(protein) Not Available 65-88 Not Available Not Available Not Available Not Available None "SCRV, MsReV" Rhabdoviridae Antiviral Assay "[ReF:26845697]SCRV:IC50: 50 μM,MsReV:Ic50=25 μM,SA-hepcidin2 showed a dose-dependent protective effect against SCRV and MsReV.CPE in GCF and EPC monolayers after co-treatment with SA-hepcidins (50 μM) and virus (0.1TCID50)" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found direct effects on the virion and effects on the innate and adaptive immunity of target cells  2515.07 C99H156N32O27S9 DEHKLOQSTUWY C 8.23 2 0 2 12 6 0.717 0.41 1.4hours 3min >10hours 32.5 500 0.199 26845697 "Fish & shellfish immunology, 50, 191–199." "Gui, L., Zhang, P., Zhang, Q., & Zhang, J. (2016). " Two hepcidins from spotted scat (Scatophagus argus) possess antibacterial and antiviral functions in vitro 10.1016/j.fsi.2016.01.038 "Anti-SCRV, Anti-MsReV" DRAVPe02298 IIIQYEGHKH 10 Rondonin "Haemolymph, Eurypelma californicum and Acanthoscurria gomesiana;" B3EWP8 Experimentally Validated 1211104 Rondonin(protein) Not Available 1 to 10 Not Available Not Available Not Available Not Available None "McV, IAV, EMCV" Orthomyxoviridae Antiviral Activity Assay "[Ref:34254458]McV: Rondonin inhibited ½ dilution of the virus (MDCK, titer 1/256); H1N1: Rondonin inhibited 1/64 dilution (Vero Cells); Rondonin (6 µg) inhibited viral mRNA completely at 7.5 ng." No hemolysis information or data found in the reference(s) presented in this entry [Ref:34254458]Not cytotoxic against mammalian cells No predicted structure available Linear Free Free None L Not Found "the mechanism of action of this peptide probably involves internal components of the microorganisms. With these results of the RNA virus test, enveloped or not, we verified the protection of the cells, avoiding viral replication. At higher concentrations of rondonin, complete blocked of the DNA was observed, showing that the DNA was aggregated by rondonin" 1237.42 C57H88N16O15 ACDFLMNOPRSTUVW I 6.92 1 1 0 6 3 -0.55 1.16 20hours 30min >10hours 117 1490 1.204 34254458 "FEBS open bio, 11(9), 2541–2559." "Riciluca, K. C. T., Oliveira, U. C., Mendonça, R. Z., Bozelli Junior, J. C., Schreier, S., & da Silva Junior, P. I. (2021)." Rondonin: antimicrobial properties and mechanism of action  10.1002/2211-5463.13253 "Anti-McV,Anti-IAV,Anti-EMCV" DRAVPe02297 RICRCICGRRICRCICGR 18 Retrocyclin-3 Derived from a silent gene (pre-stop) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Luciferase Assay Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free three intramolecular disulfide bonds L Not Found " It binds to gp120 and CD4, thereby inhibiting HIV entry." 2140.71 C82H154N36O19S6 ADEFHKLMNOPQSTUVWY CR 9.69 6 0 6 12 4 0.289 3.34 1hours 2min 2min 86.67 375 0.175 15210812 "Journal of immunology (Baltimore, Md. : 1950), 173(1), 515–520." "Wang, W., Owen, S. M., Rudolph, D. L., Cole, A. M., Hong, T., Waring, A. J., Lal, R. B., & Lehrer, R. I. (2004)." Activity of alpha- and theta-defensins against primary isolates of HIV-1 10.4049/jimmunol.173.1.515 Anti-HIV DRAVPe02296 VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR 33 NP-1 Oryctolagus cuniculus (Rabbit) P01376 Experimentally Validated 9986 Corticostatin-3(protein) AAA31387.1 63-95 Not Available M28883 mRNA "Scaffold GL018713: 117,470-184,536 forward strand" None HSV-2 Herpesviridae Antiviral Assay [Ref:12543649] HSV-2:IC50= 98.7% ± 0.7%. NP-1 inhibited ∼90% of viral infection when added at t = 0 h.reduced viral infection by only 15% ± 8.3%.NP-1 reduced the number of plaques by 59.0% ± 16.6% compared to control acetic acid buffer No hemolysis information or data found in the reference(s) presented in this entry [Ref:12543649]No cytotoxic effect was observed even after 20 h of exposure to NP-1 at the concentration of 25 or 100 μg/ml No predicted structure available Linear Free Free None L Membrane "NP-1 followed by extensive washing still partially inhibits infection suggests that the defensin may interact with or persist locally on cell surfaces.NP-1,prevents VP16 from being translocated to the nucleus, suggesting that NP-1 blocks viral entry." 3897.79 C161H283N65O36S6 DKMNOQSTUWY R 11.4 10 1 9 18 11 -0.112 3.33 100hours >20hours >10hours 85.76 375 0.096 12543649 "Antimicrobial agents and chemotherapy, 47(2), 494–500" "Sinha, S., Cheshenko, N., Lehrer, R. I., & Herold, B. C. (2003)." "NP-1, a rabbit alpha-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2." 10.1128/AAC.47.2.494-500.2003 Anti-HSV DRAVPe02295 YFKSVRTGLRYVYCS 15 eVpeL2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae inhibitory Assay [Ref:28574091]EBOV:IC50 = 37 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Acetylation "In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration" L VP24 eVpeL2 exhibit inhibitory activity against the protein-protein interaction (PPI) of VP24 and KPNA5. 1842.15 C85H128N22O22S1 ADEHIMNOPQUW Y 9.63 3 0 3 10 4 -0.133 1.79 2.8hours 10min 2min 64.67 4470 2.427 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02293 YYSSRWNHGHFTPCS 15  eVpeL1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae inhibitory Assay Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Acetylation Amination "In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration" L VP24 "Exact MoA not known (eVpeL1, a macrocyclic peptide belonging to the GL1 group from the LY-library, was found to be a poor binder to the immobilized eVP24 compared to other peptides like eVpeD1 and eVpeD2)." 1841.98 C83H108N24O23S1 ADEIKLMOQUV S 8.21 1 0 1 11 2 -1.18 2.42 2.8hours 10min 2min 0 8480 4.604 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02294 YGRKKRRQRRRGSGIEPHDWTKNITDKIDQIIHDFVDK 38 Tat-Ebo Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref: 23962564]EBOV:IC50=75 microM No hemolysis information or data found in the reference(s) presented in this entry [Ref: 23962564]Low cytotoxicity (cytotoxicity assays indicated that Tat-Ebo was well tolerated by Vero cells at concentrations up to 75 microM). No predicted structure available Linear Free Free None L Viral membrane. " Tat-Ebo, a peptide combining HIV-1 Tat Arg-rich sequence with Ebola virus GP2 residues 610 - 633, combats Ebola virus within cells. It impedes viral membrane fusion by binding to a GP2 fusion intermediate, particularly targeting the extended conformation during fusion. Tat-Ebo enhances its antiviral efficacy by promoting internalization into cells and accumulating in endosomes. Its mode of action involves sequestering the extended intermediate, crucial for its effectiveness. Tat-Ebo's specificity lies in inhibiting filovirus GP proteins, including various strains, through sequestration. Demonstrating broad-spectrum inhibition, it effectively hampers infection mediated by diverse Ebola virus strains." 4664.27 C203H329N69O58 ACLMOU R 10.27 11 6 5 26 8 -1.634 4.38 2.8hours 10min 2min 58.95 6990 1.499 21454542;## 23962564 J Biol Chem. 2011;286(18):15854-61;##Bioorg Med Chem Lett. 2013;23(19):5356-60. "Miller EH, Harrison JS, Radoshitzky SR;##Higgins CD, Koellhoffer JF, Chandran K," Inhibition of Ebola virus entry by a C-peptide targeted to endosomes;##C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking 10.1074/jbc.M110.207084;##10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02292 RGGRLCYCRRRFCICV 16 Protegrin 2 "Leukocytes; porcine neutrophil, pig,S. scrofa" P32195 Experimentally Validated 9823 NPG2 Not Available 131-146 Not Available Not Available Not Available Not Available None "HSV-1,HSV-2.SARS-CoV-2" Herpesviridae BRET-based assay [Ref:37576748]SARS-CoV-2:IC50 values of 0.83 ± 0.07 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free Disulfide bridge formation was performed on crude peptides. L Not Found Not Available 1961.42 C81H137N31O18S4 ADEHKMNOPQSTUW R 9.88 5 0 5 10 4 0.044 3.18 1hours 2min 2min 66.88 1740 0.887 8647100##37576748 "Chem Pharm Bull (Tokyo). 1995 May;43(5):853-858##Computational and structural biotechnology journal, 21, 3665–3671." "Tamamura H, Murakami T, Horiuchi S, Sugihara K, Otaka A, Takada W, Ibuka T, Waki M, Yamamoto N, Fujii N##Jan, Z., Geethakumari, A. M., Biswas, K. H., & Jithesh, P. V. (2023)" "Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity##Protegrin-2, a potential inhibitor for targeting SARS-CoV-2 main protease Mpro"  10.1111/j.1432-1033.1996.0575p.x## 10.1016/j.csbj.2023.07.020 Anti-HSV DRAVPe02291 KKKKGSGIEPHDWTKNITDKIDQIIHDFVDK 32 1-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:23962564] Inhibition concentraion = 50 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear cholesterylation Free "In the peptide sequence, the cysteine residue at position 1 is modified with a cholesterol (Chol) moiety. This HIV-1 C-peptide conjugated to cholesterol contain covalent side chain-side chain crosslinks to promote an alpha-helical conformation. The cholesterol-conjugated C-peptides proved to be potent inhibitors of Ebola virus glycoprotein (GP)-mediated cell entry (~10^3-fold reduction in infection at 40 microM)" L Glycoprotein. "1-Chol, a cholesterol-conjugated C-peptide inhibitor, disrupts Ebola virus cell entry by targeting the glycoprotein-mediated fusion process. Specifically, it binds to the GP2 C-heptad repeat region (CHR), hindering the formation of the six-helix bundle crucial for membrane fusion. Effective at a concentration of 40 microM, 1-Chol's cholesterol conjugation enhances its alpha-helical structure independently of concentration, contributing to its broad inhibitory activity against Ebola virus. The combined peptide and cholesterol components of 1-Chol play a vital role in its inhibition of viral entry" 3635.14 C163H261N45O49 ACLMORUY K 8.32 7 6 1 20 8 -1.216 2.69 1.3 hours 3min 3min 72.26 5500 1.513 23962564 Bioorg Med Chem Lett. 2013;23(19):5356-60. " Higgins CD, Koellhoffer JF, Chandran K" C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking. 10.1016/j.bmcl.2013.07.056 Anti-EBOV DRAVPe02290 LTTKLWSSWGYYLGKKARWNLKHPYVQF 28 Plantaricin NC8 α Lactiplantibacillus plantarum; Lactobacillus plantarum NC8 I6TUU6 Experimentally Validated 337330 plnc8A Not Available 20-47 Not Available Not Available Not Available Not Available None "LGTV,IAV,HIV-1.SARS-CoV-2" "Orthomyxoviridae,Coronaviridae" Virus Inhibition assays "[Ref:36449554]KUNV:A final peptide concentration of 1 μM reduced the viral load by >50%, while concentrations of ≥10 μM completely eliminated all virions.L-PLNC8 αβ or D-PLNC8 αβ caused more than 99.9% reduction in the titer of infective KUNV,WNV:The virus particles are rapidly permeabilized by both enantiomers of PLNC8 αβ that decreased the viral load by >99.9% of WNV.A 50% reduction of PFU with the L- and D-form of PLNC8 αβ was achieved at 0.001 μM.SARS-CoV-2:A 50% reduction of PFU with the L- and D-form of PLNC8 αβ was achieved at 0.001 μM. PLNC8 β (L- and D-form) alone required ~0.5 μM to cause a 50% reduction of the viral load at the same SARS-CoV-2 virus concentration.IAV: reduced IAV by 50% at ~0.5 μM.HIV-1:50% reduction concentration was ~20 μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:36449554]Non Cytotoxic in Vero Cells and to human cells. No predicted structure available Linear Free Free A two-chain bacteriocin which requires chain B for optimal activity. The sequence of chain B is SVPTSVYTLGIKILWSAYKHRKTIEKSFNKGFYH L Membrane "it mainly targets the lipid compartment of virus envelopes, which is more or less stable since it is derived from membranes of infected host cells." 3472.06 C169H244N42O38 CDEIMOU KL 10.12 5 0 5 15 10 -0.654 1.03 5.5hours 3min 2min 69.64 20970 6.04 36449554 "PloS one, 17(11), e0278419." "Omer, A. A. M., Hinkula, J., Tran, P. T., Melik, W., Zattarin, E., Aili, D., Selegård, R., Bengtsson, T., & Khalaf, H. (2022)." Plantaricin NC8 αβ rapidly and efficiently inhibits flaviviruses and SARS-CoV-2 by disrupting their envelopes 10.1371/journal.pone.0278419 "Anti-LGTV,Anti-IAV,Anti-HIV.Anti-SARS-CoV-2" DRAVPe02289 GIFPKIIGKGIVNGIKSLAKGVGMKVFKAGLNNIGNTGCNNRDEC 45 Palustrin-3AR "the crawfish frog, Rana areolata, North America" No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Anti-HIV activity Assay [Ref:16140737]HIV-1:This peptide could inhibit HIV infection at a concentration that is also toxic to T cells No hemolysis information or data found in the reference(s) presented in this entry [Ref:16140737]Non Cytotoxic No predicted structure available Linear Free Free None L Not Found Not Available 4647.5 C203H342N60O58S3 HOQUWY G 9.79 7 2 5 19 16 0.016 0.78 30hours >20hours >10hours 93.11 125 0.027 16140737 " Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)" Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe02288 CLGVGSCNDFAGCGYAIVCFW 21 NP-06 Streptomyces strain AA6532 P85078 Experimentally Validated 1931 Tricyclic peptide MS-271 (protein) 1 to 21 Not Available Not Available Not Available Not Available None HIV-1 Retroviridae HIV cytopathic effect inhibition assay "[Ref:8619594]HIV-1LAI:IC50=2.8 mM,HIV-2ROD:IC50=6.0 mM,HIV-1ERS104pre:IC50=1.3 mM" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:8619594]HIV-1LAI:CC50=28 mM,HIV-2ROD:CC50=0.23 mM,HIV-1ERS104pre:CC50=33 mM" No predicted structure available Cyclic Amidation Carboxylation A disulfide bond between Cys-7 and Cys-19 was also indicated by the cross peak between Hb of Cys-7 and Hb of Cys-1. L Membrane "NP-06 appears to block the early stage of HIV-1 infection, most likely at the stage of virus-cell fusion." 2185.53 C97H137N23O27S4 EHKMOPQRTU CG -0.94 0 1 -1 8 9 1.157 -1.157 1.2hours >20hours >10hours 74.29 7240 3.313 8619594 "Chokekijchai, S., Kojima, E., Anderson, S., Nomizu, M., Tanaka, M., Machida, M., Date, T., Toyota, K., Ishida, S., & Watanabe, K. (1995). " "Antimicrobial agents and chemotherapy, 39(10), 2345–2347." NP-06: a novel anti-human immunodeficiency virus polypeptide produced by a Streptomyces species 10.1128/AAC.39.10.2345 Anti-HIV DRAVPe02287 SCASRCKGHCRARRCGYYVSVLYRGRCYCKCLRC 34 Mytilin B "Blue mussel, Mytilus edulis and M. galloprovincialis" P81613 Experimentally Validated 6550 Not Available Not Available 1-34 Not Available Not Available Not Available Not Available None WSSV Nimaviridae Antiviral Assay [Ref:14986940] WSSV:multiplication was prevented by the preincubation with 10 or 50 lm mytilin. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Amidation Carboxylation None L Not Found Not Available 3981.76 C163H267N59O42S8 DEFIMNOPQTUW C 9.58 9 0 9 25 6 -0.344 2.83 1.9hours >20hours >10hours 45.88 6460 1.622 14986940 "Journal of fish diseases, 27(1), 57–64." "Dupuy, J. W., Bonami, J. R., & Roch, P. (2004)" A synthetic antibacterial peptide from Mytilus galloprovincialis reduces mortality due to white spot syndrome virus in palaemonid shrimp 10.1046/j.1365-2761.2003.00516.x Anti-WSSV DRAVPe02286 QEAQSVACTSYYCSKFCGSAGCSLYGCYLLHPGKICYCLHCSR 43 Myticin C "The mediterranean mussel, Mytilus galloprovincialis" A7DWS7 Experimentally Validated 29158 mync_MYTGA Not Available 18-60 Not Available Not Available Not Available Not Available None "HSV-1,HSV-2,VHSV" Herpesviridae  Viral Infectivity Assays "[Ref:21858010]VHSV:The results showed ≥85% reduced VHSV infectivity in CHSE cells transfected with Myt C.[Ref:23880927]VHSV:Maximal inhibition of viral infectivity (40%) was observed when 125 μM of red-MytCc were pre-incubated with VHSV.[Ref:27307570]The viral titer in infected oyster hemocytes treated with synthetic myticin decreased by 99.95% at 24 h. HSV-1:EC50=5.85 ± 1.24 μM (25.98 ± 5.49 μg/ml),HSV-2:EC50 =5.41 ± 0.95 μM (24.03 ± 4.21 μg/ml)," No hemolysis information or data found in the reference(s) presented in this entry "[Ref:23880927]No cytotoxicity was observed when the Epithelioma Papulosum Cyprini (EPC) cell monolayers were treated with synthetic red-MytCc at concentrations up to 125 μM during 72 h, indicating tha" No predicted structure available Linear Free Free None L Not Found "CHSE cells expressing Myt C had reduced susceptibility to VHSV.viral replication could not be detected in the cells expressing the Myt C variants but was detected in the surrounding non-expressing cells.very low levels of VHSV replication could be detected in the CHSE Myt C-expressing cells compared with the eGFP-transfected or non-transfected cells, suggesting the induction of some protective effect on the surrounding cells by the expression of Myt C, which could act as a cytokine-like molecule. " 4705.44 C202H304N54O60S8 DMNOUW C 8.19 7 4 3 28 10 0.179 0.6 0.8hours 10min 10hours 59.07 7950 1.69 21858010##23880927##27307570 "PloS one, 6(8), e23140##Marine drugs, 11(7), 2328–2346##journal of virology, 90(17), 7692–7702." "Balseiro, P., Falcó, A., Romero, A., Dios, S., Martínez-López, A., Figueras, A., Estepa, A., & Novoa, B. (2011)##Martinez-Lopez, A., Encinar, J. A., Medina-Gali, R. M., Balseiro, P., Garcia-Valtanen, P., Figueras, A., Novoa, B., & Estepa, A. (2013)##Novoa, B., Romero, A., Álvarez, Á. L., Moreira, R., Pereiro, P., Costa, M. M., Dios, S., Estepa, A., Parra, F., & Figueras, A. (2016)." Mytilus galloprovincialis myticin C: a chemotactic molecule with antiviral activity and immunoregulatory properties##pH-dependent solution structure and activity of a reduced form of the host-defense peptide myticin C (Myt C) from the mussel Mytilus galloprovincialis##Antiviral Activity of Myticin C Peptide from Mussel: an Ancient Defense against Herpesviruses 10.1371/journal.pone.0023140##10.3390/md11072328##10.1128/JVI.00591-16 "Anti-HSV,Anti-VSHRV" DRAVPe02285 KYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWKS 43 Mundticin(CRL35) Enterococcus mundtii NFRI 7397 B6DSR2 Experimentally Validated 1352 mundKS Not Available 16-58 Not Available Not Available Not Available Not Available None HSV Herpesviridae Antiviral Assay "[Ref:10493605]HSV-1 (F):Vero cells:Inhibition = 97.0%, BHK-21 cells:Inhibition = 99.2%.HSV-2 (G):Vero cells:Inhibition = 98.8%, BHK-21 cells:Inhibition = 98.8%.HSV-1 (B2006):Vero cells:Inhibition = 92.4%, BHK-21 cells:Inhibition = 96.7%.HSV-1 (F): EC50 = 11 µg/ml,HSV-1 (B2006): EC50 = 53 µg/ml,HSV-1 (KOS): EC50 = 60 µg/ml for Enterocin,HSV-1 (Field): EC50 = 76 µg/ml for Enterocin,HSV-2 (G): EC50 = 15 µg/ml for Enterocin" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:10493605]CC50 of CRL35:HSV-1 (F): 1363.64 µg/ml,HSV-1 (B2006): 283.02 µg/ml,HSV-1 (KOS): 250.00 µg/ml,HSV-1 (Field isolate): 197.37 µg/ml,HSV-2 (G): 1000.00 µg/ml." No predicted structure available Linear Free Free None L Not Found Enterocin CRL35 exerted a significant inhibitory effect in vitro on the replication of several HSV strains. 4289.81 C186H291N55O58S2 EFHMOPQRU G 9.45 5 1 4 20 14 -0.253 0.73 1.3 hours 3min 3min 63.72 14105 3.288 10493605 "International journal of antimicrobial agents, 12(4), 293–299." "Wachsman, M. B., Farías, M. E., Takeda, E., Sesma, F., de Ruiz Holgado, A. P., de Torres, R. A., & Coto, C. E. (1999)." Antiviral activity of enterocin CRL35 against herpesviruses 10.1016/s0924-8579(99)00078-3 Anti-HSV DRAVPe02284 WYQLIRTFGNLIHQKYRKLLEAYRKLRD 28 ModoCath5 "The gray short-tailed opossum, Monodelphis domestica, South America" F6W4B4 Experimentally Validated 13616 Not Found Not Found 133-160 Not Available CM000373.1 Not Found "Primary_assembly 6: 195,029,250-195,034,644 reverse strand." None WNV Flaviviridae Antiviral Assay "[Ref:32194564]ΔModoCath5, resulting in approximately 500-fold decrease in virus production" No hemolysis information or data found in the reference(s) presented in this entry "[Ref:32194564]CC₅₀:HEK293T: 93.7% (8 µg/mL), 67.4% (16 µg/mL), 47.8% (32 µg/mL), 35.0% (64 µg/mL),Human primary keratinocytes: 98.1% (8 µg/mL), 96.2% (16 µg/mL), 79.1% (32 µg/mL), 48.9% (64 µg/mL),MCF" No predicted structure available Linear Free Free None L Not Found "The presence of ΔModoCath5 resulted in lower CXCL10, IFIT2, and IL28A mRNA levels, which can be related to the reduced viral replication in keratinocytes treated with this peptide. While viperin expression was not modified, ΔModoCath5 tended to increase ISG20 expression in WNV-infected keratinocytes. However, at the protein level, type III interferon secretion in response to WNV infection was not modulated by ΔModoCath5 treatment" 3623.27 C169H265N49O40 CMOPSUV L 10.28 7 2 5 17 10 -0.846 2.66 2.8hours 3min 2min 101.07 9970 2.752 32194564 "Broad Spectrum of Pathogens Including West Nile Virus. Frontiers in immunology, 11, 347." "Cho, H. S., Yum, J., Larivière, A., Lévêque, N., Le, Q. V. C., Ahn, B., Jeon, H., Hong, K., Soundrarajan, N., Kim, J. H., Bodet, C., & Park, C. (2020)." Opossum Cathelicidins Exhibit Antimicrobial Activity Against a Broad Spectrum of Pathogens Including West Nile Virus 10.3389/fimmu.2020.00347 Anti-WNV DRAVPe02283 VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR 33 MCP-2 "Macrophage, lung, Rabbit,Oryctolagus cuniculus" P01377 Experimentally Validated 9986 Defensin alpha 4(protein) AAA31390.1 63-95 Not Available M28884 mRNA "Scaffold GL018713: 117,470-184,536 forward strand." None HSV-1 Herpesviridae Antiviral Assay [Ref:2985808]HSV-1:IC50=3.68 ± 0.11μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found MCP-1 and MCP-2 can directly neutralize several viruses in vitro and that HSV-1 strain Maclntyre and vesicular stomatitis virus strain Indiana are particularly susceptible to their action. 3854.76 C161H282N62O36S6 DKMNOQSTUWY R 11.12 9 1 8 17 12 0.139 2.73 100hours >20hours >10hours 97.58 375 0.097 2985808 "Journal of virology, 54(2), 467–472." "Lehrer, R. I., Daher, K., Ganz, T., & Selsted, M. E. (1985)." "Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes" 10.1128/JVI.54.2.467-472.1985 Anti-HSV DRAVPe02282 GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR 34 Rabbit neutrophil defensin 3a "Rabbit, O. cuniculus" P07469 Experimentally Validated 9986 Corticostatin 1(protein) 60-93 Not Available Not Available Not Available Not Available None IAV Orthomyxoviridae Antiviral Assay [Ref:12543649]IAV:(reduction >1.1 log). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free Three disulfide bridges L Not Found Not Available 4003.65 C163H265N63O44S6 DHKLMOQTUW R 10.2 9 1 8 23 7 -0.638 3.87 30hours >20hours >10hours 76.04 3355 0.838 12543649 "Antimicrobial agents and chemotherapy, 47(2), 494–500" "Sinha, S., Cheshenko, N., Lehrer, R. I., & Herold, B. C. (2003)." "NP-1, a rabbit alpha defensin, prevents the entry and intercellular spread of herpes simplex virus type 2." 10.1128/AAC.47.2.494-500.2003 Anti-IAV DRAVPe02281 SCTTCVCTCSCCTT 14 Micrococcin P1 "Staphylococcus epidermidis strain 115; Staphylococcus equorum WS 2733, from a French red smear cheese" No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae HCVcc inhibition assay "[Ref:27387825]HCV:H77 (Huh7.5 cells), EC₅₀ = 0.222 ± 0.064 μM;Jc1 (Huh7.5 cells), EC₅₀ = 0.396 ± 0.016 μM;S52 (Huh7.5 cells), EC₅₀ = 0.141 ± 0.004 μM;DE43 (Huh7.5 cells), EC₅₀ = 0.269 ± 0.002 μM;SA13 (Huh7.5 cells), EC₅₀ = 0.339 ± 0.054 μM;HK6a (Huh7.5 cells), EC₅₀ = 0.325 ± 0.027 μM;QC69 (Huh7.5 cells), EC₅₀ = 0.304 ± 0.093 μM;JFH1-GFP (Huh7.5 cells), EC₅₀ = 0.80 ± 0.28 μM;Jc1 Renilla (Huh7.5 cells), EC₅₀ = 0.52 ± 0.08 μM; TN NanoLuc (Huh7.5 cells), EC₅₀ = 0.54 ± 0.01 μM" No hemolysis information or data found in the reference(s) presented in this entry [Ref:27387825]CC50 was 11.5 ± 0.14 μM No predicted structure available Linear Free Free None L Membrane "Micrococcin P1 strongly inhibits HCV attachment similar to anti-CD81 antibodies. however, its effect was shown prior to fusion of the viral envelope to the endosomal membrane " 1415.66 C49H86N14O22S6 ADEFGHIKLMNOPQRUWY C 5.23 0 0 0 13 1 1.007 0.56 1.9hours >20hours >10hours 20.71 375 0.265 27387825 "Antiviral research, 132, 287–295." "Lee, M., Yang, J., Park, S., Jo, E., Kim, H. Y., Bae, Y. S., & Windisch, M. P. (2016)." "Micrococcin P1, a naturally occurring macrocyclic peptide inhibiting hepatitis C virus entry in a pan-genotypic manner" 10.1016/j.antiviral.2016.07.002 Anti-HCV DRAVPe02280 VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR 33 MCP-1 Oryctolagus cuniculus (Rabbit) P01376 Experimentally Validated 9986 Not Found AAA31387.1 63-95 Not Available M28883 mRNA "Scaffold GL018713: 117,470-184,536 forward strand." None HSV-2 Herpesviridae Antiviral Assay [Ref:12543649]HSV-1:IC50=15% ± 8.3%.NP-1 reduced the number of plaques by 59.0% ± 16.6%.HSV-2:IC50=infection by 98.7% ± 0.7% No hemolysis information or data found in the reference(s) presented in this entry [Ref:12543649]No cytotoxic effect was observed even after 20 h of exposure to NP-1 at the concentration of 25 or 100 μg/ml No predicted structure available Linear Free Free None L Membrane "NP-1, a cationic peptide, does not compete with viral envelope glycoproteins for binding to cellular heparan sulfate receptors, but it prevents viral entry.NP-1 prevents virally mediated fusion events, entry, and cell-to-cell spread" 3897.79 C161H283N65O36S6 DKMNOQSTUWY R 11.4 10 1 9 18 11 -0.112 3.33 100hours >20hours >10hours 85.76 375 0.096 12543649 "Antimicrobial agents and chemotherapy, 47(2), 494–500" "Sinha, S., Cheshenko, N., Lehrer, R. I., & Herold, B. C. (2003)." "NP-1, a rabbit alpha-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2." 10.1128/AAC.47.2.494-500.2003 Anti-HSV DRAVPe02279 GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ 34 mCRAMP "Adult testis, spleen, stomach, and intestine, Mice, M. musculus" A0A8C6H0U3 Experimentally Validated 10103 Not Found Not Found 140-173 Not Available Not Available Not Found "Primary_assembly QGOO01036336.1: 6,325-8,294 forward strand." None "RSV,ZIKV" Flaviviridae Antiviral Assay "[Ref:35038500]ZIKV:IC50=At 5, 10, 20 μg/mL concentrtion attenuated ZIKV CPE by 39.8%, 68.9%, 90.1%, respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Found "CRAMP can combat ZIKV outside cells, and consequently inhibit viral attachment and entry.Cathelicidin CRAMP significantly inhibited the attachment and entry of ZIKV in Vero cells" 3878.66 C178H302N50O46 ACDHMOSTUWY K 10.22 9 3 6 17 10 -0.894 1.74 30hours >20hours >10hours 88.82 0 0 26873992##35038500 "Journal of immunology (Baltimore, Md. : 1950), 196(6), 2699–2710##Antiviral research, 198, 105248." "Currie, S. M., Gwyer Findlay, E., McFarlane, A. J., Fitch, P. M., Böttcher, B., Colegrave, N., Paras, A., Jozwik, A., Chiu, C., Schwarze, J., & Davidson, D. J. (2016)##Liu, Z., Wu, J., Qin, Z., Dong, C., Yang, H., Sun, J., Xu, W., & Wei, L. (2022)" Cathelicidins Have Direct Antiviral Activity against Respiratory Syncytial Virus In Vitro and Protective Function In Vivo in Mice and Humans##Endogenous cathelicidin is required for protection against ZIKV-caused testis damage via inactivating virons 10.4049/jimmunol.1502478##10.1016/j.antiviral.2022.105248 "Anti-RSV,Anti-ZIKV" DRAVPe02278 KINNPVSCLRKGGRCWNRCIGNTRQIGSCGVPFLKCCKRK 40 MBD-3 "Epithelia, respiratory system and other mucosal surfaces, mouse, M. musculus" Q9WTL0 Experimentally Validated 10090 Defb3 AA065510##AJ011800## AF092929 24-63 Not Available CM001001.3 Genomic DNA "Chromosome 8: 19,343,376-19,345,307 forward strand." None IAV Orthomyxoviridae Cell transfection Assay [Ref:24632574]IAV:TCID50=3.4815 ± 0.1844 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane mBD1-mBD3 expressed by the recombinant plasmid pcDNA3.1(+)/mBD1-mBD3 could inhibit influenza A virus replication both in vitro and in vivo. 4495.41 C189H322N66O49S6 ADEHMOUY C 10.26 10 0 10 24 9 -0.515 2.33 1.3 hours 3min 3min 63.25 5875 1.307 22345365##19301094 "Antiviral chemistry & chemotherapy, 22(6), 255–262##Archives of virology, 154(4), 639–647" "Jiang, Y., Yang, D., Li, W., Wang, B., Jiang, Z., & Li, M. (2012)##Jiang, Y., Wang, Y., Kuang, Y., Wang, B., Li, W., Gong, T., Jiang, Z., Yang, D., & Li, M. (2009)" Antiviral activity of recombinant mouse β-defensin 3 against influenza A virus in vitro and in vivo##Expression of mouse beta-defensin-3 in MDCK cells and its anti-influenza-virus activity 10.3851/IMP2077##10.1007/s00705-009-0352-6 Anti-IAV DRAVPe02277 DQYKCLQHGGFCLRSSCPSNTKLQGTCKPDKPNCCKS 37 mBD-1 Mus musculus P56386 Experimentally Validated 10090 Defb1 AA071757 33-69 Not Available CM001001.3 mRNA "Chromosome 8: 22,266,615-22,285,201" None IAV Orthomyxoviridae Cell transfection Assay [Ref:24632574]IAV:TCID50=4.1667 ± 0.1443 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane mBD1-mBD3 expressed by the recombinant plasmid pcDNA3.1(+)/mBD1-mBD3 could inhibit influenza A virus replication both in vitro and in vivo. 4076.68 C168H272N52O54S6 AEIMOUVW C 8.89 6 2 4 27 4 -0.93 2.3 1.1hours 3min >10hours 31.62 1865 0.457 24632574 "Viruses, 6(3), 1237–1252." "Li, W., Feng, Y., Kuang, Y., Zeng, W., Yang, Y., Li, H., Jiang, Z., & Li, M. (2014)." Construction of eukaryotic expression vector with mBD1-mBD3 fusion genes and exploring its activity against influenza A virus 10.3390/v6031237 Anti-IAV DRAVPe02276 ILGPVISTIGGVLGGLLKNL 20 Maximin H1 "B. maxima, China, Asia" P83080##P83081 Experimentally Validated 161274 Not Available Not Available 124-143 Not Available Not Available Not Available Not Available 7OVZ HIV Retroviridae Anti-HIV activity Assay Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Amidation Free None L Not Found Not Available 1934.39 C90H160N22O24 ACDEFHMOQRUWY GL 8.75 1 0 1 4 10 1.42 -1.69 20hours 30min >10hours 185 0 0 11835991 " Peptides, 23(3), 427–435." "Lai, R., Zheng, Y. T., Shen, J. H., Liu, G. J., Liu, H., Lee, W. H., Tang, S. Z., & Zhang, Y. (2002)." Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima 10.1016/s0196-9781(01)00641-6 Anti-HIV DRAVPe02275 GLFVGVLAKVAAHVVPAIAEHF 22 Maculatin 1.1 "Skin secretions, Litoria genimaculate, Litoria eucnemis, Australia" No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae HIV infection and cell viability assay [Ref:16140737]HIV-1:IC50=11.3 μM No hemolysis information or data found in the reference(s) presented in this entry [Ref: 16140737] Non toxic to target cells No predicted structure available Linear Free Free None L Envelope/outer leaflet of the membrane "Maculatin 1.1 is an amphibian-derived antimicrobial peptide that demonstrates potent inhibitory effects on HIV infection and transmission. It prevents HIV by disrupting the viral envelope, a critical structure required for viral fusion with target cells. When preincubated with the virus, maculatin 1.1 effectively blocks viral fusion, thereby preventing the virus from entering T cells. This peptide also exhibits the remarkable ability to inhibit the transfer of HIV from dendritic cells (DCs) to T cells, even when DCs are exposed to the peptide up to eight hours after capturing the virus. By accessing and destroying DC-sequestered HIV, maculatin 1.1 halts the progression of infection. These properties, coupled with its non-toxic effects on target cells, suggest that maculatin 1.1 holds significant promise as a topical inhibitor for mucosal HIV transmission and provides a novel approach to understanding the complex mechanisms of HIV capture and transfer by DCs." 2245.7 C108H169N27O25 CDMNOQRSTUWY AV 6.92 1 1 0 4 15 1.432 -1.37 30hours >20hours >10hours 141.82 0 0 16140737 " Journal of virology, 79(18), 11598–11606." "VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)" Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells 10.1128/JVI.79.18.11598-11606.2005 Anti-HIV DRAVPe02274 KTCENLADTFRGPCFATSNC 20 Lunatusin Phaseolus lunatus L. (lima bean) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV Retroviridae ELISA [Ref:16269344]HIV-1: IC50=120 μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:16269344]The findings indicate that lunatusin was devoid of cytotoxicity on mammalian splenocytes at concentrations below 50 μM. No predicted structure available Linear Free Free None L Not Found This 7 kDa isolate can reduce the activity of HIV-1 reverse transcriptase. 2178.44 C90H140N26O31S3 HIMOQUVWY CT 6.05 2 2 0 13 5 -0.34 2.05 1.3 hours 3min 3min 29.5 125 0.057 16269344 "Peptides, 26(11), 2086–2092." "Wong, J. H., & Ng, T. B. (2005)." "Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.)" 10.1016/j.peptides.2005.03.004 Anti-HIV DRAVPe02273 SMWSGMWRRKLKKLRNALKKKLKGE 25 Latarcin 1 Lachesana tarabaevi Q1ELT9 Experimentally Validated 379576 Lt1a Not Available 63-87 Not Available Not Available Not Available Not Available 2PCO DENV Filoviridae Dengue NS2B-NS3 protease Assay "[Ref:24885331]Dengue protease NS2B-NS3pro (37°C) IC₅₀ = 12.68 ± 3.2 μM,Dengue protease NS2B-NS3pro (40°C) IC₅₀ = 6.58 ± 4.1 μM,Reduction in viral RNA (24 h) EC₅₀ = 8.3 ± 1.2 μM,Reduction in viral RNA (48 h) EC₅₀ = 7.6 ± 2.7 μM,Reduction in viral RNA (72 h) EC₅₀ = 6.8 ± 2.5 μM." No hemolysis information or data found in the reference(s) presented in this entry [Ref:24885331]The CC50 value of the Ltc 1 peptide obtained via the optimisation steps was estimated to be approximately 52.51 ± 3.6 μM No predicted structure available Linear Free Free None L NS2B-NS3 The Ltc 1 peptide exhibited significant inhibitory effects against dengue NS2B-NS3pro and virus replication in the infected cells 3073.8 C138H238N44O31S2 DCQHIFPTYV K 11.77 10 1 9 14 9 -1.248 2.84 1.9hours >20hours >10hours 18.36 11000 3.579 24885331 "BMC microbiology, 14, 140" "Rothan, H. A., Bahrani, H., Rahman, N. A., & Yusof, R. (2014)" Identification of natural antimicrobial agents to treat dengue infection: In vitro analysis of latarcin peptide activity against dengue virus 10.1186/1471-2180-14-140 Anti-DENV DRAVPe02272 SDWSLWECCSTGSLFACC 18 Labyrinthopeptin A2 A.namibiensis C0MP60 Experimentally Validated 182080 labA2 Not Available 21-38 Not Available Not Available Not Available Not Available None "DENV,ZIKV,WNV,HCV,CHIKV,KSHV,CMV,HSV" Herpesviridae Antiviral Assay "[Ref:3166638]CHIKV (pseudotype) IC₅₀ = >5.0 μM,DENV-1 IC₅₀ = 12.0 μM,DENV-2 (Huh-7, high content imaging) IC₅₀ = 8.0 μM,DENV-2 (Huh-7, qRT-PCR) IC₅₀ = 7.6 μM,DENV-2 (MDDC, flow cytometry) IC₅₀ = 5.2 μM,DENV-2 (MDDC, qRT-PCR) IC₅₀ = 4.2 μM,DENV-3 IC₅₀ = 9.4 μM,DENV-4 IC₅₀ = 4.0 μM,HCMV IC₅₀ = 5.4 μM,HCV IC₅₀ = 1.7 μM,HSV-1 IC₅₀ = 12.4 μM,HSV-1 (Tk-deficient) IC₅₀ = 10.7 μM,HSV-2 IC₅₀ = 5.5 μM,HSV-2 (Tk-deficient) IC₅₀ = 3.2 μM,KSHV IC₅₀ = 15.0 μM,TBEV IC₅₀ = >26.0 μM,WNV IC₅₀ = 0.7 μM,ZIKV-976 (Huh-7, high content imaging) IC₅₀ = 9.6 μM,ZIKV-976 (Huh-7, qRT-PCR) IC₅₀ = 5.7 μM,ZIKV-H/PF-2013 (Huh-7, high content imaging) IC₅₀ = 3.3 μM,ZIKV-H/PF-2013 (Huh-7, qRT-PCR) IC₅₀ = 3.4 μM." No hemolysis information or data found in the reference(s) presented in this entry "[Ref:3166638]Labyrinthopeptins exhibited low cytotoxicity and had favorable pharmacokinetic properties in mice (half-life [t1/2] = 10.0 h)," No predicted structure available Linear Free Free None L Membrane LabyA2 exert the antiviral function by disrupting viral envelopes (virolysis). 1998.24 C85H120N20O28S4 RNQHIKMPYVOU CS 3.67 0 2 -2 10 6 0.506 0.35 1.9hours >20hours >10hours 48.89 11250 5.63 31666384 "Journal of virology, 94(2), e01471-19" "Prochnow, H., Rox, K., Birudukota, N. V. S., Weichert, L., Hotop, S. K., Klahn, P., Mohr, K., Franz, S., Banda, D. H., Blockus, S., Schreiber, J., Haid, S., Oeyen, M., Martinez, J. P., Süssmuth, R. D., Wink, J., Meyerhans, A., Goffinet, C., Messerle, M., Schulz, T. F., … Brönstrup, M. (2020)." Labyrinthopeptins Exert Broad-Spectrum Antiviral Activity through Lipid-Binding-Mediated Virolysis 10.1128/JVI.01471-19 "Anti-DENV,Anti-ZIKV,Anti-WNV,Anti-HCV,Anti-CHIKV,Anti-KSHV,Anti-CMV,Anti-HSV,Anti-HIV" DRAVPe02271 SNASVWECCSTGSWVPFTCC 20 Labyrinthopeptin A1 Actinomycete Actinomadura namibiensis DSM 6313 C0MP59 Experimentally Validated 182080 labA1 Not Available 21-40 Not Available Not Available Not Available Not Available None "DENV,ZIKV,WNV,HCV,CHIKV,KSHV,CMV,HSV-2,HIV-1" Retroviridae Antiviral Assay "[Ref:3166638]CHIKV IC₅₀ = 2.2 μM,CHIKV (pseudotype):IC₅₀ = 1.8 μM,DENV-1 IC₅₀ = 0.8 μM,DENV-2 (Huh-7, high content imaging):IC₅₀ = 1.8 μM,DENV-2 (Huh-7, qRT-PCR) :IC₅₀ = 2.0 μM,DENV-2 (MDDC, flow cytometry): IC₅₀ = 0.4 μM,DENV-2 (MDDC, qRT-PCR): IC₅₀ = 0.3 μM,DENV-3 IC₅₀ = 1.1 μM,DENV-4: IC₅₀ = 0.3 μM,HCMV:IC₅₀ = 1.3 μM,HCV:IC₅₀ = 1.1 μM,HIV (laboratory strain, MT-4 T cells);IC₅₀ = 1.9 μM,HIV (laboratory strain, PBMC):IC₅₀ = 1.7 μM,HIV (laboratory strain, MDM):IC₅₀ = 2.4 μM,HIV (clinical isolate, PBMC):IC₅₀ = 1.0 μM,HSV-1:IC₅₀ = 1.6 μM,HSV-1 (Tk-deficient):IC₅₀ = 1.9 μM,HSV-2:IC₅₀ = 0.4 μM,HSV-2 (Tk-deficient):IC₅₀ = 0.3 μM,KSHV:IC₅₀ = 2.0 μM,TBEV:IC₅₀ = 24.1 μM,WNV:IC₅₀ = 0.2 μM,ZIKV-976 (Huh-7, high content imaging):IC₅₀ = 2.0 μM,ZIKV-976 (Huh-7, qRT-PCR):IC₅₀ = 1.8 μM,ZIKV-H/PF-2013 (Huh-7, high content imaging):IC₅₀ = 1.6 μM,ZIKV-H/PF-2013 (Huh-7, qRT-PCR):IC₅₀ = 1.6 μM." No hemolysis information or data found in the reference(s) presented in this entry "[Ref:3166638]Labyrinthopeptins exhibited low cytotoxicity and had favorable pharmacokinetic properties in mice (half-life [t1/2] = 10.0 h)," No predicted structure available Linear Free Free None L Membrane LabyA1 exert the antiviral function by disrupting viral envelopes (virolysis). 2167.43 C92H131N23O30S4 RDPHILKMYOU CS 4 0 1 -1 12 6 0.38 0.43 1.9hours >20hours >10hours 34 11250 5.19 31666384##23724015 "Journal of virology, 94(2), e01471-19##PloS one, 8(5), e64010." "Prochnow, H., Rox, K., Birudukota, N. V. S., Weichert, L., Hotop, S. K., Klahn, P., Mohr, K., Franz, S., Banda, D. H., Blockus, S., Schreiber, J., Haid, S., Oeyen, M., Martinez, J. P., Süssmuth, R. D., Wink, J., Meyerhans, A., Goffinet, C., Messerle, M., Schulz, T. F., … Brönstrup, M. (2020)##Férir, G., Petrova, M. I., Andrei, G., Huskens, D., Hoorelbeke, B., Snoeck, R., Vanderleyden, J., Balzarini, J., Bartoschek, S., Brönstrup, M., Süssmuth, R. D., & Schols, D. (2013)." Labyrinthopeptins Exert Broad-Spectrum Antiviral Activity through Lipid-Binding-Mediated Virolysis##The lantibiotic peptide labyrinthopeptin A1 demonstrates broad anti-HIV and anti-HSV activity with potential for microbicidal applications 10.1128/JVI.01471-19##10.1371/journal.pone.0064010 "Anti-DENV,Anti-ZIKV,Anti-WNV,Anti-HCV,Anti-CHIKV,Anti-KSHV,Anti-CMV,Anti-HSV,Anti-HIV" DRAVPe02270 XXAGXXXXKVGXX 5 Mirabamide F  sponge Stelletta clavosa No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Neutralization Assays. [Ref: 21280591]62 ± 9 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic "The N-terminal is modified by Htda (3-hydroxy-2,6,8-trimethyldeca-(4Z,6E)-dienoic acid)," The C-terminal is linked to rhamnose via β-OMeTyr "Dhtda replaced with Htda (3-hydroxy-2,6,8-trimethyldeca-(4Z,6E)-dienoic acid).β-OMeTyr-NMeThr-Ala-Gly-3-OMeAla-3-OHLeu-4-ClHPr-3,4-DiMeGln-Dab-Aba-Gly-Htda-Rha.This sequence also has several modifications. X at position 1 is β-O-methyltyrosine (β-OMeTyr), X at position 2 is N-methylthreonine (NMeThr), X at position 5 is 3-O-methylalanine (3-OMeAla), X at position 6 is 3-hydroxyleucine (3-OHLeu), X at position 7 is 4-chlorohydroxyproline (ClHPr), X at position 8 is 3,4-dimethylglutamine (3,4-DiMe" L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 403.44 C72H112ClN13O23 RNDCQEHILMFPSWYVOU G 5.57 0 0 0 1 2 0.9 -1.03 4.4 hours >20 hour >10 hours 78 0 0 21280591 J Nat Prod. 2011 Feb 25;74(2):185-93. "Lu Z, Van Wagoner RM, Harper MK, Baker HL, Hooper JN, Bewley CA, Ireland CM." "Mirabamides E-H, HIV-Inhibitory Depsipeptides from the Sponge Stelletta clavosa" 10.1021/np100613p Anti-HIV DRAVPe02269 XXAGXXXXKVGXX 5 Mirabamide E sponge Stelletta clavosa No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Neutralization Assays. [Ref: 21280591] 121 ± 20 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic "The N-terminal is modified by the Dhtda (2,3-dihydroxy-2,6,8-trimethyldeca-(4Z,6E)-dienoic acid) moiety." "The C-terminal is linked to rhamnose via β-OMeTyr, " "Threonine replaced by Aba (2-amino-2-butenoic acid).OH replaced by H in the polyketide terminal chain.Different rhamnose conformation.Threonine replaced by Aba, Dhtda (2,3-dihydroxy-2,6,8-trimethyldeca-(4Z,6E)-dienoic acid), Rhamnose linked to β-OMeTy.This sequence contains multiple modifications. X at position 1 is β-O-methyltyrosine (β-OMeTyr), X at position 2 is N-methylthreonine (NMeThr), X at position 5 is 3-O-methylalanine (3-OMeAla), X at position 6 is 3-hydroxyleucine (3-OHLeu), X at pos" L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 403.44 C72H112ClN13O24 RNDCQEHILMFPSWYVOU G 5.57 0 0 0 1 2 0.9 -1.03 4.4 hours >20 hour >10 hours 78 0 0  30154377;##21280591 "Mar Drugs. 2018 Aug 28;16(9):306;##Journal of natural products, 74(2), 185–193." "Frau J, Flores-Holguín N, Glossman-Mitnik D;##Lu, Z., Van Wagoner, R. M., Harper, M. K., Baker, H. L., Hooper, J. N., Bewley, C. A., & Ireland, C. M. (2011)." "Chemical Reactivity Properties, pKa Values, AGEs Inhibitor Abilities and Bioactivity Scores of the Mirabamides A–H Peptides of Marine Origin Studied by Means of Conceptual DFT;##Mirabamides E-H, HIV-inhibitory depsipeptides from the sponge Stelletta clavosa" 10.3390/md16090302;##10.1021/np100613p Anti-HIV DRAVPe02268 XXXAGXXXKTGX 5 Mirabamide D marine sponge Siliquariaspongia mirabilis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae disk diffusion assays. "[Ref: 17963357] mirabamides C and D (IC50 values between 140 nM and 1.3 µM for 3 and 190 nM and 3.9 µM for 4), indicating that these peptides can act at the early stages of HIV-1 entry. " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic The N-terminal contains 4-chloro-L-homoproline (ClHPr) in A and L-homoproline (HPr) in B (without chlorine). but differs in specific substitutions elsewhere in the sequence. "The C-terminal is closed via an ester bond to form a macrocyclic structure. This esterification involves a β-hydroxyl group, making the C-terminal non-free for every variant." "Similar to Mirabamide A.This sequence contains several modified residues. X at position 1 is 4-chlorohydroxyproline (ClHPr), X at position 2 is β-O-methyltyrosine (β-OMeTyr), X at position 3 is N-methylthreonine (NMeThr), X at position 6 is 3-O-methylalanine (3-OMeAla), X at position 7 is 3-hydroxyleucine (3-OHLeu), X at position 8 is 3,4-dimethylglutamine (3,4-DiMeGln), X at position 9 is diaminobutyric acid (Dab), and X at position 12 is Dhtda, a lipid-derived tail." L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 432.48 C17H32N6O7 RNDCQEHILMFPSWYVOU G 8.8 1 0 1 1 1 -0.72 0.88 4.4 hours >20 hour >10 hours 20 0 0  30154377;## 17963357 "Mar Drugs. 2018 Aug 28;16(9):305;##Journal of natural products, 70(11), 1753–1760." "Frau J, Flores-Holguín N, Glossman-Mitnik D;##Lu, Z., Van Wagoner, R. M., Harper, M. K., Baker, H. L., Hooper, J. N., Bewley, C. A., & Ireland, C. M. (2011)." "Chemical Reactivity Properties, pKa Values, AGEs Inhibitor Abilities and Bioactivity Scores of the Mirabamides A–H Peptides of Marine Origin Studied by Means of Conceptual DFT;##Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion" 10.3390/md16090302;##10.1021/np070306k Anti-HIV DRAVPe02267 XXXAGXXXKTGX 5 Mirabamide C marine sponge Siliquariaspongia mirabilis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae disk diffusion assays. "[Ref: 17963357] mirabamides C and D (IC50 values between 140 nM and 1.3 µM for 3 and 190 nM and 3.9 µM for 4), indicating that these peptides can act at the early stages of HIV-1 entry. " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic "Similar to Mirabamide A, but the rhamnose moiety is absent." "The C-terminal is closed via an ester bond to form a macrocyclic structure. This esterification involves a β-hydroxyl group, making the C-terminal non-free for every variant." "No Cl at terminal proline. Rhamnose replaced by H.This variant differs at position 1. X is hydroxyproline (HPr), followed by X at position 2 as β-O-methyltyrosine (β-OMeTyr), X at position 3 as N-methylthreonine (NMeThr), X at position 6 as 3-O-methylalanine (3-OMeAla), X at position 7 as 3-hydroxyleucine (3-OHLeu), X at position 8 as 3,4-dimethylglutamine (3,4-DiMeGln), X at position 9 as diaminobutyric acid (Dab), and X at position 12 as Dhtda." L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 432.48 C17H32N6O7 RNDCQEHILMFPSWYVOU G 8.8 1 0 1 1 1 -0.72 0.88 4.4 hours >20 hour >10 hours 20 0 0  30154377;## 17963357 "Mar Drugs. 2018 Aug 28;16(9):304;##Journal of natural products, 70(11), 1753–1760." "Frau J, Flores-Holguín N, Glossman-Mitnik D;##Lu, Z., Van Wagoner, R. M., Harper, M. K., Baker, H. L., Hooper, J. N., Bewley, C. A., & Ireland, C. M. (2011)." "Chemical Reactivity Properties, pKa Values, AGEs Inhibitor Abilities and Bioactivity Scores of the Mirabamides A–H Peptides of Marine Origin Studied by Means of Conceptual DFT;##Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibits HIV-1 fusion" 10.3390/md16090302;##10.1021/np070306k Anti-HIV DRAVPe02266 XXXAGXXXVTGX 5 Mirabamide B marine sponge Siliquariaspongia mirabilis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae disk diffusion assays. [Ref: 17963357] 62nm No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic The N-terminal contains 4-chloro-L-homoproline (ClHPr) in A and L-homoproline (HPr) in B (without chlorine). "The C-terminal is closed via an ester bond to form a macrocyclic structure. This esterification involves a β-hydroxyl group, making the C-terminal non-free for every variant." "Same as Mirabamide A but replaces Dab (2,3-diaminobutanoic acid) with Aba (2-amino-2-butenoic acid).This sequence also features modified residues. X at position 1 is 4-chlorohydroxyproline (ClHPr), X at position 2 is β-O-methyltyrosine (β-OMeTyr), X at position 3 is N-methylthreonine (NMeThr), X at position 6 is 3-O-methylalanine (3-OMeAla), X at position 7 is 3-hydroxyleucine (3-OHLeu), X at position 8 is 3,4-dimethylglutamine (3,4-DiMeGln), X at position 9 is aminobutyric acid (Aba), and X at " L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 403.44 C16H29N5O7 RNDCQEHILMFPSWYVOU G 5.57 0 0 0 1 2 0.9 -1.03 4.4 hours >20 hour >10 hours 78 0 0  30154377;## 17963357 "Mar Drugs. 2018 Aug 28;16(9):303;##Journal of natural products, 70(11), 1753–1760." "Frau J, Flores-Holguín N, Glossman-Mitnik D;##Lu, Z., Van Wagoner, R. M., Harper, M. K., Baker, H. L., Hooper, J. N., Bewley, C. A., & Ireland, C. M. (2011)." "Chemical Reactivity Properties, pKa Values, AGEs Inhibitor Abilities and Bioactivity Scores of the Mirabamides A–H Peptides of Marine Origin Studied by Means of Conceptual DFT;##Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion" 10.3390/md16090302;##10.1021/np070306k Anti-HIV DRAVPe02265 XXXAGXXXKTGX 5 Mirabamide A marine sponge Siliquariaspongia mirabilis No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae disk diffusion assays. [Ref: 17963357] Mirabamide A inhibited HIV-1 in neutralization and fusion assays with IC50 values between 40 and 140 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic The N-terminal contains 4-chloro-L-homoproline (ClHPr) in A and L-homoproline (HPr) in B (without chlorine). "The C-terminal is closed via an ester bond to form a macrocyclic structure. This esterification involves a β-hydroxyl group, making the C-terminal non-free for every variant." "Cl at terminal proline.Contains ?-methoxytyrosine glycosylated with 4′-o-?-l-rhamnopyranoside.This sequence contains several modified residues. X at position 1 is 4-chlorohydroxyproline (ClHPr), X at position 2 is β-O-methyltyrosine (β-OMeTyr), X at position 3 is N-methylthreonine (NMeThr), X at position 6 is 3-O-methylalanine (3-OMeAla), X at position 7 is 3-hydroxyleucine (3-OHLeu), X at position 8 is 3,4-dimethylglutamine (3,4-DiMeGln), X at position 9 is diaminobutyric acid (Dab), and X at p" L Glycoprotein. "The mechanism of action for peptides E through H likely involves their amphipathic and cyclic nature, which enables them to interact with both viral and host cell components to inhibit HIV-1 infection. These peptides may target the HIV-1 envelope glycoproteins, such as gp120 and gp41, which are critical for viral entry into host cells. By binding to gp120, they could block its interaction with the CD4 receptor or CCR5/CXCR4 co-receptors, preventing viral attachment. Additionally, interference with gp41 could disrupt the membrane fusion process required for viral entry. Their structural properties also suggest potential interactions with the host cell membrane, altering its lipid microdomains and impeding the fusion process. Furthermore, these peptides might inhibit the HIV-1 reverse transcriptase enzyme, blocking viral RNA to DNA transcription, or interact with viral assembly proteins to disrupt the formation of infectious virions. The exact mechanism for each peptide requires further investigation, including binding studies and structural analyses, to elucidate their precise targets and pathways of action." 432.48 C17H32N6O7 RNDCQEHILMFPSWYVOU G 8.8 1 0 1 1 1 -0.72 0.88 4.4 hours >20 hour >10 hours 20 0 0  30154377;## 17963357 "Mar Drugs. 2018 Aug 28;16(9):302;##Journal of natural products, 70(11), 1753–1760." "Frau J, Flores-Holguín N, Glossman-Mitnik D:##Plaza, A., Gustchina, E., Baker, H. L., Kelly, M., & Bewley, C. A. (2007)." "Chemical Reactivity Properties, pKa Values, AGEs Inhibitor Abilities and Bioactivity Scores of the Mirabamides A–H Peptides of Marine Origin Studied by Means of Conceptual DFT;##Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion" 10.3390/md16090302;##10.1021/np070306k Anti-HIV DRAVPe02263 DVREEEQLGERATGLNLNI 19 B-HR2-scrambled Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 2156.34 C89H150N28O34 CHMFPSWOU E 4.25 2 5 -3 4 6 -0.874 3.14 1.1 hours 3 min >10 hours 102.63 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02264 ALHALGYQLAFVLDSPSAY 19 H-HR1-SC Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 2036.31 C96H142N22O27 RNCEHIFWOU AL 5.08 0 1 -1 5 10 0.684 -0.46 4.4 hours >20 hour >10 hours 118.42 2980 1.463 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HIV DRAVPe02262 GENNELRLTRDAI 13 B-HR2-S Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. "[Ref:16603508]:HSV:IC50=Show no inhibitory effects at 500 µM, implying that these peptides are ineffective at the tested concentrations" No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 1500.63 C61H105N21O23 CQHKMFPSWYVOU RNL 4.68 2 3 -1 3 4 -1.054 3.88 30 hours >20 hour >10 hours 97.69 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02260 TAAGDARANAVAKAGLHDLNIETDTERNH 29 B-HR1-scrambled Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 3032.24 C124H203N43O46 CQMFPSWYOU A 5.33 3 5 -2 6 11 -0.734 2.71 7.2 hours >20 hours >10 hours 74.48 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02261 VEGQLGENNELRLTRDAIE 19 B-HR2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. "[Ref:16603508]:HSV:IC50=Show no inhibitory effects at 500 µM, implying that these peptides are ineffective at the tested concentrations" No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 2156.34 C89H150N28O34 CHKMFPSWYOU E 4.25 2 5 -3 3 4 -0.874 3.88 100 hours >20 hours >10 hours 102.63 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02259 AGHATLREHLRDIKAENTDAN 21 B-HR1-S Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 2332.52 C96H158N34O34 CEGIMPYOU A 6.02 3 4 -1 4 7 -1.086 3.39 4.4 hours >20 hours >10 hours 74.76 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02258 HATCSLAFALATSVALATRNDLLLRWAAARDAQTILSKRDR 41 H-HR2-scrambled Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 4469.15 C194H324N62O57S1 CEGIMPYOU A 10.64 6 3 3 9 22 0.132 1.84 3.5 hours 10 min >10 hours 107.56 5500 1.231 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02257 TSDVAAATNADLRTALARADHQKTLFWL 28 H-HR2-S Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=No significant inhibition No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 3057.42 C134H214N40O42 CEGIMPYOU A 6.42 3 3 0 7 14 -0.118 1.79 7.2 hours >20 hours >10 hours 91.07 5500 1.799 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02256 RARRSLLIASALCTSDVAAATNADLRTALARADHQKTLFWL 41 H-HR2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=40% at 500 µM. No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery "H-HR2 and B-HR1 also inhibit this step, but their effects are less pronounced compared to H-HR1." 4469.15 C194H324N62O57S1 EGMYOU A 10.64 6 3 3 9 22 0.132 1.84 1 hour 3 min 2 min 107.56 5500 1.231 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02255 YQFHLVLHEALRAQALSRQLILGRELAQELVAELAT 36 H-HR1-scrambled Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=25–30 % No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxic effect observed for any peptide at the tested concentrations. Cell viability remained similar to untreated cells. No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 4101.76 C185H303N53O52 NDCGKMFPSTWYOU L 6.04 3 4 -1 6 19 0.267 1.04 2.8 hours 10 min 2 min 141.11 1490 0.363 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02253 TARLQLEARLQHLVAEILEREQSLALHALGYQLAFV 36 H-HR1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. [Ref:16603508]:HSV:IC50=65% inhibition at 500 µM No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxicity No predicted structure available Linear Free Free None L Fusion machinery "H-HR1 likely disrupts the formation of the fusion complex, as it specifically inhibits HSV-1 entry during the virus attachment-entry phase." 4101.76 C185H303N53O52 NDCKMPWOU L 5.98 3 4 -1 6 19 0.267 1.04 7.2 hours >20 hour >10 hours 141.11 1490 0.363 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02254 LQLEARLQHLVAEILER 17 H-HR1-SN Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. Not Available No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxicity No predicted structure available Linear Free Free None L Fusion machinery The peptides derived from the heptad repeat (HR) regions of HSV-1 glycoproteins (gH and gB) inhibit the virus entry process by interfering with membrane fusion. 2031.39 C90H155N27O26 NDCGKMFPSTWYOU L 5.5 2 3 -1 2 9 0.094 1.69 5.5 hours 3 min 2 min 166.47 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02252 AGDNATVAAGHATLREHLRDIKAENTDAN 29 B-HR1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV-1 Herpesviridae Virus entry assays. "[Ref:16603508]:HSV:IC50=Shows minor inhibitory effects at 500 µM, indicating significantly lower activity. Its IC₅₀ is likely much higher than 500 µM, if effective at all." No hemolysis information or data found in the reference(s) presented in this entry [Ref:16603508]No cytotoxicity No predicted structure available Linear Free Free None L Fusion machinery "H-HR2 and B-HR1 also inhibit this step, but their effects are less pronounced compared to H-HR1." 3032 C124H203N43O46 CQMFPSWYOU A 5.53 3 5 -2 6 11 -0.734 2.71 4.4 hours >20 hour >10 hours 74.48 0 0 16603508 "The Journal of general virology, 87(Pt 5), 1085–1097." "Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Browne, H., & Galdiero, M. (2006)." Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. 10.1099/vir.0.81794-0 Anti-HSV DRAVPe02251 CLGVGSCNDFAGCGYAVVCFW 21 Siamycin I (Bacteriocin) Streptomyces strain AA6532 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae CPEb (XTT) "[Ref:8557614]HSV:ID50=48µg/ml,HIV-1:ID50=7µg/ml" No hemolysis information or data found in the reference(s) presented in this entry [Ref:8557614]TD50=>100µg/ml No predicted structure available Linear Free Amidation "Two disulfide bonds linking Cys-1 with Cys-13and Cys-7 with Cys-19, as well as an amide bond joining the side chain of Asp-9 to the N-terminus Cys-1. Amino acid anal- ysis revealed that both compounds contained the same residues with the exception that one of two valines in saimycin I is replaced by isoleucine in siamycin II." L Not Found Not Available 2171.51 C96H135N23O27S4 EHIKMPQRT CG 3.8 0 1 -1 11 9 1.143 1.893 1.2 hour >20 hour >10 hours 69.52 7240 362 8557614## 7797448 "J Antibiot (Tokyo). 1995 Dec;48(12):1515-7;##The Journal of antibiotics, 48(5), 433–434." "Detlefsen DJ, Hill SE, Volk KJ, Klohr SE, Tsunakawa M, Furumai T, Lin PF, Nishio M, Kawano K, Oki T, et al;##Tsunakawa, M., Hu, S. L., Hoshino, Y., Detlefson, D. J., Hill, S. E., Furumai, T., White, R. J., Nishio, M., Kawano, K., & Yamamoto, S. (1995). " "Siamycins I and II, new anti-HIV-1 peptides: II. Sequence analysis and structure determination of siamycin I;##Siamycins I and II, new anti-HIV peptides: I. Fermentation, isolation, biological activity and initial characterization" 10.7164/antibiotics.48.1515;##10.7164/antibiotics.48.433 Anti-HIV DRAVPe02250 CLGIGSCNDFAGCGYAIVCFW 21 Siamycin II Streptomyces strains AA3891 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae CPEb (XTT) [Ref:7787424]HIV-1:ED50=0.08μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:7787424]TC50=150 No predicted structure available Linear Free Amidation "It differs from Siamycin I only by one amino acid. Siamycin I has a valine residue at position 4. In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus (XXJ). The original has been replaced since antimicrobial assays revealed no activity." L as an inhibitor of fusion of gp160- and CD4-expressing cell Siamycin I inhibits fusion between C8166 cells and CEM-SS cells chronically infected with HIV (50% effective dose of 0.08 microM) but has no effect on Sendai virus-induced fusion or murine myoblast fusion. 2199.56 C98H139N23O27S4 EHKMPQRT CG 3.8 0 1 -1 11 9 1.171 2.069 1.2 hour >20 hour >10 hours 79.05 7240 362 7787424## 7797448 "Journal of biomolecular NMR, 5(3), 271–286;##The Journal of antibiotics, 48(5), 433–434." "Constantine, K. L., Friedrichs, M. S., Detlefsen, D., Nishio, M., Tsunakawa, M., Furumai, T., Ohkuma, H., Oki, T., Hill, S., & Bruccoleri, R. E. (1995);##Tsunakawa, M., Hu, S. L., Hoshino, Y., Detlefson, D. J., Hill, S. E., Furumai, T., White, R. J., Nishio, M., Kawano, K., & Yamamoto, S. (1995). " "High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion;##Siamycins I and II, new anti-HIV peptides: I. Fermentation, isolation, biological activity and initial characterization" 10.1007/BF00211754;##10.7164/antibiotics.48.433 Anti-HIV DRAVPe02248 DYNPYLLFLK 10 PB1-11 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 Orthomyxoviridae AlphaScreen [Ref:33166574]IAV:IC50=13 ± 1μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet Not included yet L PB1 (Basic polymerase 1 ) " The PB1-0 peptide has given excellent results in blocking the PA-PB1 interaction, in particular in the C-terminal domain of the PR8 (H1N1). The same results were confirmed by surface plasmon resonance (SPR) experiments. PB1-10 was obtained with the elimination of some amino acids from the N-terminus and C-terminus. With the addition of two substituents, the authors reached PB1-11, which proved to be the most active of all" 1285.51 C64H92N12O16 ARCQEGHIMSTWVOU L 5.83 1 1 0 3 4 -0.09 0.34 1.1hour 3 mins >10 hours 117 2980 2.318 33166574 "Antiviral research, 185, 104971." "Hejdánek, J., Radilová, K., Pachl, P., Hodek, J., Machara, A., Weber, J., Řezáčová, P., Konvalinka, J., & Kožíšek, M. (2021)." structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor 10.1016/j.antiviral.2020.104971 Anti-IAV DRAVPe02249 SRARIDARI 9 FluAPep 1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 orthomyxoviridae Docking studies [Ref:30597438]IAV:binding affinity (score = −246.155) No hemolysis information or data found in the reference(s) presented in this entry [Ref:30597438]ToxinPred analysis confirmed that designed peptides were non-toxic. No predicted structure available Linear Free Free None L PB1 (Basic polymerase 1 ) Not Available 1057.22 C43H80N18O13 NCQEGHLKMFPTWYVOU R 11.7 3 1 -2 1 4 -0.578 4.82 1.9 hours >20 hours >10 hours 108.89 0 0 30597438 "Computational biology and chemistry, 78, 273–281." "Arivajiagane, A., Ravi Varadharajulu, N., Seerangan, K., & Rattinam, R. (2019)." In silico structure-based design of enhanced peptide inhibitors targeting RNA polymerase PAN-PB1Cinteraction  10.1016/j.compbiolchem.2018.12.009 Anti-IAV DRAVPe02247 LSTAADMQGVVTDGMASGLDKDYLKPDD 28 p28 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 Orthomyxoviridae Docking studies [Ref:33575983]IAV=22 bonds No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet Not included yet L PB1 (Basic polymerase 1 ) Docking studies showed that the p28 region forms strong and stable interactions with the C-terminus of PB1 (C-PB1) and other proteins of H1N1 IAV  2914.21 C122H197N31O47S2 RNCEHIFWOU D 3.85 2 6 -4 6 10 -0.371 1.61 5.5 hours 3 min 2 min 73.21 1490 0.511 33575983 "Molecular diversity, 25(3), 1929–1943." "Sasidharan, S., Gosu, V., Shin, D., Nath, S., Tripathi, T., & Saudagar, P. (2021)." Therapeutic p28 peptide targets essential H1N1 influenza virus proteins: insights from docking and molecular dynamics simulations 10.1007/s11030-021-10193-8 Anti-IAV DRAVPe02246 LVRPLAL 7 7-1 peptide Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Influenza A H3N2, A/Aichi/2/68 (H3N2)" Orthomyxoviridae Plaque reduction [Ref:26833245]IAV:IC50=6.4μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:26833245]Negligible cytotoxicity No predicted structure available Linear Not included yet Not included yet None L Head of HA " A random phage display library of 7-mer peptides was screened by affinity selection, obtaining the peptide LVRPLAL that showed the highest affinity toward H1 and H3 HAs. The avidin–biotin-peroxidase complex (ABC) system was exploited to evaluate the binding of this peptide to HA. It showed a Kd of 92 and 194 µM for H1 HA from A/New Caledonia/20/99 (H1N1) and H3 from A/Wyoming/3/2003 (H3N2), respectively. The C18-conjugated form of this peptide was tested in plaque reduction assay, showing a good activity toward A/Aichi/2/68 (H3N2) virus (6.4 µM) and a lower potency against A/Puerto Rico/8/34 (H1N1) virus (101 µM). The Ala scan indicated the importance of Arg3 and Pro4 for the HA binding, which was also assessed by docking calculations" 781.01 C37H68N10O8 NDCQEGHIKMFSTWYOU L 9.79 1 0 -1 0 5 1.614 -0.81 5.5 hours 3 min 2 min 222.86 0 0 26833245 "Bioorganic & medicinal chemistry, 24(5), 1106–1114." "Matsubara, T., Onishi, A., Yamaguchi, D., & Sato, T. (2016). " Heptapeptide ligands against receptor-binding sites of influenza hemagglutinin toward anti-influenza therapy 10.1016/j.bmc.2016.01.039 Anti-IAV DRAVPe02245 ARDFYDYDVFYYAMD 15 PeB Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H3N2/A/Aichi/2/68 X31 (H3N2) Orthomyxoviridae Infection inhibition [Ref:27415624]IAV:IC50=32 ± 5μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:27415624]Neglible cytotoxicity No predicted structure available Linear Not included yet Not included yet None L Head of HA Not included yet 1954.1 C92H116N18O28S1 NCQEGHILKPSTWVOU D 3.77 1 4 -3 4 6 -0.506 2.29 4.4 hours >20 hours >10 hours 32.67 5960 3.05 27415624 "PloS one, 11(7), e0159074." "Memczak, H., Lauster, D., Kar, P., Di Lella, S., Volkmer, R., Knecht, V., Herrmann, A., Ehrentreich-Förster, E., Bier, F. F., & Stöcklein, W. F. (2016)." Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding  10.1371/journal.pone.0159074 Anti-IAV DRAVPe02243 ARDFYGYDVFFYAMD 15 C18-PeBGFa Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "Influenza A H3N2/A/Aichi/2/68 X31 (H3N2), Rostock H7N1 " Orthomyxoviridae Infection inhibition "[Ref:26124860]IAV:IC50=1.2 µM and 2.8 µM," No hemolysis information or data found in the reference(s) presented in this entry [Ref:26124860]Negligible cytotoxicity No predicted structure available Linear Not included yet Not included yet C17H35CO- L Head of HA "The acylated peptide was able to block hemagglutination produced by the Aichi H3N2 and Rostock H7N1 viruses at 1.2 µM and 2.8 µM," 1880.06 C90H114N18O25S1 NQEHILKMPSTWOU DFY 3.93 1 3 -2 3 7 -0.08 1.44 4.4 hours >20 hours >10 hours 32.67 4470 2.378 26124860 " Beilstein journal of organic chemistry, 11, 589–595." "Lauster, D., Pawolski, D., Storm, J., Ludwig, K., Volkmer, R., Memczak, H., Herrmann, A., & Bhatia, S. (2015)" Potential of acylated peptides to target the influenza A virus 10.3762/bjoc.11.65 Anti-IAV DRAVPe02244 ARDFYGYDVFFYAMD 15 PeBGF Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H3N2/A/Aichi/2/68 X31 (H3N2) Orthomyxoviridae Infection inhibition [Ref:27415624]IAV:IC50=25 ± 6μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:27415624]Negligible cytotoxicity No predicted structure available Linear Not included yet Not included yet None L Head of HA "The most interesting peptide was the PeBGF, which showed a micromolar activity in SPR, HI, neutralization, and infection inhibition assays toward both Aichi H3N2 and Rostock H7N1 viral strains" 1880.06 C90H114N18O25S1 NQEHILKMPSTWOU DFY 3.93 1 3 -2 3 7 -0.08 1.44 4.4 hours >20 hours >10 hours 32.67 4470 2.378 27415624 "PloS one, 11(7), e0159074." "Memczak, H., Lauster, D., Kar, P., Di Lella, S., Volkmer, R., Knecht, V., Herrmann, A., Ehrentreich-Förster, E., Bier, F. F., & Stöcklein, W. F. (2016)." Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding  10.1371/journal.pone.0159074 Anti-IAV DRAVPe02242 LSRMPK 6 P1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/chicken/Tunisia/12/2010 (H9N2) Orthomyxoviridae In ovo antiviral activity [Ref:35306102]IAV:IC50=870μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:35306102]two peptides did not show toxicity on eggs and chicken lungs. No predicted structure available Linear Not included yet Not included yet None L Head of HA "Molecular docking calculations, carried out to depict the interaction between active peptides and hemagglutinin, indicated that P1 and P2 peptides bind different regions of the HA globular head: P1 occupies the RBS, while P2 occupies a site close to the RBS and interacts with the 220-loop " 730.92 C31H58N10O8S1 ANDQEHIFTWYVOU RLKMPS 11 2 0 2 0 2 -0.85 2.76 5.5 hours 3 mins 2 min 65 0 0 35306102 "Virus research, 313, 198745." "Arbi, M., Larbi, I., Nsiri, J., Behi, I. E., Rejeb, A., Miled, K., Ghram, A., & Houimel, M. (2022). " Inhibition of avian influenza virus H9N2 infection by antiviral hexapeptides that target viral attachment to epithelial cells 10.1016/j.virusres.2022.198745 Anti-IAV DRAVPe02241 FAPRWR 6 P2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H9N1/A/chicken/Tunisia/12/2010 (H9N2) Orthomyxoviridae In ovo antiviral activity [Ref:35306102]IAV:IC50=620μM No hemolysis information or data found in the reference(s) presented in this entry [Ref:35306102]two peptides did not show toxicity on eggs and chicken lungs. No predicted structure available Linear Not included yet Not included yet None L Head of HA "Molecular docking calculations, carried out to depict the interaction between active peptides and hemagglutinin, indicated that P1 and P2 peptides bind different regions of the HA globular head: P1 occupies the RBS, while P2 occupies a site close to the RBS and interacts with the 220-loop " 831.98 C40H57N13O7 NDCEGIFSYOU R 12 2 0 2 0 3 -1.15 3.78 1.1hour 3 min 2 min 16.67 5500 6.611 35306102 "Virus research, 313, 198745." "Arbi, M., Larbi, I., Nsiri, J., Behi, I. E., Rejeb, A., Miled, K., Ghram, A., & Houimel, M. (2022). " Inhibition of avian influenza virus H9N2 infection by antiviral hexapeptides that target viral attachment to epithelial cells 10.1016/j.virusres.2022.198745 Anti-IAV DRAVPe02240 WTGDFFSSHYTVPRC 15 iHA-100 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/H5-HA Orthomyxoviridae Surface Plasmon Resonance [Ref:33976181]IAV:IC50=0.0015μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Head of HA "Escape mutant isolation demonstrated its binding at the stalk region of HA, confirmed by the stabilization effect its binding produces on HA trypsin degradation, but interaction on the globular head was not excluded. The macrocycle peptide was tested in vivo on mice infected with lethal H5N1 IAV. iHA-100 rescued 40% of mice and showed better efficacy when administered in the early or late phases of infection. " 1802.98 C83H111N21O23S1 ANQEILKMOU FST 6.73 1 1 0 5 5 -0.407 1.72 2.8 hours 3 mins 2 mins 19.33 6990 3.877 33976181 "Nature communications, 12(1), 2654." "Saito, M., Itoh, Y., Yasui, F., Munakata, T., Yamane, D., Ozawa, M., Ito, R., Katoh, T., Ishigaki, H., Nakayama, M., Shichinohe, S., Yamaji, K., Yamamoto, N., Ikejiri, A., Honda, T., Sanada, T., Sakoda, Y., Kida, H., Le, T. Q. M., Kawaoka, Y., … Kohara, M. (2021). " Macrocyclic peptides exhibit antiviral effects against influenza virus HA and prevent pneumonia in animal models  10.1038/s41467-021-22964-w Anti-IAV DRAVPe02238 ARLPR 5 C18-s2(1–5) Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/Puerto Rico/8 (H1N1) Orthomyxoviridae Plaque reduction [Ref:20476787]IAV:IC50=1.9μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Amidation C17H35CO L Binding the head of HA (protein present at the out membrane of the virus) Not included yet 611.75 C26H49N11O6 NDCQEGHIKMFSTWYVOU R 12 2 0 2 0 2 -1 4.62 4.4 hours >20 hours >10 hours 98 0 0 20476787 "Journal of medicinal chemistry, 53(11), 4441–4449." "Matsubara, T., Onishi, A., Saito, T., Shimada, A., Inoue, H., Taki, T., Nagata, K., Okahata, Y., & Sato, T. (2010)." Sialic acid-mimic peptides as hemagglutinin inhibitors for anti-influenza therapy 10.1021/jm1002183 Anti-IAV DRAVPe02239 MARRPVNHAUMARRPVNHAUMARRPVNHAUMARRPVNHAU 40 PVF-tet Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/Puerto Rico/8 (H1N1) Orthomyxoviridae Infection inhibition [Ref:31919357]IAV:IC50=1.4μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet 4-3Lys L Head of HA "This compound did not block viral entry into the cell as expected because of its binding to HA and did not act on the fusion process or in the HI assay. In fact, PVF-tet does not interact with H1 and H2, but likely does with the H0 of newly synthesized viral particles. PVF-tet is a cell-penetrating peptide, and its addition to the infected cell causes the amassment of HA in a vacuole-like structures named amphisomes" 1348.45 C55H88N20O13S1Se1 DCQEGILKSTWYO AR 12 2 0 2 1 2 -0.436 4.87 30 hours >20 hours >10 hours 44.5 0 0 31919357 "Nature communications, 11(1), 162." "Omi, J., Watanabe-Takahashi, M., Igai, K., Shimizu, E., Tseng, C. Y., Miyasaka, T., Waku, T., Hama, S., Nakanishi, R., Goto, Y., Nishino, Y., Miyazawa, A., Natori, Y., Yamashita, M., & Nishikawa, K. (2020)" The inducible amphisome isolates viral hemagglutinin and defends against influenza A virus infection 10.1038/s41467-019-13974-w Anti-IAV DRAVPe02237 ARLPRTMVHPKPAQP 15 C18-s2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/Puerto Rico/8 (H1N1) Orthomyxoviridae Plaque reduction [Ref:20476787]IAV:IC50=11μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Amidation C17H35CO L Binding the head of HA (protein present at the out membrane of the virus)  Interfering with the fusogenic activity of HA. 1699.05 C75H127N25O18S1 NDCEGIFSYOU P 12.01 3 0 3 2 5 -0.88 2.21 4.4 hours >20 hours >10 hours 58.67 0 0 20476787 "Journal of medicinal chemistry, 53(11), 4441–4449." "Matsubara, T., Onishi, A., Saito, T., Shimada, A., Inoue, H., Taki, T., Nagata, K., Okahata, Y., & Sato, T. (2010)." Sialic acid-mimic peptides as hemagglutinin inhibitors for anti-influenza therapy 10.1021/jm1002183 Anti-IAV DRAVPe02236 IHAEIKNSLKIDNLDVNRCIEAL 23 LEDGF/p75 (355-377) Synthetic construct O75475 Experimentally Validated 9606 PSIP1 Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 Retroviridae Not Available [Ref.18331842]Human immunodeficiency virus (HIV): Inhibition of integrase activity (3' end processing)(IC50=165±28 µM); inhibition of integrase activity(strand transfer)(IC50=153±28 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Integrase The LEDGF/p75 peptide modestly inhibited IN catalysis and was dependent on IN–DNA assembly. The peptide was also effective at disrupting LEDGF/p75–IN complex formation. 2622.03 C113H193N33O36S FGMPQTWY I 5.48 4 4 0 5 10 -0.048 -41.68 20 hour 30 min >10 hours 140 0 0 18331842 FEBS Lett. 2008 Apr 30;582(10):1425-30. "Al-Mawsawi LQ, Christ F, Dayam R, Debyser Z, Neamati N." Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis 10.1016/j.febslet.2008.02.076 Anti-IAV DRAVPe02235 RRKKWLVFFVIFYFFR 16 FP4 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 Orthomyxoviridae Plaque reduction [Ref:22258859]IAV:IC50=0.00004μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet Not included yet L Hemagglutinin protein "The mechanism of action was demonstrated to be the interference with the viral attachment via contact with HA, as demonstrated by ELISA assay, but they do not block hemagglutination produced by the virus, so they do not interact on the receptor binding site. Moreover, the compounds were tested on Balb/c mice infected with a lethal dose of A/WSN/33 virus, showing an ability to reduce the viral titer by 2–4 log units" 2252.78 C117H166N28O18 ANDCEQGHMPSTOU F 11.73 5 0 5 1 10 0.45 1.3 1 hours 2 min 2 mins 85 6990 3.103 22258859 "The Journal of general virology, 93(Pt 5), 980–986." "Nicol, M. Q., Ligertwood, Y., Bacon, M. N., Dutia, B. M., & Nash, A. A. (2012)." A novel family of peptides with potent activity against influenza A viruses 10.1099/vir.0.038679-0 Anti-IAV DRAVPe02234 GLFGAIAGFIKNGWKGMIKG 20 HA-FP-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H3N2 Orthomyxoviridae Cytopathic Effect Reduction [Ref:33392200]IAV:IC50=1.73μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet Not included yet L Hemagglutinin protein "these peptides specifically blocked the entry of IAV into host cells via the interaction of the pFPs and the HA2 subunit, most likely due to interactions between the N-terminal portion of HA2. The positively charged lysine residues of pFPs strongly interact with glutamic acid or aspartic acid, negatively charged, of the HA2 subunit via ionic contacts and hydrogen bonds" 2065.51 C98H153N25O22S1 RDCQEHPSTYVOU G 10.3 3 0 3 1 10 0.495 -0.81 30 hours >20 hours >10 hours 88 5500 2.663 33392200 "Frontiers in cell and developmental biology, 8, 611121." "Wu, W., Lin, D., Shen, X., Li, F., Fang, Y., Li, K., Xun, T., Yang, G., Yang, J., Liu, S., & He, J. (2015). " New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides 10.3389/fcell.2020.611121 Anti-IAV DRAVPe02233 GTYDHDVYRDEALNNRFQIKGVELKSGYKDWGSGSGC 37 P155–185-Chol Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H3N2 Orthomyxoviridae Plaque reduction [Ref:21994935]IAV:IC50=27.21µg/mL No hemolysis information or data found in the reference(s) presented in this entry [Ref:21994935]The peptides were non-cytotoxic in an ex vivo model and may be safe for in vivo use. No predicted structure available Linear Not included yet Not included yet "(PEG4-Chol)NH2, (155–185-Chol and 155–181-Chol)" L Hemagglutinin protein " The complete sequence (155–185) corresponds to the HA2 portion that bundles to the inner coiled-coil that is crucial for the fusion process; compound P155–181 lacks the four final residues between the N-capped coiled-coil and the transmembrane domain, while compound P155–175 corresponds to the most truncated sequence deficient the N-cap motif. Only cholesterol-tagged compounds containing the N-cap motif (155–185-Chol and 155–181-Chol) demonstrated antiviral activity against IAV/H3N2 in cell culture, most likely due to the ability of the cholesterol to fasten the peptide to the membrane and to form nanoparticles" 4166.51 C181H270N52O60S1 MPOU G 5.55 5 6 -1 10 9 -1.03 2.56 30 hours >20 hours >10 hours 50 9970 2.393 21994935 "The Journal of biological chemistry, 286(49), 42141–42149." "Lee, K. K., Pessi, A., Gui, L., Santoprete, A., Talekar, A., Moscona, A., & Porotto, M. (2011). " "Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus" 10.1074/jbc.M111.254243 Anti-IAV DRAVPe02232 GYHHQNEQGSGYAADLK 17 C3LB-HA Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/Puerto Rico/916/34 (H1N1) Orthomyxoviridae Cytopathic Effect inhibition [Ref:24146939]IAV:IC50=5.90 (µg/mL) No hemolysis information or data found in the reference(s) presented in this entry [Ref:24146939]inhibit IAV without cytotoxicity. No predicted structure available Linear Not included yet Not included yet None L Hemagglutinin protein "The binding to the HA, which prevents the conformational rearrangements inside the endosome, is the most likely mechanism of action.By in silico analysis of different HA1 and HA2, they discovered conserved regions (40–50 amino acids at the N- and C-terminal of HA1, and 80 amino acids at the N-terminal of HA2) that revealed short regions of HA1 N- and C-terminal ends characterized by hydrophilic, flexible, charged, and exposed (antigenic) sequences. Inhibitory activity of those peptides against IAV of various origins (human, swine, and avian) demonstrates the ability to inhibit IAV without cytotoxicity. The binding to the HA, which prevents the conformational rearrangements inside the endosome, is the most likely mechanism of action. Docking studies revealed that AVPs form several hydrogen bonds and electrostatic contacts in the HA stalk region with the fusion peptide, helix A, helix B, and loop B that could be responsible for the inhibition of HA conformational changes. Nevertheless, they did not show the stability at endosomal pH " 1874.94 C80H115N25O28 RCIMFPTWVOU G 5.99 1 2 -1 5 3 -1.471 2.37 30 hours >20 hours >10 hours 34.71 5500 1.589 24146939 "PloS one, 8(10), e76876." "López-Martínez, R., Ramírez-Salinas, G. L., Correa-Basurto, J., & Barrón, B. L. (2013). " Inhibition of influenza A virus infection in vitro by peptides designed in silico 10.1371/journal.pone.0076876 Anti-IAV DRAVPe02230 FHRKKGRGKHK 11 None Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 Orthomyxoviridae Neutralization [Ref:15729820]IAV:1 log unit inhibitory activity No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Hemagglutinin protein  interfering with the fusogenic activity of HA. 1378.65 C61H103N25O12 ANDCQEILMPSTWYVOU K 12.03 6 0 6 0 1 -2.636 5.13 1.1 hours 3 min 2 mins 0 0 0 15729820 "Journal of chromatography. A, 1064(1), 59–66." "Zhao, R., Fanga, C., Yu, X., Liu, Y., Luo, J., Shangguan, D., Xiong, S., Su, T., & Liu, G. (2005)." Screening of inhibitors for influenza A virus using high-performance affinity chromatography and combinatorial peptide libraries 10.1016/j.chroma.2004.12.023 Anti-IAV DRAVPe02231 GLFGAIAGFIKNGWKGMIKG 20 HA-FP-1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1/A/Puerto Rico/8/34 (H1N1) Orthomyxoviridae Cytopathic Effect inhibition [Ref:26382764]IAV:IC50=9.61 (µg/mL) No hemolysis information or data found in the reference(s) presented in this entry [Ref:26382764]Neglible cytotoxicity No predicted structure available Linear Not included yet Not included yet None L Hemagglutinin protein " interfering with the fusogenic activity of HA. As revealed by fusion and hemolysis inhibition assays, these peptides specifically blocked the entry of IAV into host cells via the interaction of the pFPs and the HA2 subunit,most likely due to interactions between the N-terminal portion of HA2. The positively charged lysine residues of pFPs strongly interact with glutamic acid or aspartic acid, negatively charged, of the HA2 subunit via ionic contacts and hydrogen bonds" 2065.51 C98H153N25O22S1 RDCQEHPSTYVOU G 10.03 3 0 3 1 10 0.495 -0.81 30 hours >20 hours >10 hours 88 5500 2.663  26382764 "PloS one, 10(9), e0138426." "Wu, W., Lin, D., Shen, X., Li, F., Fang, Y., Li, K., Xun, T., Yang, G., Yang, J., Liu, S., & He, J. (2015). " New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides  10.1371/journal.pone.0138426 Anti-IAV DRAVPe02229 ELVDPVVAAGAVVTSSGIVFFS 22 IntPep Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None Influenza A H1N1 Orthomyxoviridae Structural studies [Ref:33392200]IAV:IC50=47 ± 12% and 41 ± 8%μM [Ref:33392200]Low hemolytic activity [Ref:33392200]Low cytotoxicity No predicted structure available Linear Not included yet Not included yet None L Neuraminidase protein " IntPep peptides were able to interact with the TM2 domain (region 316–333) of human NEU1 and disrupt its dimerization with consequent losses in sialidase activity. Furthermore, these IntPeps inhibit membrane sialidase activity triggered by elastin-derived peptides in macrophages, which are highly dependent on NEU1 ." 2164.48 C100H158N22O31 RNCQHKMWYOU V 3.67 0 2 -2 4 13 1.455 -0.86 1 hour 30 min >10 hour 128.18 0 0 33392200 "Frontiers in cell and developmental biology, 8, 611121." "Albrecht, C., Kuznetsov, A. S., Appert-Collin, A., Dhaideh, Z., Callewaert, M., Bershatsky, Y. V., Urban, A. S., Bocharov, E. V., Bagnard, D., Baud, S., Blaise, S., Romier-Crouzet, B., Efremov, R. G., Dauchez, M., Duca, L., Gueroult, M., Maurice, P., & Bennasroune, A. (2020). " Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation 10.3389/fcell.2020.611121 Anti-IAV DRAVPe02228 PGEKGPSGEAGTAGPPGTPGPQGL 38 Peptide P cod skin hydrolysates No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available Not Available H1N1 Orthomyxoviridae Cytopathic Effect Reduction [Ref:30308963]IAV:IC50=471 ± 12 g/mL. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Not included yet Not included yet None L Neuraminidase protein "This compound showed a NA inhibitory activity with Ki of 0.29 mM, and it was demonstrated to directly bind to free enzymes. The cytopathic effect reduction assay showed that the peptide P protected MDCK cells from viral infection and reduced viral production in a dose-dependent manner with an EC50 value of 471 ± 12 μg/mL against PR8 (H1N1)" 2116.27 C90H142N26O33 RNDCHIMFWYVOU G 4.53 1 2 -1 14 3 -0.917 0.71 >20 hours >20 hours Unknown 24.58 0 0 30308963 Drugs. 2018;16:377. doi: 10.3390/md16100377.  "Li J., Chen Y., Yuan N., Zeng M., Zhao Y., Yu R., Liu Z., Wu H., Dong S." A Novel Natural Influenza A H1N1 Virus Neuraminidase Inhibitory Peptide Derived from Cod Skin Hydrolysates and Its Antiviral Mechanism. Mar.  10.3390/md16100377 Anti-IAV DRAVPe02227 RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC 31 GNCP-2 Cavia porcellus "P49112,Q9R0Z5" Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 N/A Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Not included Free Free Three Disulfide bridges. Seq differs from GNCP-1 only at position 21 (L here and I for GNCP-1). L Not found Not Available 3838.58 C164H262N54O41S6 ADEHKMSW R 9.8 7 0 7 15 7 -0.223 -93.39 1 hour 2 min 2 min 47.1 3355 111.83 8173076 DNA Seq. 1993;4(2):123-128 "Nagaoka I, Nonoguchi A, Yamashita T." Cloning and characterization of the guinea pig neutrophil cationic peptide-1 and -2 genes. Anti-HIV DRAVPe02225 FLPVLAGIAAKVVPALFCKITKKC 24 Brevinin-1 "frog, Rana brevipoda porsa, Japan, Asia" P32423 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV Herpesviridae Virus inhibition assays "[Ref:10795591]HSV-1:IC50=10 ug/ml ,HSV-2:IC50=100 ug/ml" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L Not found Not Available 2531.24 C121H204N28O26S2 DEHMNQRSWY AK 9.7 4 0 4 4 14 1.288 28.65 1.2 hour >20 hour >10 hour 134.17 125 5.43 10795591 "official publication of the European Society of Clinical Microbiology, 19(3), 187–194." "Yasin, B., Pang, M., Turner, J. S., Cho, Y., Dinh, N. N., Waring, A. J., Lehrer, R. I., & Wagar, E. A. (2000)." Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides 10.1007/s100960050457 Anti-HSV DRAVPe02226 ALWKNMLKGIGKLAGKAALGAVKKLVGAES 30 Dermaseptin-3 Phyllomedusa sauvagei (Sauvage's leaf frog) P80279 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HIV-1 N/A Not Available Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L Not found Not Available 3148.75 C133H215N37O39S6 DFHLMQT C 8.33 3 1 2 15 9 0.53 -9 30 hour >20 hour >10 hour 78 7365 253.97 7989335 J Biol Chem. 1994;269(50):31635-31641 "Mor A, Hani K, Nicolas P. 1994" The Vertebrate Peptide Antibiotics Dermaseptins Have Overlapping Structural Features but Target Specific Microorganisms N/A Anti-HIV DRAVPe02223 SGSWNFFDWFSGLMSWFGG 19 RVFV-9 Rift Valley fever virus (RVFV) Gc stem region P03518##P21403 Not experimentally validated 11588 GP Not Available 1137-1155 Not Available Not Available Not Available Not Available 6EGT EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2215.43 C108H131N23O27S1 ARCQETVOU F 3.8 0 1 -1 5 9 0.126 -0.05 1.9 hours >20 hours >10 hours 20.53 16500 7.448 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02224 CLGIGSCNDFAGCGYAVVCFW 21 Tricyclic peptide RP 71955 Streptomyces sp. (strain SP9440) (Gram-positive bacteria) P37046 Experimentally Validated 72594 Not Available Not Available 1 to 21 Not Available Not Available Not Available Not Available 1RPB##1RPC HIV-1 Retroviridae Antiviral Assay "[Ref:8286361] inhibited the HIV-1 aspartyl protease (IC50, 35 ug/ml) a" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Cyclization of a N-terminal between Cys1 and Asp9 Free "An internal amide bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well as two disulfide bridges, one between C1 and C13 and one between C7 and C19. In contrast. Class 2 lassos do not have disulfide bonds. " L Not found Not Available 2185.53 C97H137N23O27S4 EHKMPQRT CG 3.8 0 1 -1 11 9 1.157 19.81 1.2 hour >20 hour >10 hour 74.29 7240 362 8286361;##8270499 Biochemistry. 1994 Jan 11;33(1):42-50;##J Antibiot (Tokyo). 1993 Nov;46(11):1756-1757. "Fréchet D, Guitton JD, Herman F, Faucher D, Helynck G, Monegier du Sorbier B, Ridoux JP, James-Surcouf E, Vuilhorgne M." "Solution structure of RP 71955, a new 21 amino acid tricyclic peptide active against HIV-1 virus;##Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite." 10.1021/bi00167a006;##10.7164/antibiotics.46.1756 Anti-HIV DRAVPe02221 WNFFDWFSGLMSWFGGPLKTI 21 RVFV-7 Rift Valley fever virus (RVFV) Gc stem region P21401 Not experimentally validated 11589 Not Available Not Available 1140-1160 Not Available Not Available Not Available Not Available 6EGT EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2536.93 C127H166N26O28S1 ARCQETVOU F 5.84 1 1 0 4 11 0.31 -0.4 2.8 hours 16 mins 8 mins 55.71 16500 6.504 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02222 SWNFFDWFSGLMSWFGGPLK 20 RVFV-8 Rift Valley fever virus (RVFV) Gc stem region P03518##P21403 Not experimentally validated 11588 GP Not Available 1139-1158 Not Available Not Available Not Available Not Available 6EGT EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2409.75 C120H153N25O27S1 ARCQETVOU F 5.55 1 1 0 4 10 0.095 -0.14 1.9 hours >20 hours >10 hours 39 16500 6.847 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02218 FVGAAVSCDAAFLNLTGCY 19 RVFV-4 Rift Valley fever virus (RVFV) Gc stem region P03518##P21403 Not experimentally validated 11588 GP Not Available 1022-1040 Not Available Not Available Not Available Not Available 4HJ1##4HJC##6EGT##6F9B EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 1922.2 C86H128N20O26S2 RQEHIKMPWOU A 3.8 0 1 -1 3 12 1.221 -0.74 1.1 hours 3 min 2 min 92.63 1490 0.775 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02219 WNFFDWFSGLMSWFGGPLKLY 21 RVFV-5 Rift Valley fever virus (RVFV) Gc stem region  P03518 Not experimentally validated 11588 GP Not Available 1140-1160 Not Available Not Available Not Available Not Available 6EGT EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2599 C132H168N26O28S1 ARCQETVOU F 5.83 1 1 0 4 11 0.248 -0.52 2.8 hours 3 min 2 mins 55.71 17990 6.922 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02220 WNFFDWFSGLMSWFGGPLK 19 RVFV-6 Rift Valley fever virus (RVFV) Gc stem region P03518##P21403 Not experimentally validated 11588 GP Not Available 1140-1158 Not Available Not Available Not Available Not Available 4HJ1##4HJC##6EGT##6F9B EBOV Filoviridae Virus inhibition assays [Ref:24069485]EBOV:IC50=50µM No hemolysis information or data found in the reference(s) presented in this entry "[Ref:24069485] Very very less toxic (MTT toxicity assays on Vero E6 cells assessed the toxicity of RVFV-6, revealing a reduction in cell viability at peptide concentrations up to 50 microM, suggesting" No predicted structure available Linear Free Free None L DII domain of the E protein (RVFV-6 interact with a specific region of the Ebola virus (EBOV) during "RVFV-6, a peptide derived from the RVFV Gc stem region, exhibits potent inhibition of Ebola virus (EBOV), achieving nearly 100% reduction in plaques at a 50 microM concentration. Despite not interfering with EBOV binding to cells, RVFV-6 effectively inhibits EBOV infectivity, suggesting its potential as an antiviral therapy against EBOV and related viruses." 2322.67 C117H148N24O25S1 ARCQETVOU F 5.84 1 1 0 3 10 0.142 -0.32 2.8 hours 15 mins 7 mins 41.05 16500 7.104 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02216 WGCGCFNVNPSCLFVHTYL 19 RVFV-2 Rift Valley fever virus (RVFV) Gc stem region P03518##P21401 Not experimentally validated 11588 GP Not Available 821-839 Not Available Not Available Not Available Not Available 4HJ1##4HJC##6EGT##6F9B EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2160.51 C99H138N24O25S3 ARDQEIKMKMOU C 6.71 0 0 0 10 10 0.674 -0.41 2.8 hours 11 mins 3 mins 71.58 6990 3.235 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02217 LGASSSRFTNWGSVSLSLD 19 RVFV-3 Rift Valley fever virus (RVFV) Gc stem region P03518##P21402 Not experimentally validated 11588 GP Not Available 875-893 Not Available Not Available Not Available Not Available 4HJ1##4HJC##6EGT##6F9B EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 1984.15 C86H134N24O30 CQEHIKMPYOU S 5.84 1 1 0 6 7 0.079 1.33 5.5 hours 3 min 2 mins 82.11 5500 2.772 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02214 HGVSGHGQHGVHG 13 Alloferon-1 Calliphora vicina (Blue blowfly) (Calliphora erythrocephala) P83412 Experimentally Validated 7373 Not Available Not Available 1 to 13 Not Available Not Available Not Available Not Available None "IAV,IBV, HHV-1" Orthomyxoviridae Antiviral Assay [Ref:21766388] HHV:inhibited the Human Herpes Virus type 1 (HHV-1) multiplication No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Amination Free "the N-terminal amine, the three imidazoles of H1, H6, and H9 participate in the coordination of Zn(II)" L Not found Not Available 1265.31 C52H76N22O16 ACDEFIKLMNPRTWY G 7.1 4 0 4 6 2 -0.823 -14.8 3.5 hour 30 min >10 hour 44.62 0 0 12235362 "Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12628-32;##an official publication of the European Peptide Society, 17(11), 715–719." "Chernysh S, Kim SI, Bekker G, Pleskach VA, Filatova NA, Anikin VB, Platonov VG, Bulet P;##Kuczer, M., Midak-Siewirska, A., Zahorska, R., Luczak, M., & Konopińska, D." Antiviral and antitumor peptides from insects;##Further studies on the antiviral activity of alloferon and its analogues 10.1073/pnas.192301899;##10.1002/psc.1388 "Anti-IAV,Anti-IBV, Anti-HHV-1" DRAVPe02215 YWTGSISPKCLSSRRCHLV 19 RVFV-1 Rift Valley fever virus (RVFV) Gc stem region P03518 Not experimentally validated 11588 GP Not Available 762-780 Not Available Not Available Not Available Not Available 4HJ1##4HJC##6EGT##6F9B EBOV Filoviridae Virus inhibition assays Not Available No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found Not Available 2193.57 C96H153N29O26S2 ANDQEMFOU S 9.5 3 0 3 2 7 -0.153 1.67 2.8 hours 10 mins 2 mins 76.84 6990 3.187 24069485 PLoS Negl Trop Dis. 2013;7(9):e2430. "Koehler JW, Smith JM, Ripoll DR, et al." "A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses" 10.1371/journal.pntd.0002430 Anti-EBOV DRAVPe02213 QLESLTDRELLLLIARKTCGSVE 23 E30pep-wt Synthetic construct Q05323 Experimentally Validated 128952 VP30(911826) Not Available 91-113 Not Available AF086833.2 Genomic RNA "Chromosome:8,509 - 9,375" 5DVW##5T3T EBOV Filoviridae Virus inhibition assays [Ref:12912982] IC50 = 1 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Amination Carboxylation None L VP30 "E30pep-wt seemed to bind efficiently to VP30 and consequently blocked the oligomerization of the protein. When E30pep-wt was transfected into EBOV-infected cells, the peptide inhibited viral replication suggesting that inhibition of VP30 oligomerization represents a target for EBOV antiviral drugs." 2588.01 C111H195N31O37S1 NHMFPWYOU L 4.87 3 4 -1 5 10 0.087 1.71 0.8 hours 10 mins 10 hours 135.67 0 0 12912982  J Biol Chem. 2003;278(43):41830-6. "Hartlieb B, Modrof J, Mühlberger E, et al." Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide. 10.1074/jbc.M307036200 Anti-EBOV DRAVPe02212 DDIWK 5 BST-2/Tetherin HIV-1 No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV-1,EBOV,MV" Filoviridae Antiviral Assay [Ref:19036818]HIV-1:tetherin inhibits the release of a variety of lentiviruses in a manner that can be reversed by the HIV-1 Vpu protein. No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not found "BST-2, or Tetherin, restricts the release of Ebola virus-like particles (VLPs) from infected cells by tethering the budding virions to the cell membrane, thereby inhibiting their release. This restriction is similar to BST-2's activity against other enveloped viruses like HIV-1. However, Ebola glycoprotein (GP) has evolved mechanisms to counteract BST-2, enabling efficient release of Ebola VLPs. The specific molecular mechanisms by which Ebola GP antagonizes BST-2 are still under investigation, but it likely involves disrupting the interaction between BST-2 and virions, potentially by interfering with BST-2 ectodomain self-interaction." 675.74 C31H45N7O10 ARNCQEGHLMFPSTYVOU D 4.21 1 2 -1 0 2 -1.46 3.14 1.1 hours 3 min >10 hour 78 8800 8.139 19929170##19036818 "AIDS research and human retroviruses, 25(12), 1197–1210##Journal of virology, 83(4), 1837–1844." "Tokarev A, Skasko M, Fitzpatrick K, et al##Jouvenet, N., Neil, S. J., Zhadina, M., Zang, T., Kratovac, Z., Lee, Y., McNatt, M., Hatziioannou, T., & Bieniasz, P. D. (2009)." Antiviral activity of the interferon-induced cellular protein BST-2/tetherin##Broad-Spectrum Inhibition of Retroviral and Filoviral Particle Release by Tetherin 10.1089/aid.2009.0253##10.1128/JVI.02211-08 "Anti-EBOV,Anti-HIV" DRAVPe02211 WWIVVV 6 BetaWWI-4 HIV gp41 C-terminus (C-peptides) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,EBOV" Retroviridae HIV infectivity assays [Ref:16173723]HIV:EC50=5.3 ± 0.5 μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein.  Inhibit viral fusion with host cell by intramolecular protein-protein interactions. 801 C43H60N8O7 ARNDCQEGHLKMFPSTYOU V 5.49 0 0 0 0 6 2.55 -3.61 100 hours >20 hours >10 hour 210 11000 13.733 16173723 J Am Chem Soc. 2005;127(38):13126-7. "Stephens OM, Kim S, Welch BD, et al." Inhibiting HIV fusion with a beta-peptide foldamer. 10.1021/ja053444+ "Anti-EBOV,Anti-HIV" DRAVPe02209 VVVIWW 6 BetaWWI-2 HIV gp41 C-terminus (C-peptides) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,EBOV" Retroviridae HIV infectivity assays [Ref:16173723]HIV:EC50=15 ± 1.6μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein.  Inhibit viral fusion with host cell by intramolecular protein-protein interactions. 801 C43H60N8O7 ARNDCQEGHLKMFPSTYOU V 5.49 0 0 0 0 6 2.55 -3.61 100 hours >20 hours >10 hour 210 11000 13.733 16173723 J Am Chem Soc. 2005;127(38):13126-7. "Stephens OM, Kim S, Welch BD, et al." Inhibiting HIV fusion with a beta-peptide foldamer. 10.1021/ja053444+ "Anti-EBOV,Anti-HIV" DRAVPe02210 VVVWWI 6 BetaWWI-3 HIV gp41 C-terminus (C-peptides) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,EBOV" Retroviridae HIV infectivity assays [Ref:16173723]HIV:EC50=13 ± 1.9μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein.  Inhibit viral fusion with host cell by intramolecular protein-protein interactions. 801 C43H60N8O7 ARNDCQEGHLKMFPSTYOU V 5.49 0 0 0 0 6 2.55 -3.61 100 hours >20 hours >10 hour 210 11000 13.733 16173723 J Am Chem Soc. 2005;127(38):13126-7. "Stephens OM, Kim S, Welch BD, et al." Inhibiting HIV fusion with a beta-peptide foldamer. 10.1021/ja053444+ "Anti-EBOV,Anti-HIV" DRAVPe02207 EYLFEVDNL 9 P2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available 231 to 239 Not Available Not Available Not Available Not Available "3CSY, 3S88, 3VE0, 5F1B, 5FHC, 5HJ3, 5JQ3, 5JQ7, 5K" EBOV Filoviridae PRNT50 assays [Ref:12186901]EBOV:IC50:5.3 ± 0.67 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Other (immunogenic epitope). "Peptide P2 acts against Ebola virus by stimulating cytotoxic T lymphocytes (CTLs) specific to the Ebola virus glycoprotein (GP). When used in immunization alongside liposome-encapsulated irradiated Ebola virus, P2 contributes to the generation of a CTL response aimed at targeting and eliminating virus-infected cells. This specificity was demonstrated by the enhanced lysis of target cells infected with vaccinia virus GP when effector cells from mice immunized with liposome-encapsulated virus were cultured with peptide P2, suggesting its role in inducing a more precise immune response against Ebola virus GP." 1141.24 C53H76N10O18 ARCQGHIKMPSTWOU EL 3.57 0 3 -3 2 4 -0.078 1.36 1 hours 30 min >10 hours 118.89 1490 1.306 12186901 J Virol. 2002;76(18):9176-85. "Rao M, Bray M, Alving CR, et al." Induction of immune responses in mice and monkeys to Ebola virus after immunization with liposome-encapsulated irradiated Ebola virus: protection in mice requires CD4(+) T cells. 10.1128/jvi.76.18.9176-9185.2002 Anti-EBOV DRAVPe02208 IWWVVV 6 BetaWWI-1 HIV gp41 C-terminus (C-peptides) No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,EBOV" Retroviridae HIV infectivity assays [Ref:16173723]HIV:EC50=27 ± 2.5μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein.  Inhibit viral fusion with host cell by intramolecular protein-protein interactions. 801 C43H60N8O7 ARNDCQEGHLKMFPSTYOU V 5.52 0 0 0 0 6 2.55 -3.61 20 hours 30 min >10 hour 210 11000 13.733 16173723 J Am Chem Soc. 2005;127(38):13126-7. "Stephens OM, Kim S, Welch BD, et al." Inhibiting HIV fusion with a beta-peptide foldamer. 10.1021/ja053444+ "Anti-EBOV,Anti-HIV" DRAVPe02206 LYDRLASTVI 10 P1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available 161 to 169 Not Available Not Available Not Available Not Available "3CSY, 3S88, 3VE0, 5F1B, 5FHC, 5HJ3, 5JQ3, 5JQ7, 5K" EBOV Filoviridae PRNT50 assays [Ref:12186901]EBOV:IC50=6.0 ± 0.94 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Other (immunogenic epitope). "Peptide P1 likely works against the Ebola virus by serving as an immunogenic epitope, stimulating the activation and proliferation of cytotoxic T lymphocytes (CTLs) specific to the Ebola virus glycoprotein (GP). This activation of CTLs enables them to recognize and eliminate virus-infected cells, contributing to the immune response against Ebola virus infection." 1150.34 C52H87N13O16 NCQEGHKMFPWOU L 5.84 1 1 0 3 5 0.73 0.91 5.5 hours 3 min 2 min 156 1490 1.295 12186901 J Virol. 2002;76(18):9176-85. "Rao M, Bray M, Alving CR, et al." Induction of immune responses in mice and monkeys to Ebola virus after immunization with liposome-encapsulated irradiated Ebola virus: protection in mice requires CD4(+) T cells. 10.1128/jvi.76.18.9176-9185.2002 Anti-EBOV DRAVPe02205 RRRRRRRRRFFC 13 PMO Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HIV,EBOV" Filoviridae Antiviral Assay [Ref:16495261]EBOV:EC50= 5.0 microM No hemolysis information or data found in the reference(s) presented in this entry [Ref:16495261]Cytotoxic at 10 microM concentration No predicted structure available Linear Amination Free "(In the peptide sequence, N-terminus is modified with an amino group (NH2).)" L VP35 "PMOs, a type of single-stranded antisense agents, exert their antiviral action against Ebola virus by binding to specific RNA sequences, particularly within the VP35 translation start site region, thereby impeding viral replication. Their mechanism involves blocking the translation of essential viral proteins, like VP35, crucial for Ebola's replication, leading to a sequence-specific and dose-dependent inhibition of viral amplification both in vitro and in vivo. This inhibition ultimately safeguards against lethal Ebola infection in mice, showcasing PMOs' efficacy in curtailing viral spread." 1821.19 C75H133N39O13S1 ANDQEGHILKMPSTWYVOU R 12.54 9 0 9 0 3 -2.7 10.58 1 hour 3 min 2 min 0 0 0 16495261 Antimicrob Agents Chemother. 2006;50(3):984-93. "Enterlein S, Warfield KL, Swenson DL, et al."  VP35 knockdown inhibits Ebola virus amplification and protects against lethal infection in mice. 10.1128/AAC.50.3.984-993.2006 "Anti-EBOV,Anti-HIV" DRAVPe02204 RVKRCMK 7 Peptidyl chloromethylketone Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae Endoproteolytic Cleavage Inhibition Assay. ≥90% (HPLC) [Ref:9576958]EBOV:IC50=25 microM or 80 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "Peptidyl chloromethylketones, exemplified by decRVKR-cmk, function as potent inhibitors of the endoproteolytic cleavage of the Ebola virus glycoprotein. They operate by obstructing the cleavage of the glycoprotein specifically at a multibasic amino acid motif situated between positions 497 and 501 of the ORF. This cleavage is essential for the glycoprotein's maturation into its functional state. By impeding this cleavage process, peptidyl chloromethylketones hinder the glycoprotein's transformation into its mature form, thereby disrupting the viral replication cycle and potentially diminishing the virus's infectivity." 920.2 C37H73N15O8S2 ANDQEGHILFPSTWYOU RK 11.01 4 0 4 0 3 -1.171 4.75 1 hours 2 min 2 mins 41.43 0 0 9576958 Proc Natl Acad Sci U S A. 1998;95(10):5762-7.  "Volchkov VE, Feldmann H, Volchkova VA, et al." Processing of the Ebola virus glycoprotein by the proprotein convertase furin 10.1073/pnas.95.10.5762 Anti-EBOV DRAVPe02202 WFQRIPLGWFHCTYQKGKQHCRLRIRQKVEE 31 delta18-48-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.8 342-372 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding" 3972.65 C181H276N56O42S2 ANDMVOU RQ 10.05 7 2 5 6 11 -1.029 2.75 2.8 hours 3 min 2 min 59.68 12490 3.144 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02203 ELQREESPTGPPGSIRT 17 delta1-17-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.9 325-341 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding" 1854.01 C77H128N24O29 ANDCHKMFWYVOU EP 4.79 2 3 -1 5 2 -1.371 3.29 1 hour 30 min >10 hours 45.88 0 0 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02201 SPTGPPGSIRTWFQRIPLGWFHCTYQKGKQHCRLRIRQKVEE 42 delta7-48-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.7 331-372 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50<25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding" 5023.82 C226H350N70O57S2 ANDMOU R 10.44 8 2 6 10 12 -0.964 2.5 1.9 hours >20 hours >10 hours 53.33 12490 2.486 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02200 HCTYQKGKQHCRLRIRQKVEE 21 delta28-48-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.6 352-372 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding" 2641.07 C111H186N40O31S2 ANDHMFPSWOU RQK 9.7 6 2 4 5 5 -1.619 4.1 3.5 houurs 10 min >10 hours 50.95 12490 0.564 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02199 GSIRTWFQRIPLGWFHCTYQKGKQHCRLRIRQKVEE 36 delta13-48-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.5 337-372 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding" 4487.23 C202H314N64O49S2 ANDMOU R 10.44 8 2 6 8 12 -0.939 2.78 30 hours >20 hours >10 hours 62.22 12490 2.783 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02198 ELQREESPTGPPGSIRTWFQRIPLGWFHCTYQKGKQHCR 39 delta1-39-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.4 325-363 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. " The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding to filovirus-permissive cells and inhibition of EBOV glycoprotein GP1,2 entry. These Fc-tagged peptides interfere with the viral entry process, potentially preventing superinfection of producer cells and inhibiting cell transduction with filoviruses. The mechanisms of action involve binding to cell surface receptors or disrupting key viral entry steps." 4656.28 C208H313N63O56S2 ANDMVOU RQGP 9.39 6 3 3 10 10 -1.136 2.58 1 hour 30 min >10 hour 40 12490 2.682 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02197 ELQREESPTGPPGSIRTWFQRIPLGWFHCTYQK 33 delta1-33-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.3 325-357 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50<25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. " The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding to filovirus-permissive cells and inhibition of EBOV glycoprotein GP1,2 entry. These Fc-tagged peptides interfere with the viral entry process, potentially preventing superinfection of producer cells and inhibiting cell transduction with filoviruses. The mechanisms of action involve binding to cell surface receptors or disrupting key viral entry steps." 3946.46 C180H266N50O49S1 ANDCEQGHMPSTOU P 8.3 4 3 1 9 9 -0.948 2.19 1 hour 30 min >10 hour 47.27 12490 3.165 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02196 ELQREESPTGPPGSIRTWFQRIPLGWFH 28 delta1-28-Fc eboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.2 325-352 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50 < 25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding to filovirus-permissive cells and inhibition of EBOV glycoprotein GP1,2 entry. These Fc-tagged peptides interfere with the viral entry process, potentially preventing superinfection of producer cells and inhibiting cell transduction with filoviruses. The mechanisms of action involve binding to cell surface receptors or disrupting key viral entry steps." 3322.73 C153H225N43O41 ANDCKMYVOU P 6.86 3 3 0 6 8 -0.871 2.13 1 hour 30 min >10 hour 55.71 11000 3.31 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02195 ELQREESPTGPPGSIRTWFQRIPLGWFHCTYQKGKQHCRLRIRQKVEE 48 delta-Fc EboV delta peptide "P60172, Q7T9E0" Experimentally Validated 128948 GP AAB37097.1  325-372 Not Available Not Available Not Available Not Available None EBOV Filoviridae Antiviral Assay [Ref:21697477]EBOV:IC50<25 nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Glycoprotein. "The efficacy of delta-Fc and its truncated versions (delta1-28-Fc, delta1-33-Fc, delta1-39-Fc, delta13-48-Fc, delta28-48-Fc, delta7-48-Fc, delta18-48-Fc, delta1-17-Fc) in inhibiting Ebola virus (EBOV) entry was investigated, demonstrating specific binding to filovirus-permissive cells and inhibition of EBOV glycoprotein GP1,2 entry. These Fc-tagged peptides interfere with the viral entry process, potentially preventing superinfection of producer cells and inhibiting cell transduction with filoviruses. The mechanisms of action involve binding to cell surface receptors or disrupting key viral entry steps." 5808.64 C258H402N80O70S2 ANDMOU R 9.69 9 5 4 11 13 -1.15 2.94 1 hour 30 min >10 hours 54.79 12490 2.15 21697477 J Virol. 2011;85(17):8502-13.  "Radoshitzky SR, Warfield KL, Chi X, et al." Ebolavirus delta-peptide immunoadhesins inhibit marburgvirus and ebolavirus cell entry 10.1128/JVI.02600-10 Anti-EBOV DRAVPe02193 YYSSRWNHGHFTPCS 15 eVpeL1 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae "AlphaLISA assay," [Ref:28574091]It inhibits Ebola virus No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Amidation Acetylation "(In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration.)" L VP24 "Exact MoA not known (eVpeL1, a macrocyclic peptide belonging to the GL1 group from the LY-library, was found to be a poor binder to the immobilized eVP24 compared to other peptides like eVpeD1 and eVpeD2)." 1841.98 C83H108N24O23S1 AQEILKMVOU S 8.21 1 0 1 7 3 -1.18 2.42 2.8 hours 10 min 2 min 0 8480 4.604 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02194 YFKSVRTGLRYVYCS 15 eVpeL2 Synthetic construct No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None EBOV Filoviridae "AlphaLISA assay," [Ref:28574091]EBOV:IC50 = 37 microM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Amidation Acetylation "(In the peptide sequence, the N-terminus is acetylated, and the tyrosine residue at position 1 is in the D-configuration.)" L VP24 eVpeL2 exhibit inhibitory activity against the protein-protein interaction (PPI) of VP24 and KPNA5. 1842.15 C85H128N22O22S1 ANDQEMPWOU Y 9.63 3 0 3 6 5 -0.133 1.79 2.8 hours 10 min 2 min 64.67 4470 2.427 28574091 Org Biomol Chem. 2017;15(24):5155-5160. "Song X, Lu LY, Passioura T, et al." Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.  10.1039/c7ob00012j Anti-EBOV DRAVPe02330 CKPTHYNSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=46%,0.1128(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1052.1849 H43C63N13O13S2 ADEFGILMQRVW CHKNPSTY 8.054953956604 2 0 0.825475820247868 6 3 -1.11111111111111 1.057 1.2 hours 1 hours 1.1 hours 0 1490 1.41610091534292 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02331 CLHKPWSRC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=7.4 × 10^8particles/μl in Vero E6,89%,0.4629 (p value)inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1129.3584 H49C74N16O10S2 ADEFGIMNQTVY CHKLPRSW 8.95718898773193 3 0 1.82646482134686 5 4 -0.677777777777777 1.373 1.2 hours 1 hours 1.1 hours 43.33 5500 4.87002177519554 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02332 CPRSGTAYC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=0.4629 µg/ml,63%,0.0903(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 963.0868 H38C60N10O14S2 AFHKMQRSTVWY CDEGILNP 4.05002841949462 0 2 -2.25576914309566 5 4 0.0888888888888888 0.737 1.2 hours 1 hours 1.1 hours 86.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02333 CVNSPPTMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:48%, 0.0004 (p value)inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 3815.43959999999 H153C259N55O46S6 DFHKMNPQW ACEGILRSTVY 9.2155138015747 7 2 4.74002156990843 18 16 -0.185294117647058 0.913 4.4 hours 20 hours 10 hours 63.24 2980 0.781037131343922 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02334 CNHTRNMAC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNVV:IC50=29% in Vero E6 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1679.82699999999 H75C111N20O23S0 CDHKLMSW AEFGINPQRTVY 4.53139781951904 1 2 -1.23528646276327 9 6 -0.36 0.894 1.0 hours 1 hours 1 hours 71.33 1490 0.88699610138425 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02335 CRNTDTALC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=9.5 × 10^8 particles/μl,80%,0.0397(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2100.5931 H97C172N28O22S0 CDFGHIMNQSTWY AEKLPRV 11.0003854751586 4 1 2.7608940743645 7 13 0.735 0.88 1.0 hours 1 hours 1 hours 156.5 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02336 CTKYWARNC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:37% inhibition in Vero E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 10637.8489 H465C752N132O151S0 CHMPW ADEFGIKLNQRSTVY 6.4041856765747 8 8 -0.195423527186704 56 40 -0.196875 0.891 4.4 hours 20 hours 10 hours 109.69 2980 0.280131822515358 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02337 COPHTLPTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:59%,0.0001(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1119.3122 H44C64N10O15S4 ADFGHIKLNPQRVY CEMSTW 4.05002841949462 0 2 -2.25407944206229 4 5 -0.0666666666666667 0.971 1.2 hours 1 hours 1.1 hours 0 5500 4.91373184353749 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02338 CEWTESMMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:47%, 0.0001( p value) highest inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2342.6708 H106C162N28O29S1 GHLMQ ACDEFIKNPRSTVWY 9.09959964752197 4 2 1.39140172489197 11 9 -0.55 1.147 7.2 hours 6 hours 6.5 hours 58.5 6990 2.98377390455373 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02339 CTNPATPFC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:48%,0.0068(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 666.7645 H25C40N6O10S2 AFGHIKLMNPQRSTWY CDEV 4.05002841949462 0 2 -2.25576914309566 2 4 1.06666666666666 0.702 1.1 hours 1 hours 1 hours 96.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02340 CPSTGYSYC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:76%,0.0005(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1473.88739999999 H71C126N18O14S0 CDEFGHIMNPQRSTW AKLVY 10.3015481948852 5 0 4.75410760819529 5 8 0.261538461538461 1.292 1.3 hours 1.1 hours 1.2 hours 134.62 1490 1.01093204270557 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02341 CPGHIHRTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=8.0 × 10^8 particles/μl,83%,<0.0001(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1129.3036 H48C74N10O16S2 ACDFGHKPQRTVW EILMNSY 4.05002841949462 0 2 -2.53523161783498 4 5 -0.0555555555555556 0.976 1.9 hours 2 hours 1.8 hours 86.67 1490 1.31939719310201 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02342 CTNRHAAGC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:54%,0.0136(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1559.8359 H64C116N24O18S1 CDEFHIKNPQWY AGLMRSTV 11.9999677658081 3 0 2.79584458815408 8 7 0.353333333333333 0.644 4.4 hours 20 hours 10 hours 97.33 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02343 CQGPVKPLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:44%,0.0002(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 923.0694 H35C60N12O12S2 ADEFHIKLMNQWY CGPRSTV 8.07210254669189 1 0 0.740289634091281 6 3 0.0555555555555555 0.48 1.2 hours 1 hours 1.1 hours 32.22 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02344 CHARNSTQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:49%,0.0017(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 4891.6492 H225C351N60O59S1 ACDGHIPY EFKLMNQRSTVW 9.63069019317626 13 9 3.74926253802403 26 11 -1.77297297297297 1.868 100 hours 60 hours 90 hours 39.46 11000 2.24873034640342 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02345 CFPTTSRGC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:74%,0.0019(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2052.2176 H85C136N34O25S0 ACEFHIKLMNQVY DGPRSTW 11.9999677658081 5 1 3.46121722065743 17 1 -2.11111111111111 1.068 1.9 hours 2 hours 1.8 hours 0 5500 2.68002769296979 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02346 CRHNNLHHC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:46%, 0.1418 (p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 3068.5253 H143C220N37O37S0 CDEMPVW AFGHIKLNQRSTY 9.99222888946533 3 0 1.48336278072321 15 14 0.562068965517241 0.697 7.2 hours 6 hours 6.5 hours 104.48 1490 0.485575269658034 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02347 CQYNPLPYC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:27% inhibition in Verso E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1325.4243 H56C89N16O20S0 CDEFHIKLMNRWY AGPQSTV 5.57001667022705 0 0 -0.204125412145913 10 5 -0.0399999999999999 0.285 4.4 hours 20 hours 10 hours 46 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02348 CHSPLTSSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:74%,0.1709(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1680.9425 H72C114N19O22S2 ADEGHKRTVWY CFILMNPQS 5.51812267303466 0 0 -0.249799375909707 8 7 0.386666666666666 0.658 20 hours 15 hours 18 hours 104 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02349 CSPQLAPFC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=3.8 × 10^8 particles/μl,83%,0.0056 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 987.114699999999 H38C59N14O12S2 ADEFKLMPRSTWY CGHINQV 6.72305240631103 1 0 -0.17252617775413 5 4 -0.0444444444444444 0.846 1.2 hours 1 hours 1.1 hours 75.56 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02350 CNGVIHNQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:49%,0.6832(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1713.8446 H88C98N18O18S0 ACEGIKLMQRS DFHNPTVWY 5.04942836761474 1 1 -1.51550645843694 5 7 -0.9 1.494 7.2 hours 6 hours 6.5 hours 24.17 19480 11.3662580609701 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02351 CPPGKSSMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:77%,0.0001(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1040.3067 H46C86N17O9S0 ACDEFGHMNPSTWY IKLQRV 11.9999677658081 4 0 3.75808361239129 5 3 -0.975 1.659 48.0 minutes 42.0 minutes 36.0 minutes 133.75 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02352 CPPPQGQTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=7.0 × 10^8 particles/μl,81%,0.1209(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1242.3783 H60C80N13O15S0 CEGHILMNPRT ADFKQSVWY 5.83494319915771 1 1 -0.240775626868854 4 6 -0.0899999999999999 1.153 1.1 hours 1 hours 1 hours 68 6990 5.62630561077894 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02353 CPFVKTQLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=2.7 × 10^8 particles/μl,91%,0.0147 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 3200.85189999999 H146C241N47O31S1 DEKMQWY ACFGHILNPRSTV 11.9999677658081 7 0 4.2101104426431 14 14 0.492857142857142 0.902 20 hours 15 hours 18 hours 138.93 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02354 CHNLKRPTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:79%,0.0001(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1774.9049 H75C113N21O26S1 ACHIKNPQTW DEFGLMRSVY 4.40743198394775 2 4 -2.15744969721474 10 5 -0.933333333333333 1.101 1.3 hours 1 hours 1 hours 45.33 1490 0.839481597014015 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02355 CQSQNHNTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:76%,0.4057(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 925.0388 H35C57N10O14S2 ADFHKLMNPRTWY CEGIQSV 4.05002841949462 0 1 -1.2568899040355 5 4 0.522222222222222 0.567 1.2 hours 1 hours 1.1 hours 75.56 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02356 CVSGQESIC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:56%,0.1935(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1539.76179999999 H63C108N24O18S1 CEFINPQTVWY ADGHKLMRS 10.8352174758911 4 1 1.88315053624951 9 6 -0.446666666666666 0.915 4.4 hours 20 hours 10 hours 72 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02357 CQSIRGPMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:76%,0.58429(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1772.0551 H74C124N22O23S2 FGKMPQSWY ACDEHILNRTV 5.2899709701538 2 2 -1.53050997456375 7 9 0.56875 0.804 7.2 hours 6 hours 6.5 hours 128.12 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02358 CLFNHPKYC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:79%,0.0008(pvalue) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1124.335 C51H55N13O3S2 ADEGIMQRSTVW CFHKLNPY 8.055 2 0 0.825 5 3 -0.211 0.617 1.2 hours 1 hours 1.1 hours 43.333 1490 1.6555555555556 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02359 CTPTVTRSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:21% inhibition in Vero E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 967.122 C37H48N12O5S2 ADEFGHIKLMNQWY CPRSTV 8.072 1 0 0.74 6 1 0.022 0.291 1.2 hours 1 hours 1.1 hours 32.222 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02360 CLALRHSNC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=6.0 × 10^8 particles/μl,83%,0.0491(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1016.199 C40H51N15O3S2 DEFGIKMPQTVWY ACHLNRS 8.082 2 0 0.827 5 3 0.267 0.596 1.2 hours 1 hours 1.1 hours 97.778 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02361 CNPYNTSMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:49%,0.1999(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2177.4738 H90C157N37O25S0 ACDFHLMNVWY EGIKPQRST 11.9999677658081 7 1 5.7608640746645 17 1 -2.43333333333333 1.428 1.0 hours 1 hours 1 hours 21.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02362 CMTSHPTLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:64%,0.0001(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 883.988499999999 H36C51N9O12S2 DHIKLMNQRTVWY ACEFGPS 4.05002841949462 0 1 -1.2568899040355 4 5 0.566666666666666 0.544 1.2 hours 1 hours 1.1 hours 22.22 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02363 CNLLRQQTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:54%,0.1822(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1746.079 H79C130N20O21S1 CHNQSVWY ADEFGIKLMPRT 6.49285449981689 2 2 -0.0385489104075915 7 9 0.5375 0.815 20 hours 15 hours 18 hours 116.25 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02364 CDATSAQVC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:46%, 0.1483 (p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1856.1035 H83C128N20O25S1 FKMNQRW ACDEGHILPSTVY 4.35172977447509 1 2 -2.45964812071277 8 10 0.694444444444444 0.589 1.9 hours 2 hours 1.8 hours 113.89 1490 0.802756958326947 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02365 CLWPTLKGC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:48%,0.8779 (p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1274.49329999999 H52C93N19O15S1 CEFHINPQTVWY ADGKLMRS 10.8352174758911 3 1 1.79597634799492 7 5 -0.408333333333333 0.934 4.4 hours 20 hours 10 hours 81.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02366 CNQSTLLTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:74%,0.0011(p value)inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1520.7718 H68C114N19O19S0 CDEFHMRWY AGIKLNPQSTV 10.0027372360229 2 0 1.7581036121913 10 5 -0.36 0.757 48.0 minutes 42.0 minutes 36.0 minutes 84.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02367 CLALNMSYC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:58%,0.0044 (p value)inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1682.0632 H75C138N24O18S0 ACDEFHMNPQTWY GIKLRSV 11.9999677658081 4 0 3.73197038815714 9 7 0.64375 0.794 100 hours 60 hours 90 hours 151.87 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02368 CTNSTLQSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:72%,0.0002(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1470.6534 H60C101N21O19S1 CEFINPQTVWY ADGHKLMRS 8.79859676361084 3 1 0.883160536149516 9 6 -0.2 0.753 4.4 hours 20 hours 10 hours 72 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02369 CPSRLSSQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:35% inhibition in Vero E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 993.116199999999 H38C61N12O14S2 ADEFGKLMNPRVWY CHIQST 6.72305240631103 1 0 -0.17252617775413 6 3 -0.0111111111111111 0.624 1.2 hours 1 hours 1.1 hours 43.33 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02370 CNTSSTPHC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:71%,0.5842(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1566.7211 H64C109N25O20S0 ACDEFHIKMNQVWY GLPRST 11.9999677658081 3 0 2.76007161448929 15 1 -1.2125 0.637 30 hours 15 hours 28 hours 24.38 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02371 CLTSPTSTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:70%,0.0418(P value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1916.1237 H84C122N26O23S1 ACEGKPSW DFHILMNQRTVY 6.91835117340087 3 1 -0.065438249260681 9 6 -0.88 1.227 5.5 hours 10 hours 6 hours 71.33 1490 0.777611591568958 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02372 CLTDRHRTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=39%,0.3065(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1913.17819999999 H86C139N23O25S0 CEFHIMNQSY ADGKLPRTVW 8.74773120880127 2 1 0.760213374230145 11 7 0.00555555555555558 0.668 2.8 hours 2.5 hours 2.6 hours 81.11 5500 2.87479754891625 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02373 CQAMHNRFC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:18%inhibition in Vero E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 924.0772 H34C55N11O12S3 ADEFIKNPQRTVWY CGHLMS 6.72305240631103 1 0 -0.17252617775413 5 4 0.522222222222222 0.507 1.2 hours 1 hours 1.1 hours 43.33 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02374 CKPDAISVC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:72%,0.0068(P value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1602.95789999999 H80C108N15O15S2 CDEGHIKNPRSV AFLMQTWY 5.52431812286376 0 0 -0.240897386809698 2 10 1.04166666666666 1.055 48.0 minutes 42.0 minutes 36.0 minutes 105.83 12490 7.79184531296798 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02375 CIHAPHTQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=8.7 × 10^7 particles/μl,83%,0.0004 (p value)inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1055.1922 H41C64N16O12S2 EFGKLMNPQSVWY ACDHIRT 6.8999921798706 3 1 -0.0842412284596996 5 4 -0.422222222222222 1.099 1.2 hours 1 hours 1.1 hours 54.44 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02376 CQSASPRLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:70%,0.0203(P value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 3783.2488 H161C276N49O54S0 CFHMPWY ADEGIKLNQRSTV 8.40172939300537 6 5 0.740645293958466 21 14 -0.385714285714285 0.993 100 hours 60 hours 90 hours 103.14 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02377 CNPMKPLMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:61%,0.7131(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1036.356 C42H55N11O2S4 ADEFGHIQRSTVWY CKLMNP 8.058 1 0 0.739 3 3 0.222 0.421 1.2 hours 1 hours 1.1 hours 43.333 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02378 CHPTGLHQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50= 39% inhibition in Vero E6 cells, 0.0001(p value) Highest inhibition" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 995.137 C40H44N14O3S2 ADEFIKMNRSVWY CGHLPQT 6.898 2 0 -0.085 6 1 -0.422 0.3 1.2 hours 1 hours 1.1 hours 43.333 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02379 CYETKTHSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=52%,0.5725(p value) inhibition in Vero E6" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1071.185 H43C64N12O15S2 ADFGILMNPQRVW CEHKSTY 6.72987308502197 2 1 -0.171713717778921 6 3 -1.01111111111111 1.11 1.2 hours 1 hours 1.1 hours 0 1490 1.39098288344217 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02380 CTPSLPWLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50= 42%, 0.0875 (p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1605.8311 H75C113N18O20S0 ACEHMNRSTW DFGIKLPQVY 5.83494319915771 1 1 -0.240775626868854 9 7 0.49375 0.623 1.1 hours 1 hours 1 hours 103.12 1490 0.927868441456888 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02381 CSGSETKVC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1A1Q SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:52%,0.0643(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1521.62919999999 H61C106N20O24S0 CDFGHLMPQWY AEIKNRSTV 8.79279460906982 2 1 0.797676048928295 10 5 -0.393333333333333 0.687 4.4 hours 20 hours 10 hours 65.33 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02382 CNTKNFHSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:61%,0.0007(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1678.8375 H73C117N19O25S0 ACFHIKMQW DEGLNPRSTVY 4.3681562423706 1 2 -1.59888118361931 10 5 -0.373333333333333 0.761 7.2 hours 6 hours 6.5 hours 97.33 1490 0.88751889328181 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02383 CSTNPPTQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:47%, 0.2520( p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1019.2378 H46C68N10O11S2 ADEFGHIKMNQRVY CLPSTW 5.51141567230224 0 0 -0.259700366008717 4 5 0.777777777777777 0.647 1.2 hours 1 hours 1.1 hours 86.67 5500 5.39618919157041 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02384 CRTLPPILC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:5% in Vero E6 No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 992.133 H41C59N13O11S2 DEFILMNPQRVY ACGHKSTW 8.06797657012939 2 0 0.826474821246869 5 4 -0.344444444444444 1.012 1.2 hours 1 hours 1.1 hours 11.11 5500 5.54361159239739 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02385 CTESTINTC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:22% inhibition in Verso E6 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1258.4939 H52C93N19O14S1 CEFHINPQSTVWY ADGKLMR 10.8352174758911 3 1 1.79597634799492 6 6 -0.191666666666666 0.938 4.4 hours 20 hours 10 hours 90 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02386 CRSLTDNQC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:IC50=2.9 × 10^8 particles/μl,84%,0.0094(P value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1717.0178 H76C119N19O21S2 EGKMQRWY ACDFHILNPSTV 5.07619953155517 1 1 -1.17140541681428 6 10 1.1375 0.616 1.2 hours 1 hours 1.1 hours 128.12 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02387 CTQKNIAAC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:71%,0.0021(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2269.5569 H103C158N29O28S0 ACEHLMW DFGIKNPQRSTVY 9.98616886138916 3 1 1.75920437333114 12 8 -0.125 0.866 1.3 hours 1.1 hours 1.2 hours 77.5 1490 0.656515815928651 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02388 CGFSNFRSC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:76%,0.0387(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 965.1491 H38C66N12O12S2 ADEFGHKMNQTVWY CILPRS 8.07210254669189 1 0 0.740289634091281 5 4 0.533333333333333 0.566 1.2 hours 1 hours 1.1 hours 86.67 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02389 CSTPELTFC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:63%,0.2126(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 2889.48189999999 H137C224N36O31S0 ACEIKMNQWY DFGHLPRSTV 10.0290403366088 4 1 1.13397800522737 13 13 0.846153846153846 0.735 20 hours 15 hours 18 hours 164.62 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02390 CNPMKPLMC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:61%,0.7131(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic  Free Free None L beta-3 integrins Blocking of SNV entry into Vero E6 cells 1039.1448 H38C63N14O15S2 AEFGHIKMPVWY CDLNQRST 5.82255229949951 1 1 -0.258589604968873 6 3 -0.855555555555555 0.92 1.2 hours 1 hours 1.1 hours 43.33 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02391 CHLLLPRPC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:16% inhibition in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L beta-3 integrins Not Available 1802.9399 H80C117N23O24S0 ACFIMQ DEGHKLNPRSTVWY 6.76596584320068 3 2 -0.145563696773568 11 4 -1.36666666666666 1.199 30 hours 15 hours 28 hours 45.33 6990 3.87700111357012 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02392 CHTKIFPNC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:49%,0.6223(p value) inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L beta-3 integrins Not Available 1681.94909999999 H71C121N32O15S0 CDEILMPSTVWY AFGHKNQR 11.9999677658081 8 0 6.88001177351166 11 2 -2.74615384615384 1.932 4.4 hours 20 hours 10 hours 7.69 0 0 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02393 CSLTNTLLC 9 - Phage display No entry found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:15919886]SNV:49%,0.1870(p value) inhibition in VeroE6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L beta-3 integrins Not Available 1506.8725 H74C121N17O15S0 CDEGHILMNQRSW AFKPTVY 10.1768663406372 4 0 3.75510660919429 6 7 0.169230769230769 1.152 1.3 hours 1.1 hours 1.2 hours 96.92 1490 0.988802967736156 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02394 KKKKVVAATYVFF 13 P153 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1009.11709999999 H41C57N12O13S2 DEFGIKLMNRVW ACHPQSTY 6.72219982147216 1 0 -0.173525178753131 5 4 -0.477777777777777 0.807 1.2 hours 1 hours 1.1 hours 11.11 1490 1.47653825309273 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02395 KKKKLLLPTLFFF 13 P158 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1A1R##1A1V HCV "Flaviviridae,Paramyxoviridae,Coronaviridae" Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1091.30029999999 H51C84N12O13S0 CDEHMNPQRTWY AFGIKLSV 8.46510181427002 1 0 0.459147458218598 5 6 1.32727272727272 0.535 1.9 hours 2 hours 1.8 hours 141.82 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02396 DEMEECASHLPYK 15 P194 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2100.5931 H97C172N28O22S0 CDFGHIMNQSTWY AEKLPRV 11.0003854751586 4 1 2.7608940743645 7 13 0.735 0.88 1.0 hours 1 hours 1 hours 156.5 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02397 AKLKVVAATYVKKK 14 P39 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 981.1056 H37C62N12O14S2 ADEFGILMNPQRVWY CHKST 8.06797657012939 2 0 0.826474821246869 7 2 -0.633333333333333 0.738 1.2 hours 1 hours 1.1 hours 0 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02398 DLEVVAATYV 10 P14 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 941.0896 H37C58N14O10S2 DEFGIKLMNQTVWY ACHPRS 8.08164386749267 2 0 0.827463822345868 5 4 -0.344444444444444 0.787 1.2 hours 1 hours 1.1 hours 22.22 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02399 KKKKLLLPTLFLF 13 P184 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1198.4619 H52C96N19O12S0 CDEFGHMNPTWY AIKLQRSV 11.9999677658081 4 0 3.79385658605608 6 4 -0.679999999999999 1.357 4.4 hours 20 hours 10 hours 117 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02400 KKKKVVALTYVLV 13 P59 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1706.0184 H75C125N22O20S1 EFHIMPSTVW ACDGKLNQRY 9.1960443496704 3 1 1.74831438213313 7 8 -0.213333333333333 1.123 1.3 hours 1.1 hours 1.2 hours 117.33 1490 0.873378622411107 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02401 KKKKLLLPFLVFF 13 P160 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1144.3266 H49C71N15O12S2 DEFGHILMPQSV ACKNRTWY 8.90322895050048 2 0 1.73829163209328 4 5 -0.888888888888888 1.338 1.2 hours 1 hours 1.1 hours 11.11 6990 6.10839597716246 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02402 AKDEMEECASHLPYEA 16 P192 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1050.2153 H43C65N15O11S2 DEGIKMPQTVWY ACFHLNRS 8.08164386749267 2 0 0.827463822345868 4 5 0.155555555555555 0.992 1.2 hours 1 hours 1.1 hours 54.44 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02403 FDEMEECSQHLPYA 14 P195 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1575.9795 H74C132N20O16S0 CDEFGHIMNPQRSW AKLTVY 10.3983152389526 6 0 5.75310860719629 7 7 -0.557142857142857 1.411 1.3 hours 1.1 hours 1.2 hours 90.71 1490 0.945443770049039 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02404 KKKKVVAATYKLKA 14 P36 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1629.08139999999 H86C131N17O13S0 CDEGHIMNPQRSTWY AFKLV 10.4777402877807 4 0 3.75610561019329 4 9 1 1.357 1.3 hours 1.1 hours 1.2 hours 120 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02405 KKKKLVAATYVLV 13 P56 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 906.081899999999 H36C61N11O11S2 DEFHIMQRSVWY ACGKLNPT 8.05837078094482 1 0 0.739300632992282 5 4 0.0555555555555555 0.687 1.2 hours 1 hours 1.1 hours 54.44 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02406 KKKKVLLAFLFFF 13 P171 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3130.67449999999 H135C216N45O34S3 AEHLTY CDFGIKMNPQRSVW 10.8600378036499 6 1 4.73938239333312 17 9 -0.919230769230769 1.178 1.2 hours 1 hours 1.1 hours 52.31 5500 1.75680991428524 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02407 DEMEEC 8 P193 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1682.0632 H75C138N24O18S0 ACDEFHMNPQTWY GIKLRSV 11.9999677658081 4 0 3.75808361239129 9 7 0.64375 0.794 1.3 hours 1.1 hours 1.2 hours 151.87 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02408 DEVVCC 8 P199 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 932.0397 H34C55N15O11S2 DEFIKLMPQSVWY ACGHNRT 8.08164386749267 2 0 0.827463822345868 5 4 -0.411111111111111 0.826 1.2 hours 1 hours 1.1 hours 22.22 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02409 KKKKVLLPFLFFV 13 P118 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 4283.8155 H192C292N51O57S1 ACDHPRS EFGIKLMNQTVWY 6.28834781646728 4 4 -0.234650543911861 22 13 -1.00285714285714 1.311 5.5 hours 10 hours 6 hours 83.43 8480 1.9795437035045 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02410 KKKKVVAATYVTV 13 P95 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 966.1784 H42C65N11O10S2 DEGHIMQRSTVWY ACFKLNP 8.05837078094482 1 0 0.739300632992282 3 6 0.688888888888888 0.814 1.2 hours 1 hours 1.1 hours 65.56 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02411 KKKKVVAAKYVLV 13 P85 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1667.85599999999 H76C116N18O23S0 CDHLMPQRSW AEFGIKNTVY 4.53139781951904 1 2 -1.23627546386227 7 8 0.233333333333333 0.886 1.4 hours 1.2 hours 1.3 hours 104 1490 0.893362496522482 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02412 KKKKVVAATYVFVA 14 P32 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1528.6843 H74C91N15O18S1 CEGHIKLNQRVY ADFMPSTW 4.05002841949462 0 1 -1.23877762487085 6 6 -0.35 1.009 2.8 hours 2.5 hours 2.6 hours 8.33 16500 10.7935955121669 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02413 DDDEVVAATYVA 12 P16 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2118.3022 H88C150N26O33S0 CFGHIMPQRWY ADEKLNSTV 6.25651798248291 4 4 -0.200258970315807 13 7 -0.975 1.097 4.4 hours 20 hours 10 hours 68.5 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02414 AKLEVVAATYVKKK 14 P40 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1486.88289999999 H72C125N17O15S0 CDEFGHIMNQRSW AKLPTVY 10.1768663406372 4 0 3.75510660919429 6 7 0.215384615384615 1.146 1.3 hours 1.1 hours 1.2 hours 134.62 1490 1.00209639911791 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02415 KKKKLVAPTYVLV 13 P127 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1048.3072 H41C71N15O10S3 ADEFLNPQSVWY CGHIKMRT 8.95718898773193 3 0 1.82646482134686 5 4 -0.144444444444444 1.047 1.2 hours 1 hours 1.1 hours 43.33 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02416 KKKKVVAPTYVLV 13 P110 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1011.0917 H36C59N14O15S2 DFGHIKLMPVWY ACENQRST 5.988010597229 1 1 -0.256899903935508 6 3 -1.07777777777777 0.964 1.2 hours 1 hours 1.1 hours 11.11 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02417 KKKKLLLPFYVFF 13 P168 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 991.143399999999 H39C64N12O13S2 DFGIMNPQRVWY ACEHKLST 6.73078250885009 2 1 -0.17071471677992 5 4 -0.166666666666666 0.997 1.2 hours 1 hours 1.1 hours 54.44 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02418 ADKEVVAATYVKKK 14 P43 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3715.125 H158C266N45O56S0 CFHMPRWY ADEGIKLNQSTV 6.06900615692138 2 2 -0.237965164895644 22 13 -0.131428571428571 0.749 20 hours 15 hours 18 hours 111.43 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02419 KKKKLLLPFLFLV 13 P117 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3740.22419999999 H160C276N48O53S0 CFGHMPWY ADEIKLNQRSTV 8.40172939300537 6 5 0.740645293958466 19 16 -0.234285714285714 0.96 100 hours 60 hours 90 hours 103.43 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02420 KKKKVVAATYTLV 13 P94 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 728.8836 H29C46N10O7S2 ADEFHILMNPQSTVW CGKRY 8.90322895050048 2 0 1.73829163209328 3 3 -0.85 1.3 1.2 hours 1 hours 1.1 hours 0 1490 2.04422215014853 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02421 KKKKVVAATYVLP 13 P114 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1475.8603 H70C124N18O15S0 CDEFGHIMNPQRSW AKLTVY 10.3015481948852 5 0 4.75410760819529 6 7 -0.115384615384615 1.297 1.3 hours 1.1 hours 1.2 hours 112.31 1490 1.00958064933382 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02422 KKKKVVEATYVLV 13 P74 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3435.8778 H149C252N42O49S0 CFHMPTWY ADEGIKLNQRSV 4.65678462982177 4 6 -2.25553524316932 18 12 -0.416666666666666 1.13 100 hours 60 hours 90 hours 136.33 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02423 KKKKLLAATYVLV 13 P125 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1138.3617 H52C72N13O11S2 ADEGHIMRSTVY CFKLNPQW 8.05837078094482 1 0 0.739300632992282 4 5 -0.2 1.257 1.2 hours 1 hours 1.1 hours 43.33 5500 4.8315047844635 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02424 SEDVVSSSMSYTFT 14 P198 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1687.9007 H72C120N26O20S0 CFMNPQSVWY ADEGHIKLRT 8.80207805633545 5 2 0.973135186477312 9 6 -0.66 1.195 4.4 hours 20 hours 10 hours 98 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02425 KKKKVVAATYVLK 13 P88 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1603.8169 H85C100N16O15S0 ACDEGIKMNQRSV FHLPTWY 6.40100269317627 1 0 -0.516627219376787 6 6 -0.675 1.217 7.2 hours 6 hours 6.5 hours 32.5 13980 8.7167057536306 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02426 KKKKVVAATKVLV 13 P86 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3125.7888 H141C223N46O28S3 DEHNY ACFGIKLMPQRSTVW 11.8403440475463 8 0 7.73725263149427 13 12 -0.576 1.351 1.1 hours 30.0 minutes 54.0 minutes 50.8 11000 3.51911171989611 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02427 EDCSTPSSGSFLDR 14 P187 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 948.1185 H38C63N11O12S2 ADEFGKMNPQRTWY CHILSV 6.72305240631103 1 0 -0.17252617775413 4 5 1.32222222222222 0.498 1.2 hours 1 hours 1.1 hours 118.89 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02428 DDSVVSAAMSYSHA 14 P6 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1050.1723 H42C60N15O12S2 ADEFIKLMNTVW CGHPQRSY 8.06784763336181 2 0 0.826464821346867 6 3 -1.14444444444444 1.058 1.2 hours 1 hours 1.1 hours 0 1490 1.41881479829548 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02429 KKKKVVAATLFLV 13 P149 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1078.2669 H42C71N15O13S2 ADEFGHIKMPSVWY CLNQRT 8.07210254669189 1 0 0.740289634091281 5 4 -0.344444444444444 1.01 1.2 hours 1 hours 1.1 hours 86.67 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02430 KKKKVVAAFYVFV 13 P147 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1526.905 C77H97N17O2 CDEGHILMNPQRSTW AFKVY 10.177 4 0 3.755 1 9 0.7 1.122 1.3 hours 1.1 hours 1.2 hours 104.615 1490 1.14615384615385 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02431 KKKKVLLPFLLFF 13 P173 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 384.4738 H17C30N6O3S0 ACDEFGHIKMNQSTVWY LPR 9.75002117156982 1 0 0.760091614289301 2 1 -0.766666666666666 1.19 5.5 hours 10 hours 6 hours 130 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02432 ADLKVVAATYVLVA 14 P46 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1960.1584 H82C131N30O25S0 ACGHIMNPTVWY DEFKLQRS 10.7372900009155 4 2 1.76300383640335 12 3 -2.15333333333333 1.611 1.0 hours 1 hours 1 hours 52 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02433 KKKKVVAATYVLE 13 P80 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1020.2689 H46C71N11O10S2 ADEFHIMNQRSVY CGKLPTW 8.05837078094482 1 0 0.739300632992282 4 5 0.566666666666666 0.894 1.2 hours 1 hours 1.1 hours 86.67 5500 5.39073571682916 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02434 FDEMEECASHLPYA 14 P196 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1535.6523 H63C106N18O25S0 CDEFGHKMPRWY AILNQSTV 5.24000949859619 0 0 -0.539853540782401 10 5 0.146666666666666 0.47 1.9 hours 2 hours 1.8 hours 104 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02435 KKKKVVAATYFFV 13 P152 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1442.65839999999 H66C105N17O18S0 CEFHIMNQRSVWY ADGKLPT 9.00624942779541 2 1 0.957651626520198 12 3 -1 0.706 20 hours 15 hours 18 hours 39.33 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02436 KKKKVLAATLVLV 13 P134 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1535.8093 H74C104N18O15S1 ACDEFHKNPQVY GILMRSTW 9.50007724761963 1 0 0.500344687641343 5 7 0.341666666666666 1.082 30 hours 18 hours 25 hours 97.5 16500 10.7435213473444 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02437 KKKKLLLPFLFFV 13 P115 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1713.97739999999 H74C114N22O20S2 FKPQSTY ACDEGHILMNRVW 5.50811901092529 2 2 -1.15346668487457 6 9 0.346666666666666 0.953 3.5 hours 4 hours 3 hours 104 5500 3.20891045587882 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02438 KKKKVVAPTYVFV 13 P143 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1359.55299999999 H59C91N18O16S1 ACDEFHILNTY GKMPQRSVW 11.0001920700073 2 0 1.45913745831859 9 3 -1.05833333333333 0.958 1.9 hours 2 hours 1.8 hours 24.17 5500 4.04544729039618 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02439 KKKKVVTSTYVLVEA 15 P188 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Not Available Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 955.073 H37C56N14O11S2 DEFGKLMPQRTVWY ACHINS 6.89834384918212 2 0 -0.0853519894995431 4 5 0.266666666666666 0.832 1.2 hours 1 hours 1.1 hours 65.56 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02440 KKKKLLLPFLVFV 13 P124 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1887.1425 H78C129N23O26S2 FGKMPQSWY ACDEHILNRTV 4.53645648956298 2 3 -2.16748419380123 8 9 0.329411764705882 0.829 1.1 hours 1 hours 1 hours 120.59 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02441 KKKKVVAATYPLV 13 P112 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3048.2742 H129C206N37O47S0 CGHKMPTWY ADEFILNQRSV 4.05002841949462 1 4 -3.23204593988458 16 12 -0.0821428571428571 0.799 1.4 hours 1.2 hours 1.3 hours 111.43 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02442 FDEMEESSSHLPYI 14 P191 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1175.2035 H47C76N14O20S0 CDEFGIKLMNQRWY AHPSTV 6.45642070770263 1 0 -0.452679352527814 10 2 -0.399999999999999 0.342 1.9 hours 2 hours 1.8 hours 32.5 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02443 KKKKGVAATYVLV 13 P97 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1870.0572 H78C122N28O23S1 CEGHKLPQSTVW ADFIMNRY 8.74083309173584 4 3 0.762424896409831 8 7 -1.24666666666666 1.278 1.1 hours 1 hours 1 hours 46 1490 0.79676707215159 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02444 KKKKVVAATYVLKK 14 P28 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1651.8319 H72C112N16O25S1 CGHKQRTVWY ADEFILMNPS 4.05002841949462 0 3 -3.23484640195779 8 7 0.339999999999999 0.669 20 hours 15 hours 18 hours 110.67 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02445 KKKKVVAATYKKKA 14 P35 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2273.5893 H96C169N31O31S0 CDFHLMNPWY AEGIKQRSTV 10.2779527664184 5 2 2.73659231110456 15 5 -0.975 1.121 100 hours 60 hours 90 hours 73 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02446 AESTTPCSGSYLKA 14 P186 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2099.65139999999 H98C177N29O20S0 CDEFGHIMNQSTWY AKLPRV 11.9999677658081 5 0 4.75708461139229 7 13 0.715 0.919 1.0 hours 1 hours 1 hours 156.5 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02447 AKLEVVAATYKKKK 14 P41 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 965.1458 H39C65N10O13S2 ADEFGHIKMNRVWY CLPQST 5.51141567230224 0 0 -0.259700366008717 5 4 0.588888888888888 0.49 1.2 hours 1 hours 1.1 hours 86.67 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02448 KKKKVVAATYGLV 13 P103 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 955.1161 H38C60N14O10S2 ADEFIKLMNQTWY CGHPRSV 8.08164386749267 2 0 0.827463822345868 6 3 -0.322222222222222 0.758 1.2 hours 1 hours 1.1 hours 32.22 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02449 KKKKVLAATYFLV 13 P135 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1025.1183 H37C61N14O15S2 DFGHIKLMPSVWY ACENQRT 5.988010597229 1 1 -0.256899903935508 6 3 -1.06666666666666 0.966 1.2 hours 1 hours 1.1 hours 11.11 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02450 KKKKVLLATYVLV 13 P131 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 3379.84239999999 H152C221N40O41S3 MST ACDEFGHIKLNPQRVWY 5.56575374603271 4 4 -1.20013737042405 17 13 -0.313333333333333 1.007 100 hours 60 hours 90 hours 65 6990 2.06814376907042 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02451 KKKKVEAATYVLV 13 P73 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 989.1672 H41C65N10O13S2 AEFGHKMNRSVWY CDILPQT 4.05002841949462 0 1 -1.25857960506887 5 4 0.266666666666666 0.619 1.2 hours 1 hours 1.1 hours 86.67 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02452 KKKKVGAATYVLV 13 P98 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2100.5931 H97C172N28O22S0 CDFGHIMNQSTWY AEKLPRV 11.0003854751586 4 1 2.7608940743645 7 13 0.735 0.88 1.0 hours 1 hours 1 hours 156.5 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02453 KKKKVVAATYALV 13 P53 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 971.0643 H36C60N10O16S2 ADFGHKLMPQRVWY CEINST 4.05002841949462 0 1 -1.2568899040355 6 3 -0.0444444444444444 0.548 1.2 hours 1 hours 1.1 hours 43.33 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02454 KKKKVVAATPVLV 13 P111 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1058.1877 H46C60N11O13S2 DEFGHIKLMNRV ACPQSTWY 5.51073360443115 0 0 -0.260699367007718 4 5 -0.222222222222222 0.849 1.2 hours 1 hours 1.1 hours 11.11 6990 6.60563338621305 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02455 KKKKVLAAFYVLV 13 P133 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 989.1936 H41C74N14O11S1 CDEFHINPQTVWY AGKLMRS 11.0008367538452 2 0 1.7590926132903 6 4 0.0899999999999999 0.726 30 hours 15 hours 28 hours 88 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02456 KKKKVVAAPYVLV 13 P109 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1012.0779 H39C55N13O14S2 ADEFIKLMPQRSVW CGHNTY 6.72219982147216 1 0 -0.173525178753131 6 3 -0.922222222222222 0.834 1.2 hours 1 hours 1.1 hours 0 1490 1.47221868988543 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02457 KKKKVLAATYVFV 13 P136 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2160.6216 H88C148N36O19S4 ADEHIKMNPQSTW CFGLRVY 10.6632158279418 6 0 5.71943865339425 9 9 -0.25 1.137 1.0 hours 1 hours 1 hours 53.89 1490 0.689616358551632 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02458 KKKKVVAATLVFV 13 P150 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1671.1181 H88C133N17O14S0 ACDEGHIMNQRSTW FKLPVY 10.1768663406372 4 0 3.75510660919429 5 8 0.423076923076923 1.415 1.3 hours 1.1 hours 1.2 hours 112.31 1490 0.891618611515248 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02459 KKKKVLLPFLFVF 13 P174 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1574.9913 H75C133N19O16S0 CDEFGHIMNPQRSW AKLTVY 10.3015481948852 5 0 4.75410760819529 6 8 0.192857142857142 1.209 1.3 hours 1.1 hours 1.2 hours 125 1490 0.946036971759781 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02460 KKKKVVAATYVKV 13 P87 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2717.09179999999 H101C160N34O37S8 DFKMPQVW ACEGHILNRSTY 6.68417453765869 2 1 -0.230130657273981 12 14 0.246153846153846 0.675 1.2 hours 1 hours 1.1 hours 41.54 1490 0.548380441176113 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02461 KKKKLLLPFYFFV 13 P123 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 550.6476 H26C40N6O6S0 CDEGHILMNPQRTWY AFKSV 8.72000980377197 1 0 0.732989388956151 2 3 0.82 0.86 100 hours 60 hours 90 hours 78 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02462 KKKKVVAATYVLVK 14 P29 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1454.5696 H61C89N21O18S1 EFGKLMPQSVY ACDHINRTW 6.95001049041748 3 1 -0.0385672646959054 8 4 -1.00833333333333 1.142 4.4 hours 20 hours 10 hours 40.83 5500 3.78118723229194 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02463 KKKKVVLATYVLF 13 P139 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1500.8978 H63C110N21O14S3 CDEFGKNPSVWY AHILMQRT 11.9999677658081 3 0 1.84725580264388 5 7 0.324999999999999 0.992 3.5 hours 4 hours 3 hours 105.83 0 0 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02464 KKKKVVAATYELV 13 P78 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1124.3351 H51C71N13O11S2 ADEGIMQRSTVW CFHKLNPY 8.054953956604 2 0 0.825475820247868 4 5 -0.211111111111111 1.214 1.2 hours 1 hours 1.1 hours 43.33 1490 1.32522768345487 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02465 KKKKVVLPTYVLV 13 P137 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 1514.936 C74H105N17O3 ACDEFGHIMNQRSW KLPTVY 10.177 4 0 3.755 2 7 0.4 1.228 1.3 hours 1.1 hours 1.2 hours 149.231 1490 1.14615384615385 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02466 KKKKVVAATYVEV 13 P79 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2717.0355 H119C195N32O39S0 CEFHIMPY ADGKLNQRSTVW 4.42897396087646 2 3 -1.23754510389016 14 11 0.123999999999999 0.77 1.0 hours 1 hours 1 hours 124.8 5500 2.02426504916848 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02467 KKKKKVAATYVLV 13 P81 Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) P26662 Experimentally Validated 11116 Not Available Not Available Not Available Not Available Not Available Genomic RNA Not Available 1DXP##1DY8 HCV Flaviviridae Fluorescent probe [Ref:14694985]HCV:IC50=inhibition of activation of NS3-6K protease(50 nM)(0.1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS3 protease "HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication" 2867.08929999999 H117C186N36O43S2 AFHMQY CDEGIKLNPRSTVW 4.65110073089599 3 5 -2.24686555740109 18 7 -1.052 1.052 1.4 hours 1.2 hours 1.3 hours 58.4 5500 1.9183218325289 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. "Portal-Nunez S, Gonzalez-Navarro CJ, Garcia-Delgado M, Vizmanos JL, Lasarte JJ, Borras-Cuesta F." Peptide inhibitors of hepatitis C virus NS3 protease. 10.1177/095632020301400501 10.1177/095632020301400501 Anti-HCV DRAVPe02468 PVPFEEVIDKINAKG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 987.1546 H40C64N12O12S2 ACHLMQSTWY PV 8.05824184417724 1 0 0.73929063309228 3 6 0.566666666666666 0.684 7.2 hour >20 hours >10 hours 65.56 1490 1.50938870162789 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02469 DYTEVQRRNQLHDLR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1046.22509999999 H41C69N15O12S2 ABCGIKMNPW DY 8.08164386749267 2 0 0.827463822345868 5 4 0.0666666666666666 0.898 7.2 hour >20 hours >10 hours 86.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02470 LEVYTRHEIKDSGLL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2261.57339999999 H100C166N27O31S0 ABCFJMPQWXZ LE 6.25532436370849 4 4 -0.233353241848225 12 8 -0.46 1.183 7.2 hour >20 hours >10 hours 102.5 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02471 AKYVRNNLETTAFHR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1010.1448 H42C60N11O13S2 BCDGIMPSW AK 5.51073360443115 0 0 -0.260699367007718 5 4 -0.344444444444444 0.708 7.2 hour >20 hours >10 hours 32.22 1490 1.47503605423698 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02472 GYVYFEEYAYSHQLS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1772.9951 H79C127N21O24S0 BCDIMPNTW GY 5.44542560577392 3 3 -1.14799051456784 9 6 -0.346666666666666 1.127 7.2 hour >20 hours >10 hours 123.33 1490 0.840385853294236 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02473 VAADNVIVQNSMRIS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2330.7628 H110C177N26O28S0 BCGHJKLPWXY VA 6.75113086700439 3 2 -0.150790976641057 11 9 0.214999999999999 1.014 7.2 hour >20 hours >10 hours 151 5500 2.359742484306 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02474 GTPGVAAATQAANGG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1926.1403 H83C132N28O24S0 BCDEFHIKLMRSVWY GT 10.834314918518 3 1 1.39829835450746 14 4 -0.927777777777777 0.903 7.2 hour >20 hours >10 hours 53.89 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02475 GATVVQFEQPRRCPT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2925.5476 H116C199N40O33S7 BDHIKLMNSVWY GA 8.96073474884033 6 1 3.78696262109167 15 11 -0.173076923076923 0.916 7.2 hour >20 hours >10 hours 52.31 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02476 KNPTPPRPAGDNATV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1890.9618 H88C107N23O24S0 BCEFHIJKLMQSWY KN 4.37025928497314 1 2 -1.23597716279764 10 5 -1.18666666666666 1.29 7.2 hour >20 hours >10 hours 0 11000 5.81714553937578 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02477 RVDLGDCIGKDARDA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 804.0131 H34C63N11O8S1 BEFHIJKMNPQSTW RV 11.0001920700073 2 0 1.45913745831859 4 3 -0.0142857142857143 1.01 7.2 hour >20 hours >10 hours 111.43 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02478 EARKLNPNAIASVTV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1603.7561 H64C108N22O23S1 BCDFGHJMOQWXY EA 4.57755107879638 3 4 -1.24633533294933 9 6 -0.606666666666666 0.97 7.2 hour >20 hours >10 hours 84.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02479 TRNLLTTPKFTVAWD 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3689.1206 H166C249N47O46S1 BCEGHIJMNQSY TR 9.9888765335083 5 1 2.84606026072109 18 13 -0.693548387096774 1.034 7.2 hour >20 hours >10 hours 60 15470 4.1934112969904 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02480 GTTVNCIVEEVDARS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1017.2037 H40C61N12O12S3 BCFHJLMOPQWXY GT 5.07619953155517 1 1 -1.17140541681428 4 5 0.0777777777777777 0.847 7.2 hour >20 hours >10 hours 54.44 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02481 ANFYVCPPPTGATVV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1620.9124 H66C111N19O21S3 BEHIJKLQRSWXY AN 4.37020244598388 1 2 -1.26568013309467 6 9 0.593333333333333 0.762 7.2 hour >20 hours >10 hours 117.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02482 RADITTVSTFIDLNI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 891.0705 H35C60N12O10S2 BEGHJKMOQSWXY RA 8.07210254669189 1 0 0.740289634091281 5 4 0.588888888888888 0.512 7.2 hour >20 hours >10 hours 75.56 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02483 DARDAMDRIFARRYN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4494.8813 H192C311N56O67S0 BEGHJKLMPQSTW DA 4.64734935760498 5 7 -3.1428167707741 27 14 -0.539024390243902 0.953 7.2 hour >20 hours >10 hours 99.76 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02484 SQVWFGHRYSQFMGI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1763.0019 H81C125N21O22S0 ABCDJKLNTW SQ 8.40933666229248 2 1 0.401489256014774 9 6 -0.286666666666666 0.935 7.2 hour >20 hours >10 hours 78 5500 3.11967899750987 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02485 FSSDAISTTFTTNLT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1678.8805 H74C121N19O24S0 BCGHJKMPQWXY FS 4.20781345367431 1 2 -1.237666863831 8 7 0.546666666666666 0.644 7.2 hour >20 hours >10 hours 130 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02486 EEYAYSHQLSRADIT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 6726.7578 H294C457N91O78S6 BCFGJKMNOPVW EE 9.89262523651122 10 0 8.78180585655581 41 22 -0.384126984126984 0.787 7.2 hour >20 hours >10 hours 50.95 5960 0.886013764313025 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02487 EQSRKPPNPTPPPPG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1727.0788 H79C129N21O19S1 BCDGHIJLMVWXY EQ 8.49778728485107 1 0 0.499345686642342 7 11 1.03333333333333 0.461 7.2 hour >20 hours >10 hours 125 1490 0.862728440647873 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02488 PANAATRTSRGWHTT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1605.6974 H70C106N16O26S0 BCDEFIKLMNQSVY PA 4.05002841949462 0 1 -1.23877762487085 10 5 0.186666666666666 0.457 7.2 hour >20 hours >10 hours 58.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02489 AFHRYGTTVNCIVEE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Random coil Linear Free Free None L Virus entry His6‐HR1 and GST‐removed‐HR2 were tested for their entry inhibition activity. 1023.2264 H45C67N10O12S2 BCDJKLMPQS AF 5.51073360443115 0 0 -0.260699367007718 4 5 0.5 0.66 7.2 hour >20 hours >10 hours 86.67 1490 1.45617822214126 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02490 CYSRPLVSFRYEDQG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4027.3706 H173C273N53O57S0 ABHIKMNTW CY 6.50342655181884 7 6 -0.443211986551289 25 9 -1.37058823529411 1.326 7.2 hour >20 hours >10 hours 71.76 11000 2.73131059753974 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02491 DNATVAAGHATLREH 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 861.0644 H36C66N12O9S1 BCFIJKMOPQS DN 11.0001920700073 2 0 1.45913745831859 5 3 -0.0625 0.885 7.2 hour >20 hours >10 hours 97.5 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02492 HEFVPLEVYTRHEIK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1444.80319999999 H69C119N17O15S0 ABCDGJMNOPQS HE 10.1768663406372 4 0 3.75510660919429 6 7 0.0615384615384615 1.116 7.2 hour >20 hours >10 hours 112.31 1490 1.03128232274126 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02493 PPPPGASANASVERI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1912.25259999999 H87C124N30O15S2 BCDFHIKLMNTW PP 10.4131429672241 6 0 3.00179219905504 7 8 -0.0733333333333333 1.309 7.2 hour >20 hours >10 hours 45.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02494 DVMAVSTCVPVAADN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1121.3279 H53C70N10O12S2 BEFGHIJKLMPQW DV 8.03290576934814 1 0 0.73730263099428 4 5 -0.288888888888889 1.001 7.2 hour >20 hours >10 hours 0 2980 2.65756341209382 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02495 ARMLGDVMAVSTCVP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4755.63009999999 H220C356N60O54S1 BEFHIKNPQSTW AR 9.36978664398193 7 3 2.12936963831014 24 18 0.13095238095238 0.883 7.2 hour >20 hours >10 hours 122.86 1490 0.313312845757285 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02496 INAKGVCRSTAKYVR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1573.0597 H81C135N17O13S0 BCDEFHJLMPQSW IN 10.4777402877807 4 0 3.75610561019329 5 8 0.923076923076923 1.253 7.2 hour >20 hours >10 hours 164.62 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02497 AAPTGDPKPKKNKKP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2534.9282 H117C177N30O30S1 BCDEFHIJLQRSTUVW AA 8.58991260528564 2 1 0.76090407426451 11 9 -0.485 1.154 7.2 hour >20 hours >10 hours 97.5 12490 4.92716125056323 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02498 IAWCELQNHELTLWN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4027.3706 H173C273N53O57S0 BCDFGHJKMOPRSTV IA 6.77574214935302 7 6 -0.143256831579585 25 9 -1.37058823529411 1.326 7.2 hour >20 hours >10 hours 71.76 11000 2.73131059753974 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02499 LQFTYNHIQRHVNDM 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1665.95789999999 H71C122N24O19S1 ABCEGJKLOPSTUW LQ 10.3068346023559 4 0 3.74718362129328 8 7 -0.299999999999999 1.003 7.2 hour >20 hours >10 hours 78 1490 0.894380344185168 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02500 HVNDMLGRVAIAWCE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3990.5805 H174C294N48O55S1 BCDFJKLOPQSTY HV 8.88872356414795 7 5 1.4529263689259 22 13 -0.777142857142857 1.217 7.2 hour >20 hours >10 hours 100.29 1490 0.373379261488398 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02501 LRSEYGGSFRFSSDA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3990.5805 H174C294N48O55S1 ABCEHIJKMNOPQTUVW LR 8.90368022918701 7 5 1.7528815238976 22 13 -0.777142857142857 1.217 7.2 hour >20 hours >10 hours 100.29 1490 0.373379261488398 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02502 FEDRAPVPFEEVIDK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1267.5009 H48C96N32O8S0 BCGHJLMNQSTW FE 11.9999677658081 8 0 7.76002161498929 8 0 -4.5 2.56 7.2 hour >20 hours >10 hours 0 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02503 AENTDANFYVCPPPT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1041.2517 H44C81N18O10S0 BCGHIKLMQRSTW AE 11.9999677658081 3 0 2.76007161448929 5 3 -0.7375 1.328 7.2 hour >20 hours >10 hours 133.75 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02504 IAVVFKENIAPYKFK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1621.1025 H85C135N17O13S0 BCDGHJLMNQRSTVW IA 10.4777402877807 4 0 3.75610561019329 5 8 0.815384615384615 1.335 7.2 hour >20 hours >10 hours 142.31 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02505 PPPLGAAPTGDPKPK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2779.43259999999 H129C222N34O30S1 BCDEFHIJKLNOQRSUVW PP 10.4778692245483 4 0 3.79187858385808 8 19 1.0037037037037 0.811 7.2 hour >20 hours >10 hours 148.52 5500 1.97882114500636 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02506 RRCPTRPEGQNYTEG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1513.4299 H60C86N16O29S0 ABCDHIJKLMOSVW RR 4.05002841949462 0 4 -4.23054473941065 12 3 -0.953333333333333 0.632 7.2 hour >20 hours >10 hours 26 5500 3.63412933760592 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02507 KENIAPYKFKATMYY 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1071.1864 H46C60N12O13S2 BCDGHIJLMNOPQRSVWX KE 6.72219982147216 1 0 -0.173525178753131 5 4 -0.366666666666666 0.871 7.2 hour >20 hours >10 hours 0 1490 1.39098106548029 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02508 LGRVAIAWCELQNHE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3798.2204 H160C273N50O55S0 BCDFJKMNOPSTUV LG 8.47322483062744 6 5 0.802531491857401 22 13 -0.605714285714285 1.026 7.2 hour >20 hours >10 hours 94.86 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02509 MTKWQEVDEMLRSEY 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1126.3098 H46C73N15O13S2 ABCDFGIJKLNOPU MT 8.05843524932861 2 1 0.74209109516549 5 4 -0.822222222222222 1.19 7.2 hour >20 hours >10 hours 43.33 1490 1.32290423114493 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02510 IEFARLQFTYNHIQR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1509.6827 H71C93N16O18S1 ABCDGKJLMNOPSTUVW IE 4.05002841949462 0 1 -1.49683485048544 5 7 -0.216666666666666 1.127 7.2 hour >20 hours >10 hours 49.17 16500 10.9294489497694 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02511 EVIDKINAKGVCRST 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1117.3228 H44C69N14O13S3 BCDFHJLMPQOQSWY EV 8.04547710418701 2 1 0.74110209406649 5 4 -1.13333333333333 1.32 7.2 hour >20 hours >10 hours 0 1490 1.33354479117405 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02512 QVDGFYARDLTTKAR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 956.052899999999 H35C58N11O15S2 BCEHIJKLMPNSUW QV 5.51141567230224 0 0 -0.259700366008717 6 3 -0.133333333333333 0.529 7.2 hour >20 hours >10 hours 43.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02513 AAATQAANGGPATPA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1199.4234 H51C88N16O14S1 BCDEFIJKLNOQRSVWY AA 8.79266567230224 2 1 0.795986347894929 6 6 0.0499999999999999 0.762 7.2 hour >20 hours >10 hours 90 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02514 NNLETTAFHRDDHET 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1632.88009999999 H68C119N21O22S1 BCGIJKLMPQSVWXY NN 8.29400272369385 3 2 0.826039387640825 9 6 -0.199999999999999 0.951 7.2 hour >20 hours >10 hours 97.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02515 ISTTFTTNLTEYPLS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2976.27989999999 H129C200N37O41S1 ABCGHJLMOQRVWXY IS 7.17372875213623 2 1 0.0468138168727858 25 4 -1.08965517241379 0.592 7.2 hour >20 hours >10 hours 30.34 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02516 FADIDTVIHADANAA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1432.7029 H67C111N15O18S0 BCEGJKLMNOPQRSVWY FA 5.87944812774658 1 1 -0.20500265320407 3 11 1.58571428571428 0.561 7.2 hour >20 hours >10 hours 167.14 1490 1.03999231103671 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02517 MDRIFARRYNATHIK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2202.4616 H94C162N26O33S0 BCEGJLOPQSVW MD 6.25651798248291 4 4 -0.200258970315807 13 7 -0.775 1.136 7.2 hour >20 hours >10 hours 97.5 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02518 KDVTVSQVWFGHRYS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1808.989 C83H91N23O8 ABCEGIJLMNOPUW KD 8.597 3 1 0.846 6 6 -0.54 0.77 7.2 hour >20 hours >10 hours 58 6990 4.66 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02519 HTTYAADRFKQVDGF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1032.1719 H40C59N11O14S3 BCEIJLMNOPSWY HT 5.51073360443115 0 0 -0.260699367007718 5 4 -0.5 0.673 7.2 hour >20 hours >10 hours 0 1490 1.44355799649264 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02520 VYPYDEFVLATGDFV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1738.9638 H76C116N23O21S1 ABCHIJLMNOPQRSW VY 5.55154399871826 2 2 -1.15177698384121 7 8 -0.04 1.116 7.2 hour >20 hours >10 hours 110.67 5500 3.16280304397366 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02521 VIVQNSMRISSRPGA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3241.8576 H148C240N46O33S1 BCDEHKLOPQTUWY VI 10.6994470596313 6 1 3.12474771536272 17 11 -0.314285714285714 1.015 7.2 hour >20 hours >10 hours 121.79 1490 0.459613031738347 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02522 EVDEMLRSEYGGSFR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1026.194 H41C65N15O11S2 ABCDHIJKLNOPQTW EV 8.08164386749267 2 0 0.827463822345868 6 3 -0.711111111111111 0.948 7.2 hour >20 hours >10 hours 43.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02523 ARRYNATHIKVGQPQ 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1444.8462 H70C123N17O14S0 BCDEFJLMNOSTW AR 10.4777402877807 4 0 3.75610561019329 5 8 0.792307692307692 1.088 7.2 hour >20 hours >10 hours 142.31 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02524 EFVLATGDFVYMSPF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2609.9256 H113C191N31O38S0 BCDHIJKLNOPQRSW EF 4.83332653045654 3 4 -2.14418105159563 14 10 0.154166666666666 0.833 7.2 hour >20 hours >10 hours 130 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02525 GWHTTDLKYNPSRVE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1727.98929999999 H68C111N26O20S3 ABCDFIJKLMPQTUXY GW 8.09079837799072 4 1 0.915748771640299 8 7 -0.313333333333333 0.992 7.2 hour >20 hours >10 hours 58.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02526 VGQPQYYQANGGFLI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1111.3152 H42C84N28O7S0 BCDEHJKLMNOPRSTW VG 11.9999677658081 7 0 6.76003161488929 7 0 -4.5 2.56 7.2 hour >20 hours >10 hours 0 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02527 TMLEDHEFVPLEVYT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1722.95249999999 H83C113N15O22S1 BCDFGIJKLNOQRSW TM 4.05002841949462 0 2 -2.16305062136116 6 9 0.833333333333333 0.687 7.2 hour >20 hours >10 hours 71.33 1490 0.864794589520025 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02528 ATAPTTRNLLTTPKF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1072.2855 H42C66N15O11S3 BCDEGIJKMNOQRSVWY AT 8.07719554901122 3 0 0.913649009501456 5 4 -0.388888888888888 1.171 7.2 hour >20 hours >10 hours 32.22 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02529 DSGLLDYTEVQRRNQ 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1034.0852 H37C55N15O15S2 ABCFHIJKLMPOTUVW DS 6.72305240631103 1 0 -0.17252617775413 7 2 -1.52222222222222 1.011 7.2 hour >20 hours >10 hours 0 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02530 SVERIKTTSSIEFAR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1475.8603 H70C124N18O15S0 BCDGHJLMNOPQTW SV 10.3015481948852 5 0 4.75410760819529 6 7 -0.115384615384615 1.297 7.2 hour >20 hours >10 hours 112.31 1490 1.00958064933382 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02531 GRRVSARMLGDVMAV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 945.028399999999 H37C53N10O14S2 BCEHIJKLNPQSTUW GR 4.05002841949462 0 1 -1.25957860606787 4 5 0.166666666666666 0.628 7.2 hour >20 hours >10 hours 43.33 1490 1.57667219313197 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02532 AAGHATLREHLRDIK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1071.2777 H43C72N16O11S2 BCDEFIJKMNOPQSVW AA 8.95718898773193 3 0 1.82646482134686 6 3 -0.955555555555555 1.21 7.2 hour >20 hours >10 hours 43.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02533 LSNTLAELYVREHLR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2152.3314 H92C127N30O26S2 BCDFGHIJKMNPQTW LS 7.3292402267456 4 1 0.200361212184938 13 5 -1.28333333333333 1.133 7.2 hour >20 hours >10 hours 21.67 6990 3.24764113927809 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02534 DDHETDMELKPANAA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2295.4159 H96C153N27O37S0 BCFGHIKLMNOPQRSVW DD 4.30659961700439 3 6 -3.22932221832996 15 5 -0.99 0.968 7.2 hour >20 hours >10 hours 68 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02535 LVSFRYEDQGPLVEG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2264.4924 H100C152N28O31S0 ABCHIJKMNOPQSTWY LV 6.00068569183349 1 1 -0.239085925835488 12 8 -0.445 0.967 7.2 hour >20 hours >10 hours 92.5 1490 0.657984102750797 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02536 CIVEEVDARSVYPYD 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1708.8649 H77C114N19O24S0 ABGHJKLMNOPQSTWX CI 4.13738994598388 1 3 -2.23416570182343 9 6 -0.28 0.936 7.2 hour >20 hours >10 hours 90.67 1490 0.87192381328682 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02537 TRDAIEPCTVGHRRY 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3845.35769999999 H168C282N47O54S0 BCDEFGJKLNPQSVWX TR 8.47303142547607 5 4 0.836874597655886 20 15 -0.148571428571428 0.944 7.2 hour >20 hours >10 hours 116.86 1490 0.387480207628019 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02538 DLKYNPSRVEAFHRY 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1444.80319999999 H69C119N17O15S0 ABCGIJLMNOPQSTVWX DL 10.1768663406372 4 0 3.75510660919429 6 7 0.0615384615384615 1.116 7.2 hour >20 hours >10 hours 112.31 1490 1.03128232274126 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02539 PYKFKATMYYKDVTV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 921.0766 H34C53N12O11S3 ABCGHIJLNOQRSW PY 6.72305240631103 1 0 -0.17252617775413 3 6 0.533333333333333 0.65 7.2 hour >20 hours >10 hours 33.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02540 NHIQRHVNDMLGRVA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1399.67449999999 H70C104N14O15S0 ABCEGJLMOPQSTW NH 8.75005207061767 1 0 0.759102613190301 5 8 1.63076923076923 0.625 7.2 hour >20 hours >10 hours 127.69 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02541 APTSPGTPGVAAATQ 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3055.54339999999 H144C217N32O38S1 BCDEFHIJKLMNORSVW AP 4.35354862213134 1 2 -1.96126571235201 16 12 0.214285714285714 0.689 7.2 hour >20 hours >10 hours 111.43 6990 2.28764546430596 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02542 LQNHELTLWNEARKL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 7115.7814 H311C496N82O107S0 BCDFGHIJKMNOPSTVW LQ 4.46648769378662 8 14 -7.12797036528924 41 22 -0.693650793650793 1.076 7.2 hour >20 hours >10 hours 102.06 2980 0.418787457411213 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02543 DPKPKKNKKPKNPTP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2997.64419999999 H144C211N34O29S3 ABCEFGHIJLMOQRSUVW DP 9.15671863555908 3 0 2.72838064209426 8 17 1.07599999999999 0.908 7.2 hour >20 hours >10 hours 101.2 6990 2.33183110924238 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02544 SRPGACYSRPLVSFR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2226.471 H95C149N30O29S1 ABCDHIJKMNOPTUW SR 11.1662626266479 3 0 2.7580936122913 14 6 -0.73 0.932 7.2 hour >20 hours >10 hours 43.5 5500 2.47027695397784 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02545 QFMGIFEDRAPVPFE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 965.1473 H42C61N10O11S2 ABCDHJKLNOPQSTUW QF 5.51141567230224 0 0 -0.259700366008717 4 5 0.655555555555555 0.591 7.2 hour >20 hours >10 hours 54.44 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02546 TLREHLRDIKAENTD 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1667.91089999999 H68C112N24O20S2 ABCFGIJKMNOPQRSVWY TL 10.7630128860473 3 0 2.44921646841958 10 5 -0.726666666666666 0.804 7.2 hour >20 hours >10 hours 32.67 1490 0.89333309111416 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02547 YARDLTTKARATAPT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 935.1231 H37C64N12O11S2 BCDEFGHIKLMNOPQRSVW YA 8.07210254669189 1 0 0.740289634091281 5 4 0.499999999999999 0.58 7.2 hour >20 hours >10 hours 86.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02548 CPPPTGATVVQFEQP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2014.136 H84C125N26O29S1 BDHIKLMNOSVWY CP 6.45698909759521 2 1 -0.463467583584982 11 7 -0.627777777777777 0.846 7.2 hour >20 hours >10 hours 59.44 2980 1.47954259295301 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02549 KNKKPKNPTPPRPAG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4625.195 H216C320N52O60S0 BCDEFHIJLMOQRSUVW KN 4.76801853179931 5 7 -2.23060756095796 20 17 -0.778378378378378 1.374 7.2 hour >20 hours >10 hours 102.7 20970 4.53386289659139 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02550 SMRISSRPGACYSRP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2688.0519 H125C185N37O29S0 ABCDFHIKLNOPQTUW SM 9.98977909088134 7 2 3.84517301976293 12 8 -1.59 1.605 7.2 hour >20 hours >10 hours 58.5 5960 2.21721909461644 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02551 NELRLTRDAIEPCTV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2888.2823 H125C210N39O38S0 ABCDGHIKLMOPQRSVWY NE 5.57177867889404 4 4 -1.10573937569848 13 12 -0.16 1.104 7.2 hour >20 hours >10 hours 136.8 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02552 PRPAGDNATVAAGHA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1729.9523 H72C122N22O24S1 BCDEFIJKLMPQSTVW PR 4.67912235260009 2 3 -1.24307769082344 9 6 -0.36 0.962 7.2 hour >20 hours >10 hours 104 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02553 PSRVEAFHRYGTTVN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1882.01 H79C122N20O30S1 BCDEGHIJKLNOQRTUW PS 4.05002841949462 0 3 -3.60765141287848 9 9 0.105555555555555 0.629 7.2 hour >20 hours >10 hours 92.22 1490 0.791706739071525 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02554 PATPAPPPLGAAPTG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2095.368 H90C149N33O24S0 BCDEFGHIJKLMNORSVW PA 11.9999677658081 5 1 3.46022821955843 14 4 -1.31111111111111 1.137 7.2 hour >20 hours >10 hours 59.44 5500 2.62483726008987 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02555 GGFLIAYQPLLSNTL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1671.1181 H88C133N17O14S0 ABCDHKMOPRSTVW GG 10.1768663406372 4 0 3.75510660919429 5 8 0.423076923076923 1.415 7.2 hour >20 hours >10 hours 112.31 1490 0.891618611515248 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02556 GGSFRFSSDAISTTF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2766.1126 H122C198N35O37S0 ABCDHIKLMNOPQRSVWY GG 4.55771427154541 3 4 -2.14826115359673 12 13 0.38 0.828 7.2 hour >20 hours >10 hours 144.4 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02557 ASVTVGRRVSARMLG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 208.2355 H6C10N2O3S1 BCDEFIJKLNOPQTUW AS 5.51812267303466 0 0 -0.249799375909707 1 1 0.85 0.27 7.2 hour >20 hours >10 hours 0 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02558 YGYREGSHTEHTTYA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2521.825 H116C158N29O30S2 BCDFIJKLNPQRSVW YG 8.13657093048096 3 2 0.750826543041708 10 10 -1.175 1.464 7.2 hour >20 hours >10 hours 24.5 19480 7.72456455146571 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02559 AANGGPATPAPPPLG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1079.2002 H49C76N10O16S0 BCDEFHIJKLMNOPQRSVW AA 4.05002841949462 0 2 -2.23696616389664 3 7 1.1 0.611 7.2 hour >20 hours >10 hours 146 1490 1.38065207919717 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02560 REHLREQSRKPPNPT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1287.4209 H57C88N16O17S0 ABCDGIJKLMPQSTVWY RE 5.57001667022705 0 0 -0.204125412145913 10 5 -0.16 0.326 7.2 hour >20 hours >10 hours 52.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02561 YYQANGGFLIAYQPL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1845.0282 H77C126N29O23S0 BCDFGHIKLMNOPQRSVW YY 10.7372900009155 5 2 1.8518677256913 14 1 -2.47333333333333 1.458 7.2 hour >20 hours >10 hours 26 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02562 TRTSRGWHTTDLKYN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3984.5423 H178C282N52O49S1 ABCEGIJKLMPQOSVWY TR 8.26692600250244 4 1 0.925649761739309 17 23 0.854999999999999 0.604 7.2 hour >20 hours >10 hours 115 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02563 GHRYSQFMGIFEDRA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3277.969 H155C248N42O33S1 ABCDJKLMPQSTUVW GH 9.93955821990966 5 2 1.13677846730058 13 15 0.692857142857142 0.924 7.2 hour >20 hours >10 hours 156.43 5500 1.67786821656947 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02564 STCVPVAADNVIVQN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 932.1423 H39C71N13O10S1 BCDEFGHIKLMNOPQRSVW ST 11.0001920700073 2 0 1.45913745831859 5 4 0.144444444444444 0.806 7.2 hour >20 hours >10 hours 97.78 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02565 EPCTVGHRRYFTFGG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1215.4195 H52C88N14O16S1 BCDIJKLMNOPQSTUVW EP 4.20781345367431 1 2 -1.24756785393001 5 6 0.618181818181818 0.699 7.2 hour >20 hours >10 hours 141.82 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02566 IDLNITMLEDHEFVP 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2663.9861 H117C170N35O32S2 BCGHJKLMNOPQRSVWY ID 8.85977725982666 5 2 1.83008774329528 15 7 -1.32727272727272 1.392 7.2 hour >20 hours >10 hours 17.73 11000 4.12915067387176 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02567 NYTEGIAVVFKENIA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1726.9116 H77C109N23O20S1 BCDFGHJKLMOPQRSVW NY 8.32597904205322 3 1 0.913081816054567 10 5 -0.593333333333333 0.972 7.2 hour >20 hours >10 hours 19.33 1490 0.862811970224764 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02568 WVPKRPSVCTMTKWQ 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1812.9242 H91C107N15O24S0 ABCDFGHJKLNOPQRSY WV 4.05002841949462 0 2 -2.23827346586028 6 9 0.0199999999999999 0.952 7.2 hour >20 hours >10 hours 26 5960 3.28750644952503 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02569 VDARSVYPYDEFVLA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2888.2823 H125C210N39O38S0 BCGHIKLMNOPQRSWX VD 5.53557224273681 4 4 -1.50341736918594 13 12 -0.16 1.104 7.2 hour >20 hours >10 hours 136.8 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02570 GSHTEHTTYAADRFK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1847.211 H84C128N23O19S2 BCDEHIJKLMNOPQRTVW GS 10.0619192123413 3 0 2.74819262219229 9 6 -0.679999999999999 1.167 7.2 hour >20 hours >10 hours 38.67 11000 5.95492339532409 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02571 LHDLRFADIDTVIHA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1720.7964 H74C107N23O24S0 ABCEGJKLMNOPQRSTVW LH 6.92147731781005 4 2 -0.0636267882864713 11 4 -1.33333333333333 1.127 7.2 hour >20 hours >10 hours 13.33 1490 0.865878148048194 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02572 LTLWNEARKLNPNAI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1143.36 H46C70N14O13S3 BCDFGHJKMOPQRSVWY LT 5.82255229949951 1 1 -0.258589604968873 4 5 -0.166666666666666 1.108 7.2 hour >20 hours >10 hours 43.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02573 TVSTFIDLNITMLED 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1192.4453 H60C91N11O13S0 BCFGHJLMNOPQRSWXY TV 4.05002841949462 0 1 -1.163172381302 2 8 2.26 0.74 7.2 hour >20 hours >10 hours 204 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02574 YMSPFYGYREGSHTE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 967.0822 H35C59N14O13S2 ABCDHIKLNOPQRSVW YM 8.07210254669189 1 0 0.740289634091281 5 4 -0.477777777777777 0.76 7.2 hour >20 hours >10 hours 22.22 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02575 ATMYYKDVTVSQVWF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1462.7754 H68C117N17O17S0 BCDEFGHIJKLMNOPQRSVW AT 9.82564258575439 4 1 2.7579170711675 6 7 -0.0538461538461537 1.199 7.2 hour >20 hours >10 hours 104.62 1490 1.01861160640246 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02576 PPNPTPPPPGASANA 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1021.083 H47C61N12O13S0 BCDEFGHIJKLNOQRSVW PP 5.52500019073486 0 0 -0.239898385810697 5 3 -0.85 1.093 7.2 hour >20 hours >10 hours 36.25 11000 10.772875466539 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02577 TTKARATAPTTRNLL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2236.6529 H107C168N26O25S0 BCDFGIJKLMNOPQRSVWY TT 11.0008367538452 2 0 1.7590926132903 9 11 0.865 0.751 7.2 hour >20 hours >10 hours 127 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02578 QFEQPRRCPTRPEGQ 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1036.1856 H43C63N13O12S2 ABCDHIKLMNOPQRSTVWY QF 8.07210254669189 1 0 0.740289634091281 6 3 -0.655555555555555 0.821 7.2 hour >20 hours >10 hours 0 5500 5.30792939025595 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02579 PLVEGQLGENNELRL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1026.3198 H45C77N13O9S2 ABCDFHIKMNOPQRSVW PL 8.90451831817626 3 0 1.82547582024786 4 5 0.511111111111111 1.1 7.2 hour >20 hours >10 hours 107.78 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02580 SHQLSRADITTVSTF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3276.6552 H138C224N41O46S2 BCDEFGIJKLMNOPQRTVW SH 4.86367855072021 4 5 -1.25373416203976 17 13 -0.459999999999999 0.932 7.2 hour >20 hours >10 hours 78 1490 0.45473200842127 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02581 RHEIKDSGLLDYTEV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3403.0598 H154C255N49O35S1 BCDFGIJKLMNOPQSTVW RH 11.8240335464477 8 2 3.22562235678853 16 12 -0.075 1.126 7.2 hour >20 hours >10 hours 132.14 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02582 LRDIKAENTDANFYV 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 4869.766 H211C352N68O55S4 BCDFGHJKLMNOPQRSTVW LR 9.89539737701416 9 3 5.01968476802516 26 16 -0.54047619047619 1.06 7.2 hour >20 hours >10 hours 92.86 1490 0.305969527077892 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02583 ADRFKQVDGFYARDL 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2858.21789999999 H125C201N41O35S0 BCEGHIKLMNOPQRSVWY AD 11.0000631332397 5 1 3.39629035260946 19 7 -0.884615384615384 0.971 7.2 hour >20 hours >10 hours 63.46 1490 0.521303851606275 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02584 PSVCTMTKWQEVDEM 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2374.5651 H107C151N30O31S0 BCDFGHIKLMNOPQRTVW PS 9.17438297271728 3 2 0.959751388659041 15 5 -1.085 1.062 7.2 hour >20 hours >10 hours 14.5 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02585 EYPLSRVDLGDCIGK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3694.4419 H151C244N56O36S8 ABCDFGHJKLMNOPQRSVW EY 9.82564258575439 10 0 9.67583868900221 16 17 -0.406060606060606 1.138 7.2 hour >20 hours >10 hours 15.15 6990 1.89203137827124 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02586 DMELKPANAATRTSR 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2036.35649999999 H98C136N24O21S1 BCFGHIJKLNOPQRSVW DM 8.64103603363037 2 0 0.881050774110671 7 11 0.516666666666666 0.916 7.2 hour >20 hours >10 hours 86.67 12490 6.13350363750159 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02587 RPEGQNYTEGIAVVF 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available 136-150 Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1016.15269999999 H40C62N13O13S2 BCDFGHJKLMNOPQRSVW RP 5.07619953155517 1 1 -1.17140541681428 4 5 0.0777777777777777 0.946 7.2 hour >20 hours >10 hours 97.78 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02588 TGDFVYMSPFYGYRE 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available 291-305 Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1664.8771 H72C115N19O23S1 ABCDFHIJKLMNOPQRSVW TG 4.5583963394165 2 3 -1.17283985141933 9 6 -0.306666666666666 0.931 7.2 hour >20 hours >10 hours 97.33 1490 0.894960955376226 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02589 QRRNQLHDLRFADID 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available 706-720 Not Available K01760 Genomic DNA Not Available 2GUM##3NW8 HSV- Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry "peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1897.0594 H80C125N29O24S0 BCDEGHIKLMNOPQSTVW QR 6.76056613922119 4 3 -0.146211012829276 10 5 -1.4 1.392 7.2 hour >20 hours >10 hours 84.67 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02590 YEDQGPLVEGQLGEN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1647.694 C70H76N18O13 BCDFGHJKLMNOPQRSTVW YE 4.05 0 4 -4.231 4 4 -1.12 -0.188 7.2 hour >20 hours >10 hours 71.333 1490 0.993333333333333 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02591 ASANASVERIKTTSS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1521.629 C61H78N20O10 BCDEFGHIJKLMNOPQRTVW AS 8.793 2 1 0.798 7 5 -0.393 0.069 7.2 hour >20 hours >10 hours 65.333 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02592 TTNLTEYPLSRVDLG 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 967.122 H37C64N12O13S2 BCDFGHIKLMNOPQRSTVW TT 8.07210254669189 1 0 0.740289634091281 6 3 0.0222222222222222 0.494 7.2 hour >20 hours >10 hours 32.22 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02593 TVAWDWVPKRPSVCT 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 3811.2985 H164C280N47O55S0 BCDFGHIKLMNOPQRSVW TV 6.30721836090088 5 5 -0.231740281333444 21 14 -0.202857142857142 0.94 7.2 hour >20 hours >10 hours 119.71 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02594 VCRSTAKYVRNNLET 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 737.8838 H35C57N7O9S0 BCDFGHIJKLMNOPQRSW VC 8.59087963104248 1 0 0.758103612191301 3 3 0.166666666666666 0.968 7.2 hour >20 hours >10 hours 130 1490 2.01928813181696 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02595 QLGENNELRLTRDAI 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1647.6942 H70C102N18O27S0 BCDFGHIKLMNOPQRSVW QL 4.05002841949462 0 4 -4.23134523995022 11 4 -1.12 1.001 7.2 hour >20 hours >10 hours 71.33 1490 0.90429401280893 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02596 NPNAIASVTVGRRVS 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1036.356 H42C71N11O10S4 BCDEFGHIKLMOQRSVW NP 8.05837078094482 1 0 0.739300632992282 4 5 0.222222222222222 0.801 7.2 hour >20 hours >10 hours 43.33 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02597 ATHIKVGQPQYYQAN 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 2144.3919 H95C146N30O26S0 BCDEFGHIJKLMNOPQRSVW AT 9.98616886138916 3 1 1.75920437333114 14 6 -0.675 0.89 7.2 hour >20 hours >10 hours 63 1490 0.694835678123947 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02598 TAFHRDDHETDMELK 15 - Synthetic construct(derived from HSV-1 B glycoprotein (gB)) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV Herpesviridae beta-galactosidase activity [Ref:19104014]HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Not Available 1082.2142 H43C64N15O13S2 BCDFGHIKLMNOPQRSVW TA 8.06784763336181 2 0 0.826464821346867 5 4 -0.788888888888888 1.042 7.2 hour >20 hours >10 hours 11.11 1490 1.3768069204784 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV DRAVPe02599 TVSSGADTEDVVC 13 Viroporin p7 HCV non-structural protein 5A P27958 Experimentally Validated 63746 Not Available Not Available 2407-2419 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 20% and 50%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1282.3316 H50C81N13O23S1 ABEHJKMNQWXZ TV 4.05002841949462 0 3 -3.60665241187948 8 5 0.23076923076923 0.448 7.2 hours 6 hours 6.5 hours 74.62 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02600 GAPLGGAARALAHGVRVL 18 141-158 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 141-158 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 83% and 92%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 2938.0015 H112C163N39O46S4 BCDEIJKMNQWXYZ GA 4.36673526763916 3 6 -3.26723647769263 20 6 -1.69615384615384 1.131 1.3 hours 1.1 hours 1.2 hours 0 11000 3.74404165552672 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02601 GRKRRQTSMTDFYHS 15 139-153 Host p21 protein P38936 Experimentally Validated 9606 CDKN1A Not Available 139-153 Not Available CM000668.2 Not Available "Chromosome 6: 36,676,460-36,687,397" 1AXC##2ZVV HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 105% and 101%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1022.15889999999 H42C61N13O12S2 ABCEIJLNPVWXZ GR 8.054953956604 2 0 0.825475820247868 5 4 -0.833333333333333 1.06 1.2 hours 1 hours 1.1 hours 11.11 1490 1.45769899376702 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02602 RRHGDEDMFYMHVRG 15 339-353 Host p73 protein Q9JJP2 Experimentally Validated 10090 Tp73 Not Available 339-353 Not Available CM000997.3 Not Available "Chromosome 4: 154,140,706-154,224,665" None HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 96% and 99%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 982.1098 H46C61N9O12S1 ABCIJKLNPQTWXZ RR 4.05002841949462 0 2 -2.16036191932879 3 5 0.249999999999999 1.134 1.3 hours 1 hours 1 hours 61.25 5500 5.60018849216249 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02603 TCGFADLMGYIPLVGAPL 18 127-144 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 127-144 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 79% and 71%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 736.859399999999 H33C54N10O8S0 BEHJKNQRSWXZ TC 9.41014385223388 1 0 0.398186594466627 6 1 -0.942857142857143 0.66 7.2 hours 6 hours 6.5 hours 55.71 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02604 AIPALGTNVKKRRHG 15 328-342 Host p73 protein Q9JJP2 Experimentally Validated 10090 Tp73 Not Available 328-342 Not Available CM000997.3 Not Available "Chromosome 4: 154,140,706-154,224,665" None HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 91% and 89%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 938.0807 H36C61N11O13S2 BCDEJMQSWXZ AI 5.82187023162841 1 1 -0.259578606067873 4 5 0.0888888888888888 0.791 1.2 hours 1 hours 1.1 hours 65.56 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02605 SWGPTDPRRRSRNLGKVI 18 106-123 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 106-123 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 88% and 96%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 3954.39779999999 H172C283N48O57S0 ABCEHJMQXZ SW 4.85503902435302 6 8 -2.25112182058133 22 12 -0.817647058823529 1.205 100 hours 60 hours 90 hours 106.18 5500 1.39085652940632 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02606 VKKRRHGDEDMFYMH 15 336-350 Host p73 protein Q9JJP2 Experimentally Validated 10090 Tp73 Not Available 336-350 Not Available CM000997.3 Not Available "Chromosome 4: 154,140,706-154,224,665" None HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 101% and 99%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 3810.2194 H168C272N42O57S0 ABCIJLNPQSTWXZ VK 4.1967866897583 3 7 -4.02986400470627 21 13 -0.373529411764705 0.987 20 hours 15 hours 18 hours 117.65 5500 1.44348643020399 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02607 QRKTKRNTNRRPQDVKFP 18 45870 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 8 to 25 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 107% and 102%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 989.2135 H41C70N12O11S2 ABCEGHJLMWXZ QR 5.82255229949951 1 1 -0.258589604968873 4 5 0.711111111111111 0.75 1.2 hours 1 hours 1.1 hours 130 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02608 SPRGSRPSWGPTDPRRRS 18 99-116 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 99-116 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 110% and 105%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1950.33379999999 H89C149N28O20S0 ABCEHJKMQXZ SP 11.7113428115844 3 0 2.75907261349029 10 8 0.3 0.78 48.0 mins 42.0 mins 36.0 mins 135 1490 0.763971787803708 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02609 SMTDFYHSKRRLIFS 15 146-160 Host p21 protein P38936 Experimentally Validated 9606 CDKN1A Not Available 146-160 Not Available CM000668.2 Not Available "Chromosome 6: 36,676,460-36,687,397" 1AXC##2ZVV HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 98% and 96%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1528.7507 H69C111N19O19S0 ABCEGJNQVWXZ SM 10.0102155685424 2 0 1.95652086568035 11 4 -0.4 0.678 20 hours 15 hours 18 hours 78 1490 0.97465204758369 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02610 VKFPGGGQIVGGVYLLPR 18 22-39 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 22-39 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 58% and 70%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 745.9273 H33C57N7O9S1 ABCDEHJMNSTWXZ VK 4.05002841949462 0 1 -1.24867861496986 1 6 2.44285714285714 0.473 1.2 hours 1 hours 1.1 hours 222.86 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02611 AFKQSPPAIPALGTN 15 321-335 Host p73 protein Q9JJP2 Experimentally Validated 10090 Tp73 Not Available 321-335 Not Available CM000997.3 Not Available "Chromosome 4: 154,140,706-154,224,665" None HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 102% and 97%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1854.1719 H89C130N18O22S1 BCDEHJMQRVWXZ AF 9.34793186187744 3 1 1.95365562252419 7 8 -0.479999999999999 1.139 20 hours 15 hours 18 hours 45.33 4470 2.41077971249591 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02612 QIVGGVYLLPRRGPRLGV 18 29-46 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 29-46 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 81% and 92%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 910.0276 H34C56N11O13S2 ABCDEHJKMNSTWXZ QI 8.05837078094482 1 0 0.739300632992282 7 2 -0.744444444444444 0.677 1.2 hours 1 hours 1.1 hours 0 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02613 VRVLEDGVNYATGNLPGC 18 155-172 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 155-172 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 82% and 100%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 4040.4091 H175C277N52O57S0 BHJKMQWXZ VR 5.63867816925048 7 7 -1.14213607063974 24 10 -1.21470588235294 1.32 1.1 hours 1 hours 1 hours 83.24 11000 2.72249659075364 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02614 RRRSRNLGKVIDTLTCGF 18 113-130 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 113-130 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 98% and 104%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1214.3783 H54C69N17O11S2 ABEHJMPQWXZ RR 8.07719554901122 3 0 0.913649009501456 5 4 -1.25555555555555 1.674 1.2 hours 1 hours 1.1 hours 0 11000 9.05813287342173 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02615 MSTNPKPQRKTKRNTNRR 18 43101 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 1 to 18 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 92% and 94%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1423.6866 H54C108N36O9S0 ABCDEFGHJLMVWXZ MS 11.9999677658081 9 0 8.76001161508929 9 0 -4.5 2.56 1.0 hours 1 hours 1 hours 0 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02616 FYHSKRRLIFSKRKP 15 150-164 Host p21 protein P38936 Experimentally Validated 9606 CDKN1A Not Available 150-164 Not Available CM000668.2 Not Available "Chromosome 6: 36,676,460-36,687,397" 1AXC##2ZVV HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 87% and 89%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 4053.4509 H176C279N53O56S0 ABCDEGJMNQTVWXZ FY 6.77574214935302 7 6 -0.143256831579585 24 10 -1.21470588235294 1.331 20 hours 15 hours 18 hours 83.24 11000 2.71373707770828 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02617 QSPPAIPALGTNVKK 15 324-338 Host p73 protein Q9JJP2 Experimentally Validated 10090 Tp73 Not Available 324-338 Not Available CM000997.3 Not Available "Chromosome 4: 154,140,706-154,224,665" None HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 105% and 102%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 425.482699999999 H18C29N7O4S0 BCDEHJMRWXZ QS 9.75002117156982 1 0 0.760091614289301 4 0 -2.025 0.868 1.0 hours 1 hours 1 hours 0 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02618 RLGVRATRKTSERSQPRG 18 43-60 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 43-60 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 71% and 85%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1095.2545 H41C71N16O14S2 BCDEHJMNWXZ RL 8.0720380783081 2 1 0.741400395131125 6 3 -0.955555555555555 1.069 1.2 hours 1 hours 1.1 hours 43.33 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02619 DGSWSTVSSGADTED 15 2402-2416 HCV non-structural protein 5A P27958 Experimentally Validated 63746 Not Available Not Available 2402-2416 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 74% and 89%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1638.752 H72C101N17O24S1 BCHJKMQXZ DG 4.05002841949462 0 2 -2.21109418033086 9 6 -0.56 0.727 4.4 hours 20 hours 10 hours 32.67 1490 0.909228486067446 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02620 ARALAHGVRVLEDGVNYA 18 148-165 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 148-165 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 92% and 97%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 2175.3415 H96C131N29O27S1 BCIJKMQWXZ AR 6.9094274520874 3 1 -0.0743402383606897 13 5 -1.04444444444444 1.103 30 hours 15 hours 28 hours 21.67 5500 2.52833865395387 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02621 MGYIPLVGAPLGGAARAL 18 134-151 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 134-151 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 78% and 93%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 3767.2495 H161C276N49O53S0 BCDEHJKNQRSTWXZ MG 8.15642719268798 6 5 0.466803363220913 19 16 -0.314285714285714 1.002 1.9 hours 2 hours 1.8 hours 103.43 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02622 QPRGRRQPIPKARRPEGR 18 57-74 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 57-74 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 103% and 96%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 986.1699 H40C64N13O11S2 BCDEHJLMNSTVWXZ QP 8.06797657012939 2 0 0.826474821246869 5 4 -0.266666666666666 0.986 1.2 hours 1 hours 1.1 hours 54.44 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02623 PGDPDLSDGSWSTVSSGA 18 2395-2412 HCV non-structural protein 5A P27958 Experimentally Validated 63746 Not Available Not Available 2395-2412 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 74% and 89%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 3942.3441 H170C279N48O58S0 BCHJKMQXZ PG 4.76710910797119 6 8 -2.19241652428969 23 11 -0.964705882352941 1.206 4.4 hours 20 hours 10 hours 97.65 5500 1.39510906721714 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02624 PIPKARRPEGRTWAQPGY 18 64-81 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 64-81 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 87% and 97%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1744.0016 H81C123N22O20S0 BCDEHJLMNSVXZ PI 6.74965305328369 2 1 -0.149923735482901 8 7 0.493333333333333 0.915 1.0 hours 1 hours 1 hours 123.33 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02625 LLPRRGPRLGVRATRKTS 18 36-53 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 36-53 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 87% and 95%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1655.8885 H76C120N18O22S0 BCDEHJMNQWXZ LL 4.67997493743896 2 3 -1.03672744953338 9 6 -0.226666666666666 1.005 20 hours 15 hours 18 hours 97.33 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02626 PEGRTWAQPGYPWPLYGN 18 71-88 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 71-88 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 88% and 96%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 2042.55699999999 H95C170N28O20S0 BCDHJKMNQSVXZ PE 11.9999677658081 4 0 3.75808361239129 6 14 1 0.787 1.0 hours 1 hours 1 hours 161.5 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02627 RKTSERSQPRGRRQPIPK 18 50-67 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 50-67 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 86% and 92%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 933.107299999999 H37C62N12O11S2 BCDEHJLMNVWXZ RK 8.9037446975708 2 0 1.73830163199328 7 2 -1.18888888888888 0.966 1.2 hours 1 hours 1.1 hours 0 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02628 GKVIDTLTCGFADLMGYI 18 120-137 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 120-137 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 40% and 69%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1175.3589 H48C84N16O15S1 BEHJNQRSWXZ GK 8.79266567230224 2 1 0.795986347894929 7 5 -0.0666666666666667 0.722 4.4 hours 20 hours 10 hours 81.67 0 0 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02629 TNRRPQDVKFPGGGQIVG 18 15-32 HCV core protein P27958 Experimentally Validated 63746 Not Available Not Available 15-32 Not Available Not Available Not Available Not Available 1A1R##1A1V HCV Flaviviridae EMSA "[Ref:22452666]HCV:IC50=decrease the initial rate and maximum OD strongly to levels as low as 105% and 101%,respectively." No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L NS5A protein "Peptide derived from the C-terminal end of NS5A protein moderately inhibits the assembly process.Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding." 1129.2225 H50C74N14O15S0 BCEHJLMSWXZ TN 6.78495007 1 0 -0.1179502 5 6 0.24545455 0.595 4.4 hours 20 hours 10 hours 80 1490 1.319492 22452666 Can J Microbiol. 2012 "Duvignaud JB, Majeau N, Delisle P, Voyer N, Gagne SM, Leclerc D." Interfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein. 10.1139/w2012-009 Anti-HCV DRAVPe02630 RRKKAAVALLKAVLLALAAP 20 C3 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 mRNA "Chromosome 11: 69,773,312-69,775,084" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=-0.21µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1786.0103 H80C122N18O25S1 FHIMTW RAL 4.05002841949462 1 4 -3 8 7 0.166666666666666 0.936 20hours 15hours 18hours 123.33 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02631 RRKKAAVAELPAVLLALLAP 20 E2 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,084" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=5.11µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1198.4619 H52C96N19O12S0 FHIMTW RLA 11.9999677658081 4 0 3.75808361239129 6 4 -0.679999999999999 1.357 48mins 42mins 36mins 117 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02632 RRKKAAVAKLPAVLLALLAP 20 D2 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,085" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=4.06µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 547.671899999999 H21C39N9O5S1 FHIMTW RLA 11.0008367538452 2 0 1.7590926132903 4 1 -1.46 1.166 30hours 15hours 28hours 0 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02633 RRKKAAVALEPAVLLALLAP 20 E1 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,086" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=4.7µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1621.1025 H85C135N17O13S0 FHIMTW RLA 10.4777402877807 4 0 3.75610561019329 5 8 0.815384615384615 1.335 1.3hours 1.1hours 1.2hours 142.31 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02634 RRKKAAVALLPAVLKALLAP 20 A6 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,087" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=1.05µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 7326.64169999999 H322C513N92O86S8 FHIMTW RLA 8.66231060028076 9 5 2.53573884060418 35 31 0.125757575757575 0.886 30hours 18hours 25hours 91.67 6990 0.954052386648033 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02635 RRKKAAVALLPAVALALLAP 20 C7 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,088" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=3.38µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 3421.8597 H149C245N46O45S0 FHIMTW RLA 5.42070064544677 5 5 -2.05321740016884 16 14 -0.223333333333333 1.078 1.1hours 1hours 1hours 130.33 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02636 RRKKAAVALLPAVLLALEAP 20 B3 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,089" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=4.87µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1821.1886 H82C139N21O22S1 FHIMTW RLA 9.31079807281494 2 0 1.72207939795813 8 9 0.776470588235294 0.643 100hours 60hours 90hours 131.76 1490 0.818147005752177 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02637 RRKKAAVALLPAVLAALLAP 20 C6 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,090" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=0.8µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1062.2658 H46C69N13O11S2 FHIMTW RLA 8.06797657012939 2 0 0.826474821246869 5 4 -0.0666666666666667 1.023 1.2hours 1hours 1.1hours 43.33 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02638 RRKKAAVALLKAVLLAALAP 20 C4 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,091" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=-0.06µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 3995.5771 H172C288N47O56S2 FHIMTW RLA 8.19459247589111 6 5 0.827796067432086 22 13 -0.76 1.156 1.3hours 1hours 1hours 89.14 1490 0.372912338495483 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02639 RRKKAAVALAPAVLLALLAP 20 F1 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,092" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=1.09µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 2937.57789999999 H128C212N40O30S4 FHIMTW RLA 9.30396442413329 6 1 3.80844430242305 11 14 0.379999999999999 1.024 1.2hours 1hours 1.1hours 109.2 1490 0.507220591494782 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02640 RRKKAAVALLPAVLLAELAP 20 B4 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,093" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=6.43µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1245.4918 H53C94N16O15S1 FHIMTW RLA 8.79266567230224 2 1 0.795986347894929 6 6 0.291666666666666 0.768 4.4hours 20hours 10hours 114.17 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02641 RRKKAAVALKPAVLLALLAP 20 D1 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,094" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=1.58µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1175.3589 H48C84N16O15S1 FHIMTW RLA 8.74773120880127 2 1 0.760213374230145 7 5 -0.0666666666666667 0.722 1.1hours 1hours 1hours 81.67 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02642 RRKKAAVALLPAVLLAKLAP 20 A4 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,095" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=2.46µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 2099.651 C98H139N29O FHIMTW RLA 12 5 0 4.757 0 13 0.715 0.997 1.0hours 1hours 1hours 156.5 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02643 RRKKAAVALLKAVLLALKAP 20 A3 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,096" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=0.11µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1476.802 H69C119N17O17S0 FHIMTW RLA 9.82564258575439 4 1 2.76315435093499 6 7 -0.0846153846153845 1.237 1.3hours 1.1hours 1.2hours 112.31 1490 1.00893687847118 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02644 RRKKAAVAALPAVLLALLAP 20 F2 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,097" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=1.09µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 2155.4731 H90C155N39O22S0 FHIMTW RLA 11.9999677658081 7 1 5.7618530757635 16 2 -2.34999999999999 1.428 48mins 42mins 36mins 27.22 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02645 RRKKAAVALLPAVKLALLAP 20 A7 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,098" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=-0.03µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 269.296999999999 H12C17N3O3S0 FHIMTW RLA 5.95498714447021 0 0 -0.0414711324216447 3 0 -1.2 0.303 20hours 15hours 18hours 0 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02646 RRKKAAVALLPAVELALLAP 20 B7 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,099" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=4.32µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1430.8196 H69C121N17O14S0 FHIMTW RLA 10.4777402877807 4 0 3.75610561019329 5 8 0.823076923076923 1.05 1.3hours 1.1hours 1.2hours 134.62 0 0 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02647 RRKKAAVALLPAVLEALLAP 20 B6 Synthetic construct(derived from FGF-4 signal sequence) P08620 Experimentally Validated 9606 FGF4/2249 AAB59555.1 Not Available AAA59473.1 CM000673.2 Genomic DNA "Chromosome 11: 69,773,312-69,775,084" 1IJT VACV Poxviridae Plaque assay [Ref:19395056]VACV:EC50=0.53µM mOD/min in Hela cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 3580.0097 H160C253N44O48S0 FHIMTW RLA 6.27879886627197 5 5 -0.233241481807383 17 14 -0.512903225806451 1.156 5.5hours 10hours 6hours 97.74 6990 1.95250867616364 19395056 Virology. 2009 "Altmann SE, Jones JC, Schultz-Cherry S, Brandt CR." Inhibition of Vaccinia virus entry by a broad spectrum antiviral peptide.  10.1016/j.virol.2009.03.023 Anti-VACV DRAVPe02648 PPWCCCSPMKRASPPPAQSDLPATPKCPP 29 GFP-NP9-5 Synthetic Contrust (from Conotoxin) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None IAV Orthomyxoviridae Luciferase assay "[Ref:22095520]IAV:IC50=40.7% ±15.8%,multiplicity of infection of 0.01 was inhibited to 20% and 69% at 12 and 24 h post-infection, respectively. " No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Nucleoprotein Inhibit Replication 1048.2211 H39C63N15O12S3 NYOUM PCL 8.08164386749267 2 0 2 6 3 -0.822222222222222 0.901 1.2hours 1hours 1.1hours 0 0 0 22095520 Antivir Chem Chemother. 2011 "Jiang H, Xu Y, Li L, Weng L, Wang Q, Zhang S, Jia B, Hu H, He Y, Jacob Y, Toyoda T." Inhibition of influenza virus replication by constrained peptides targeting nucleoprotein. 10.3851/IMP1902 Anti-IAV DRAVPe02649 EALMWEGF 8 38 Synthetic-Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None VACV Poxviridae RT PCR [Ref:19428604]VACV:IC50=75% in Flp-In-293 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 2089.2671 H99C130N25O25S0 NDCPMWYOU E 6.4212942123413 1 1 0 12 6 -1.22777777777777 1.042 20hours 15hours 18hours 27.22 13980 6.69134166713294 19428604 Antiviral Res. 2009 "Saccucci L, Crance JM, Colas P, Bickle M, Garin D, Iseni F." Inhibition of vaccinia virus replication by peptide aptamers. 10.1016/j.antiviral.2009.02.191 Anti-VACV DRAVPe02650 RQLVLRTR 8 72 Synthetic-Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None VACV Poxviridae RT PCR [Ref:19428604]VACV:IC50=40% in Flp-In-293 cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 3081.4395 H144C207N38O37S0 RNDCPQYVOU RL 8.51158351898193 4 1 3 13 14 0.162962962962962 0.936 2.8hours 2.5hours 2.6hours 86.67 8480 2.75196056907819 19428604 Antiviral Res. 2009 "Saccucci L, Crance JM, Colas P, Bickle M, Garin D, Iseni F." Inhibition of vaccinia virus replication by peptide aptamers. 10.1016/j.antiviral.2009.02.191 Anti-VACV DRAVPe02651 CGYKLC 6 MrIA-SL Conotoxin No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV:IC50=16.7μM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1271.5142 H57C95N20O12S0 RNDQWVOU CG 11.9999677658081 4 0 3.75808361239129 6 4 -1.15 1.572 48 mins 42 mins 36 mins 78 5500 4.32555137803416 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02652 CGYGLC 7 Inhibitor 1 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=15.1Ki (µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 614.734499999999 H25C36N6O7S2 RNDQWVOU CG 5.51073360443115 0 0 -0.260699367007718 2 4 1.11666666666666 0.502 1.2hours 1hours 1.1hours 65 1490 2.4238106044154 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02653 CGYGLC 6 Inhibitor 2 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=>100Ki (µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 3869.28989999999 H169C277N45O57S0 RNDQWVOU CG 4.44119434356689 4 7 -3.22830125799532 21 13 -0.458823529411764 1.049 1.4hours 1.2hours 1.3hours 117.65 5500 1.42144944993654 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02654 CGYKGC 6 Inhibitor 3 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=12Ki (µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 3575.9746 H154C254N44O52S0 RNDQWVOU CG 8.59094409942627 2 1 0.759224373131145 21 13 -0.0705882352941176 0.721 5.5hours 10hours 6hours 103.24 0 0 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02655 CGYKRC 6 Inhibitor 4 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=5Ki (µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1685.936 H73C122N18O24S1 RNDQWVOU CG 7.91892566680908 1 0 0.448247467120587 9 8 0.876470588235294 0.419 1.9hours 2hours 1.8hours 108.82 1490 0.883782065274127 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02656 CGKRRC 6 Inhibitor 5 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=3.5Ki (µM) No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1855.9508 H88C111N18O26S0 RNDQWVOU CG 4.50724124908447 1 2 -2.15109927760569 7 8 -0.553333333333333 1.108 30hours 15hours 28hours 52 5960 3.2112920234739 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02657 CGKRKLC 7 Inhibitor 6 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=6.7µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 3878.3445 H167C282N48O56S0 RNDQWVOU CG 4.65689830780029 4 6 -2.22942201893517 21 14 -0.311428571428571 1.021 30hours 15hours 28hours 130.86 0 0 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02658 CGKRKSC 9 Inhibitor 7 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=3.3µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 971.1155 H38C60N14O11S2 RNDQWVOU CG 8.07719554901122 3 0 0.913649009501456 6 3 -0.388888888888888 1.012 1.2hours 1hours 1.1hours 43.33 0 0 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02659 AGKRKSG 8 Inhibitor 8 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=16.7µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1844.95519999999 H77C115N23O27S1 RNDQWVOU CG 4.79575595855712 4 5 -3.41948082325724 11 4 -1.56 1.356 7.2hours 6hours 6.5hours 32.67 0 0 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02660 CAGKRKSG 12 Inhibitor 9 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DENV 2 Flaviviridae Flouroscence spectrtophotometery [Ref:22780881]DENV-2:IC50=6.7µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 2069.23279999999 H84C131N25O31S2 RNDQWVOU CG 5.82800884246826 1 1 -0.250676616967864 14 6 -0.755 0.659 30hours 15hours 28hours 34 1490 0.720073642753005 22780881 J Med Chem. 2012 "Xu S, Li H, Shao X, Fan C, Ericksen B, Liu J, Chi C, Wang C." Critical effect of peptide cyclization on the potency of peptide inhibitors against Dengue virus NS2B-NS3 protease. 10.1021/jm300655h Anti-DENV DRAVPe02661 DPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKP 37 HBD2 Human alpha defensin Q9TT12 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None BKV Polyomaviridae Flow cytometry [Ref:18782756]BKV:IC50=45% in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane HBD2 inhibit BKV infection by targeting an early event in the viral lifecycle 1560.7777 H63C110N23O20S1 HMW CPTKG 10.8352174758911 3 1 1.79597634799492 10 5 -0.633333333333333 0.865 4.4hours 20hours 10hours 65.33 0 0 18782756 J Biol Chem. 2008 "Dugan AS, Maginnis MS, Jordan JA, Gasparovic ML, Manley K, Page R, Williams G, Porter E, O'Hara BA, Atwood WJ." Human alpha-defensins inhibit BK virus infection by aggregating virions and blocking binding to host cells. 10.1074/jbc.M805902200 Anti-BKV DRAVPe02662 AYQPLLSNTLAELYV 15 - HSV-1 B glycoprotein (gB) P06437 Experimentally Validated 10306 gB Not Available Not Available Not Available K01760 Not Available Not Available 2GUM##3NW8 HSV 1 Herpesviridae beta-galactosidase activity [Ref:19104014] HSV-1:IC50=Low in Vero cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1623.0754 H84C133N17O14S0 HIKMFTWV LA 10.4777402877807 4 0 3.75610561019329 6 7 0.438461538461538 1.34 1.3hours 1.1hours 1.2hours 120 0 0 19104014 Antimicrob Agents Chemother. 2009 "Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR." Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. 10.1128/AAC.00793-08 Anti-HSV 1 DRAVPe02663 RRRRR 5 - Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae Flouroscence spectrtophotometery [Ref:10958789]HCMV:IC50=0.99¬±0.08µM in CHO cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Not Available 1551.69639999999 H65C96N16O23S2 HILMFTWV R 4.39697360992431 2 4 -3.15507104279364 8 5 -1.13846153846153 1.246 1.1hours 1hours 1hours 37.69 1490 0.960239387034732 10958789 J Biol Chem. 2000 "Cameron A, Appel J, Houghten RA, Lindberg I." Polyarginines are potent furin inhibitors. 10.1074/jbc.M003848200 Anti-HCMV DRAVPe02664 CRCCELKSLCPTLMRVVRLLGLVLL 25 C8 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RV Rhabdoviridae GFP assay [Ref:15220414]HCV:IC50=78% in BSR cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Phosphoprotein Not Available 4417.9677 H202C310N51O59S0 HIMFTW CLR 4.76801853179931 5 7 -2.22960855995896 21 15 -0.827777777777777 1.343 20hours 15hours 18hours 108.33 13980 3.16435088468392 15220414 J Virol. 2004 "Real E, Rain JC, Battaglia V, Jallet C, Perrin P, Tordo N, Chrisment P, D'Alayer J, Legrain P, Jacob Y." Antiviral drug discovery strategy using combinatorial libraries of structurally constrained peptides. 10.1128/JVI.78.14.7410-7417.2004 Anti-RV DRAVPe02665 PPARSSPPMPPNLPPLRRRIILLRFLFH 28 P13 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RV Rhabdoviridae GFP assay [Ref:15220414]RV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Phosphoprotein Not Available 5271.9675 H235C386N60O75S0 HMTW PLR 8.10575504302978 14 13 0.780653603857022 33 9 -2.15238095238095 1.857 1.4hours 1.2hours 1.3hours 53.33 2980 0.565253863951172 15220414 J Virol. 2004 "Real E, Rain JC, Battaglia V, Jallet C, Perrin P, Tordo N, Chrisment P, D'Alayer J, Legrain P, Jacob Y." Antiviral drug discovery strategy using combinatorial libraries of structurally constrained peptides. 10.1128/JVI.78.14.7410-7417.2004 Anti-RV DRAVPe02666 KNEWGCRCNDSSDGNEWGCRCNDSSD 26 P4 INFV A matrix protein 2 P0DOF5 Experimentally Validated 381517 M Not Available Not Available Not Available Not Available Not Available Not Available 1MP6##2KIH INFV A Orthomyxoviridae ELISA [Ref:12628550]IAV:IC50=Low in MDCK cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1667.87919999999 H75C112N18O22S1 HILMFTV CDS 5.0764268875122 1 1 -1.16250342771427 6 9 0.813333333333333 0.663 3.5hours 4hours 3hours 110.67 1490 0.893350069957105 12628550 FEMS Immunol Med Microbiol. 2003 "Liu W, Li H, Chen YH." N-terminus of M2 protein could induce antibodies with inhibitory activity against influenza virus replication. 10.1016/S0928-8244(03)00009-9 Anti-INFV A DRAVPe02667 HCIYATTNDALIFSV 15 K6-10-B Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae FRET assay [Ref:22965230]HCV:IC50=>>1nM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 3009.81589999999 H132C219N40O27S6 HKMW AT 9.42748584747314 6 0 5.69765867099823 8 17 0.792 1.076 1.2hours 1hours 1.1hours 109.2 1490 0.495046889744984 22965230 J Biol Chem. 2012 "Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J." High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants. 10.1074/jbc.M112.393843 Anti-HCV DRAVPe02668 TATQCRIRGGFCRVGSCRFPHIAIGKCATFISCCGRAYEVDALNSVRTSPWLLAPGNNPH 60 AvBD3 Duck beta defensin Q9DG58 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None DHV Picornaviridae Neutralization assay [Ref:23112840]DHV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Not Available 2099.65139999999 H98C177N29O20S0 HMW CATR 11.9999677658081 5 0 4.75708461139229 7 13 0.715 0.919 1.0hours 1hours 1hours 156.5 0 0 23112840 PLoS One. 2012 "Ma D, Zhang K, Zhang M, Xin S, Liu X, Han Z, Shao Y, Liu S." "Identification, expression and activity analyses of five novel duck beta-defensins." 10.1371/journal.pone.0047743 Anti-DHV DRAVPe02669 CGRCLQRACCKYCRLKCRLILFVIF 25 C27 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RV Rhabdoviridae GFP assay [Ref:15220414]RV:IC50=22% No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Phosphoprotein Not Available 1120.3068 H50C66N15O10S2 HMTW CRL 6.89834384918212 2 0 -0.0853519894995431 5 4 -0.577777777777778 1.251 1.2hours 1hours 1.1hours 43.33 5500 4.90936946914899 15220414 J Virol. 2004 "Real E, Rain JC, Battaglia V, Jallet C, Perrin P, Tordo N, Chrisment P, D'Alayer J, Legrain P, Jacob Y." Antiviral drug discovery strategy using combinatorial libraries of structurally constrained peptides. 10.1128/JVI.78.14.7410-7417.2004 Anti-RV DRAVPe02670 CHTLPHTKC 9 - Phage display No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:18391034]SNV:IC50=35% No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 2275.5622 H95C167N31O32S0 IMWV CHT 10.2779527664184 5 2 2.73659231110456 16 4 -1.23 1.113 100hours 60hours 90hours 53.5 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade. 10.1128/AAC.01415-07 Anti-SNV DRAVPe02671 GCASRCKAKCAGRRCKGWASAFRGRCYCKCFRC 33 Mytilin-A Mytilin-A P81612 Experimentally Validated 6550 Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV 1 Herpesviridae Viral titer [Ref:23389903]HSV-1:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 899.987599999999 H45C55N9O10S0 HILMTWV CARK 5.52500019073486 0 0 -0.239898385810697 3 4 0.585714285714285 0.967 2.8hours 2.5hours 2.6hours 55.71 5500 6.11119530980205 23389903 J Pept Sci. 2013 "Galdiero S, Falanga A, Tarallo R, Russo L, Galdiero E, Cantisani M, Morelli G, Galdiero M." Peptide inhibitors against herpes simplex virus infections. 10.1002/psc.2489 Anti-HSV 1 DRAVPe02672 WSFFSNI 7 - Phage display No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HBV Hepadnaviridae Isothermal titration calorimetery [Ref:17918821]HBV:IC50=18.5µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Not Available 2273.5033 H94C162N31O33S0 HILKMTV FS 8.74354076385498 4 3 0.767503999409929 16 4 -1.145 1.004 1.0hours 1hours 1hours 53.5 0 0 17918821 J Med Chem. 2007 "Tang KF, Abdullah MP, Yusoff K, Tan WS." Interactions of hepatitis B core antigen and peptide inhibitors. 10.1021/jm070468d Anti-HBV DRAVPe02673 PSSKRFQPFQQFGRDVSDFT 20 P8 SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available Not Available Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-COV:IC50=50% No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1589.0592 H81C135N17O14S0 QHILKMTWV SF 10.4777402877807 4 0 3.75610561019329 6 7 0.515384615384615 1.296 1.3hours 1.1hours 1.2hours 150 0 0 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential. 10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02674 NQGRHFSGGALIHARFVMTAASCFQ 25 CAP3720-44ser26 Antimicrobial peptide CAP37 P20160 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None AdV Adenoviridae Direct time kill assay [Ref:19274533]ADV:IC50=Medium No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Assembly formation 957.0856 H38C58N12O12S2 HW AG 8.05824184417724 1 0 0.73929063309228 5 4 -0.277777777777777 0.654 1.2hours 1hours 1.1hours 11.11 1490 1.55680954765175 19274533 Curr Eye Res. 2009 "Gordon YJ, Romanowski EG, Shanks RM, Yates KA, Hinsley H, Pereira HA." CAP37-derived antimicrobial peptides have in vitro antiviral activity against adenovirus and herpes simplex virus type 1. 10.1080/02713680802714066 Anti-AdV DRAVPe02675 VETTVTTAQETKRGRIQTKK 20 Peptide 11 MVMp NS1 protein P03134 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None MVM Parvoviridae ELISA [Ref:9311818]MVM:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 4894.80999999999 H221C364N65O55S2 HMW TKE 10.2433977127075 8 4 3.0521982002954 24 18 -0.228571428571428 1.008 20hours 15hours 18hours 115.95 2980 0.60880810491112 9311818 J Virol. 1997 "Pujol A, Deleu L, Nuesch JP, Cziepluch C, Jauniaux JC, Rommelaere J." Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1. 10.1128/JVI.71.10.7393-7403.1997 Anti-MVM DRAVPe02676 ASLRVRIKKQ 10 SB105 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV 1 Herpesviridae Plaque assay [Ref:21576348]HSV-1:EC50=0.21¬±0.04µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 2795.3307 H127C201N36O30S2 HMTWV KR 9.02262439727783 3 1 1.74308009626448 11 14 0.92 0.79 1.2hours 1hours 1.1hours 120.4 5500 1.96756684280683 21576348 Trop Doct. 2011 "Gumbo FZ, Kandawasvika GQ, Duri K, Mapingure MP, Kurewa NE, Nathoo K, Rusakaniko S, Chirenje MZ, Stray-Pedersen B." Reduced HIV transmission at subsequent pregnancy in a resource-poor setting. 10.1258/td.2011.100458 Anti-HSV DRAVPe02677 ASLRVRIKKQ 10 SB105 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV 2 Herpesviridae Plaque assay [Ref:21576348]HSV-2:EC50=0.78±0.02µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 996.1201 H37C63N13O14S2 HMTWV KR 5.82255229949951 1 1 -0.258589604968873 5 4 -0.255555555555555 0.761 1.2hours 1hours 1.1hours 54.44 0 0 21576348 Trop Doct. 2011 "Gumbo FZ, Kandawasvika GQ, Duri K, Mapingure MP, Kurewa NE, Nathoo K, Rusakaniko S, Chirenje MZ, Stray-Pedersen B." Reduced HIV transmission at subsequent pregnancy in a resource-poor setting. 10.1258/td.2011.100458 Anti-HSV DRAVPe02678 KNGRKLCLDLQAALY 15 PD3 Thrombin-induced platelet-derived protein P83470 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None VACV Poxviridae Plaque assay [Ref:20347875]VACV:IC50=40µg/ml No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Not Available Multifunctional 3055.4008 H137C198N36O39S2 HMTWV LK 5.98954524993896 3 2 -1.08342876848449 13 13 -0.0846153846153846 0.936 1.2hours 1hours 1.1hours 78.85 8480 2.77541329438678 20347875 Antiviral Res. 2010 "Mohan KV, Rao SS, Atreya CD." Antiviral activity of selected antimicrobial peptides against vaccinia virus. 10.1016/j.antiviral.2010.03.012 Anti-VACV DRAVPe02679 ALDKAEESNSKADKVNVKLT 20 "NDVFz20-L5,12A peptide" NDV fusion protein (HR2) P12572 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None NDV Paramyxoviridae Fusion assay [Ref:9527912]NDV:IC50=35µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Fusion 3795.3026 H163C280N49O53S0 DHMW KA 8.43035335540771 6 5 0.766758518192617 19 16 -0.245714285714285 0.999 20hours 15hours 18hours 108.86 0 0 9527912 Virology. 1998 "Young JK, Hicks RP, Wright GE, Morrison TG." The role of leucine residues in the structure and function of a leucine zipper peptide inhibitor of paramyxovirus (NDV) fusion. 10.1006/viro.1998.9044 Anti-NDV DRAVPe02680 TKRNTNRRPQDVKFPGGGQIVGGVYL 26 HCVc11-36 HCV core protein P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref:20862261]HCV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1870.0573 H78C121N28O23S1 HMW GRV 10.9035539627075 5 1 2.84636856168572 12 3 -1.84 1.293 30hours 15hours 28hours 0 1490 0.796767029545031 20862261 PLoS One. 2010 "Sun C, Pager CT, Luo G, Sarnow P, Cate JH." Hepatitis C virus core-derived peptides inhibit genotype 1b viral genome replication via interaction with DDX3X. 10.1371/journal.pone.0012826 Anti-HCV DRAVPe02681 CDVIALLACHLNTPSFNTTHYRESWY 26 P13 Phage display No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None WNV Flaviviridae Q-PCR [Ref:17151121]WNV:IC50=Low No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Virus entry Inhibit Virus entry 3566.01109999999 H158C230N44O44S3 HMW LAC 4.751194190979 3 4 -2.16567273282702 17 13 -0.68 1.138 2.8hours 2.5hours 2.6hours 68.33 16500 4.62701868763112 17151121 J Virol. 2007 "Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E." Antiviral peptides targeting the west nile virus envelope protein. 10.1128/JVI.01840-06 Anti-WNV DRAVPe02682 WCNWHNIDPWIQLMNRTQADLAEGPPVKEC 30 S25 CSFV envelope protein (E2) P21530 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None CSFV Flaviviridae Plaque assay [Ref:21400206]CSFV:IC50=42% No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit CSFV entering 3324.562 H143C222N39O51S0 HMF PWN 4.05002841949462 1 5 -4.22399819814388 17 13 -0.1 0.851 1.1hours 30.0mins 54.0mins 104 0 0 21400206 Virus Genes. 2011 "Li X, Wang L, Zhao D, Zhang G, Luo J, Deng R, Yang Y." Identification of host cell binding peptide from an overlapping peptide library for inhibition of classical swine fever virus infection. 10.1007/s11262-011-0595-7 Anti-CSFV DRAVPe02683 CQRCGWETGVGVSGFLVRILRFVVL 25 C4 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RV Rhabdoviridae GFP assay [Ref:15220414]RV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Phosphoprotein Not Available 2160.3819 H91C156N26O33S0 CHIKMFTW VLG 6.25651798248291 4 4 -0.200258970315807 13 7 -0.875 1.116 4.4hours 20hours 10hours 83 0 0 15220414 J Virol. 2004 "Real E, Rain JC, Battaglia V, Jallet C, Perrin P, Tordo N, Chrisment P, D'Alayer J, Legrain P, Jacob Y." Antiviral drug discovery strategy using combinatorial libraries of structurally constrained peptides. 10.1128/JVI.78.14.7410-7417.2004 Anti-RV DRAVPe02684 PPSHSFRPESLERLHLLRRVLLLMRIVH 28 P24 Synthetic-Contruct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None RV Rhabdoviridae GFP assay [Ref:15220414]RV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Phosphoprotein Not Available 902.0468 H37C57N9O12S2 HMTW LRP 5.51073360443115 0 0 -0.260699367007718 3 6 1.03333333333333 0.402 1.2hours 1hours 1.1hours 65.56 1490 1.65179899756864 15220414 J Virol. 2004 "Real E, Rain JC, Battaglia V, Jallet C, Perrin P, Tordo N, Chrisment P, D'Alayer J, Legrain P, Jacob Y." Antiviral drug discovery strategy using combinatorial libraries of structurally constrained peptides. 10.1128/JVI.78.14.7410-7417.2004 Anti-RV DRAVPe02685 FNVALDQVFESIENSQALVDQSNRILSSAE 30 HRB2 hMPV fusion (F) protein Q6WB98 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None hMPV Paramyxoviridae RT PCR "[Ref:17967906]hMPV:IC50=>9,000nM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1680.8566 H72C118N21O24S0 HKMTW VLS 4.25288677215576 1 3 -2.03304974640201 10 5 -0.566666666666666 1.031 20hours 15hours 18hours 123.33 0 0 17967906 Antimicrob Agents Chemother. 2008 "Deffrasnes C, Hamelin ME, Prince GA, Boivin G." Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. 10.1128/AAC.00793-07 Anti-hMPV DRAVPe02686 AYRFNGIQVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLIT 96 sHR1 SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available Not Available Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Immunofluorescence [Ref:15150417]SARS-CoV:EC50=>50µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Fusion 4022.64549999999 H174C293N48O55S2 HMW TLVIAQ 8.90368022918701 7 5 1.7528815238976 22 13 -0.851428571428571 1.232 1.3hours 1.1hours 1.2hours 89.14 1490 0.370403009661179 15150417 Proc Natl Acad Sci U S A. 2004 "Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ." Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. 10.1073/pnas.0400576101 Anti-SARS-CoV DRAVPe02687 CNIAPASIVSRNIVYTRAQPNQDIA 25 VP4-peptide BRV capsid protein-VP4 P08713 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None BRV Reoviridae Plaque assay [Ref:9682337]BRV:IC50=200µg/ml No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 4078.57939999999 H176C298N50O59S0 HKMFTW IANV 4.65689830780029 4 6 -2.22942201893517 22 15 -0.194594594594594 0.978 20hours 15hours 18hours 134.32 0 0 9682337 Vaccine. 1998 "Ijaz MK, Nur-E-Kamal MS, Dar FK, Uduman S, Redmond MJ, Attah-Poku SK, Dent D, Babiuk LA." Inhibition of rotavirus infection in vitro and in vivo by a synthetic peptide from VP4. 10.1016/s0264-410x(97)00298-3 Anti-BRV DRAVPe02688 NRRPQDVKFPGGGQIVGGVYL 21 HCVc16-36 HCV core protein P26663 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCV Flaviviridae Luciferase assay [Ref:20862261HCV:IC50=High No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 1829.0055 H76C116N27O23S1 HMW GVR 8.24964847564697 3 2 0.755791548336709 13 2 -2.10666666666666 1.306 48.0mins 42mins 36mins 0 0 0 20862261 PLoS One. 2010 "Sun C, Pager CT, Luo G, Sarnow P, Cate JH." Hepatitis C virus core-derived peptides inhibit genotype 1b viral genome replication via interaction with DDX3X. 10.1371/journal.pone.0012826 Anti-HCV DRAVPe02689 RRLQVGGGTLKFFLT 15 peptide 57 HSV UL42 protein P10226 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HSV 1 Herpesviridae DNA polymerase assay [Ref:8380075HSV-1:IC50=12µM No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 4731.6336 H228C356N48O57S1 HIMW GLFTR 6.43772068023681 9 9 -0.249708461276961 20 17 -0.497297297297297 1.599 100hours 60hours 90hours 102.7 11000 2.32477848665205 8380075 J Virol. 1993 "Owsianka AM, Hart G, Murphy M, Gottlieb J, Boehme R, Challberg M, Marsden HS." Inhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecific. 10.1128/JVI.67.1.258-264.1993 Anti-HSV DRAVPe02690 CTMLLFHRC 9 - Phage display No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:IC50=2.8 × 10^8 particles/μl No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L beta-3 integrins Not Available 1838.0863 H87C121N18O23S1 HIKMTWV LFC 5.87859554290771 1 1 -0.206001654203071 6 9 0.166666666666666 0.929 4.4hours 20hours 10hours 64.67 8480 4.61349393660134 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02691 LFGLIPSLIGGLVSAFK 17 Mucroporin Scorpion venom B9UIY3 Experimentally Validated 172552 Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "MV,SARS-CoV,IAV" "Paramyxoviridae,Coronaviridae,Orthomyxoviridae" Plaque assay "[Ref:21620914]MV:EC50=3.52µm in Vero cells,SARS-CoV:EC50=7.12µM in MDCK cells, IAV:EC50=1.03µM inMDCK cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Replication 629.7492 H25C37N7O7S2 HMTWV LGIF 8.04528369903564 1 0 0.738301631993281 3 3 -0.166666666666666 0.875 1.2hours 1hours 1.1hours 0 1490 2.36602126687894 21620914 Peptides. 2011 "Li Q, Zhao Z, Zhou D, Chen Y, Hong W, Cao L, Yang J, Zhang Y, Shi W, Cao Z, Wu Y, Yan H, Li W." "Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses." 10.1016/j.peptides.2011.05.015 "Anti-MV,Anti-SARS-CoV,Anti-IAV" DRAVPe02692 CQLPAERWC 9 - Phage display No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay [Ref:15919886]SNV:IC50=9.1 × 10^8 particles/μl No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L beta-3 integrins Not Available 2584.891 H122C172N24O35S1 HILKMFTWV CAR 4.05002841949462 0 6 -6.03096177194726 11 11 0.113636363636363 0.99 20hours 15hours 18hours 97.27 11000 4.25549858775476 15919886 J Virol. 2005 "Larson RS, Brown DC, Ye C, Hjelle B." Peptide antagonists that inhibit Sin Nombre virus and hantaan virus entry through the beta3-integrin receptor. 10.1128/JVI.79.12.7319-7326.2005 Anti-SNV DRAVPe02693 KVDISSQISSMNQSLQQSKDYIKEAQRLLDTVNPSL 37 NiV FC2 NiV fusion glycoprotein Q9IH63 Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HeV,NiV" Paramyxoviridae Immunofluorescence [Ref:16026621]HeV:IC50=17.59nM inHela Cells: NiV:IC50=13.08nM in Hela Cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Fusion Not Available 1857.2022 H88C138N23O20S0 CYOU QKSL 9.99396953582763 2 0 1.73198038805714 10 8 0.505555555555555 0.683 100hours 60hours 90hours 113.33 1490 0.802282056310293 16026621 Virol J. 2005 "Bossart KN, Mungall BA, Crameri G, Wang LF, Eaton BT, Broder CC." Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein. 10.1186/1743-422X-2-57 "Anti-NiV,Anti-HeV" DRAVPe02694 TSSMRGVYYPDEIFRSDTLYL 21 P1 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 34–54 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 2513.775 C113H127N27O15S NCNVOU SYL 4.555 2 3 -1.6 8 9 -0.39 0.644 7.2hours 6hours 6.5hours 69.524 4470 2.12857142857143 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02695 KSNVVRGWVFGSTMNNKSQS 20 P2 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 94–113 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1895.0815 H86C125N25O23S0 DOYVOU VN 8.50358943939209 4 2 0.848190022559939 9 6 -1.26666666666666 1.364 1.1hours 1hours 1hours 52 2980 1.57249173716275 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02696 YKGYQPIDVVRDLPSGFNTL 20 P3 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 197–216 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 4595.9751 H206C310N49O69S0 COU VY 4.12011089324951 4 9 -6.16867647522656 26 15 -0.502439024390243 0.953 100hours 60hours 90hours 87.8 2980 0.648393417100976 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02697 TDAVDCSQNPLAELKCSVKSF 21 P4 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 273–293 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 983.0831 H38C56N14O12S2 RNWMNYOU CS 6.89834384918212 2 0 -0.0853519894995431 6 3 -0.433333333333333 0.832 1.2hours 1hours 1.1hours 32.22 0 0 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02698 KGIYQTSNFRVVPSGDVVRF 20 P5 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 297–316 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1943.0848 H81C127N29O26S0 ANDCMWYOU FV 6.75533695220947 4 3 -0.148701214402215 11 4 -1.85999999999999 1.459 1.1hours 1hours 1hours 71.33 1490 0.766821911220756 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02699 TKFPSVYAWERKKISNCVAD 20 P6 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 332–351 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 1753.0103 H79C127N23O21S0 CQMNOU K 8.74786014556885 2 1 0.761903075263511 8 7 -0.406666666666666 1.113 5.5hours 10hours 6hours 117.33 5500 3.13746017350839 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02700 YNYKYRYLRHGKLRPFERDI 20 P7 S1 of SARS-CoV spike protein P59594 Experimentally Validated 694009 S Not Available 436–455 Not Available AY274119.3 Genomic RNA "Chromosome:21,492 - 25,259" 1WNC##1ZV7 SARS-CoV Coronaviridae Syncitia assay [Ref:15811330]SARS-CoV:IC50=inhibiti SRS-CoV in HEK293T cells No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit Virus entry 8740.7551 H378C625N109O126S0 ADCMWOU KY 6.31989345550537 7 7 -0.231998960926694 48 32 -0.18125 0.87 1.4hours 1.2hours 1.3hours 113.37 0 0 15811330 FEBS Lett. 2005 "Lu W, Wu XD, Shi MD, Yang RF, He YY, Bian C, Shi TL, Yang S, Zhu XL, Jiang WH, Li YX, Yan LC, Ji YY, Lin Y, Lin GM, Tian L, Wang J, Wang HX, Xie YH, Pei G, Wu JR, Sun B." Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential.  10.1016/j.febslet.2005.02.070 Anti-SARS-CoV DRAVPe02701 QKKIRVRLSA 10 SB101 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1546.93 H73C129N19O16S0 CDEFGHIMNPQRSW AKLTVY 10.3016771316528 5 0 4.78988058186008 6 8 2.142 1.216 4.4 hours 20 hours 10 hours 111.43 1490 0.963192970475485 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02702 QKKIRVRL 8 SB102 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1633.71 H64C98N18O27S2 AFIMNQRTWY CDEGHKLPSV 4.10050144195556 2 5 -4.46449712695888 11 4 -1.13 102 1.9 hours 2 hours 1.8 hours 45.33 0 0 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02703 QKKIRVRWSA 10 SB103 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1271.53 H166C277N48O55S0 CFHMPW ADEGIKLNQRSTVY 8.37935886383056 5 4 0.768196334887896 21 14 -0.35 0.963 1.3 hours 1.1 hours 1.2 hours 105.71 1490 0.387385007425443 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02704 NKKIRVRL 8 SB104 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1540.72 H64C111N23O20S0 CDEFHKLMQWY AGINPRSTV 11.9999677658081 2 0 1.7600816143893 9 6 2.66 0.62 1.4 hours 1.2 hours 1.3 hours 97.33 0 0 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02705 ASLRVRIKKQ 10 SB105 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCMV,MCMV" Herpesviridae EGFP expression "[Ref:20083141]HCMV:IC50=0.23 μM in HELFs cells,MCMV:IC50=0.67μM in NIH3T3 cells,The IC50 and IC90 concentrations for HCMV replication were 0.22 and 0.77 μM for SB105" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1488.89 H72C127N17O15S0 CDEFGHIMNPQRSW AKLTVY 10.1768663406372 4 0 3.75510660919429 5 8 0.66 1.117 1.3 hours 1.1 hours 1.2 hours 156.92 1490 17396 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02706 ASLRVRIKK 9 SB105_A10 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None "HCMV,MCMV" Herpesviridae EGFP expression "[Ref:20083141]HCMV:IC50=0.25 μM in HELFs cells,IC50= 0.98 μM in NIH3T3 cells,The IC50 and IC90 concentrations for HCMV replication were 0.29 and 14 μM" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1077.32 H47C74N14O10S2 DEFGHIKMPQSTY ACLNRVW 8.7210254 1 0 0.740289634091281 2 7 1.7777 0.964 1.2 hours 1 hours 1.1 hours 130 5500 5.10524509167814 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02707 FKKIRVRL 8 SB106 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1059.35 H50C88N16O8S0 ACDEGHMNPQSTWY FIKLRV 11.9999677658081 4 0 3.75808361239129 4 4 -0.1875 1.599 1.1 hours 30 mins 54 mins 133.75 0 0 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02708 QKKIRVRISA 10 SB107 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1683.78 H74C104N16O26S1 ACGKNQRTVW DEFHILMPSY 45002841949462 1 4 -4.14417105169563 9 5 -0.67 137 1.1 hours 30 mins 54 mins 55.71 1490 0.884908818460837 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02709 QKKIRVRLSW 10 SB108 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1741.9 H72C121N24O25S0 CFHKMPSVWY ADEGILNQRT 4.67912235260009 2 3 -1.23317670072443 10 5 -0.89 1.118 48 mins 42 mins 36 mins 110.67 0 0 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02710 QKKIRVRFSA 10 SB109 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1232.49 H113C167N27O35S1 ACHKNQW DEFGILMPRSTVY 4.55544071197509 2 3 -1.59976842457747 12 9 -0.39 0.888 7.2 hours 6 hours 6.5 hours 69.52 4470 1.77820217713209 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02711 QKKIRFRLSA 10 SB110 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1242.29 H50C80N17O19S0 CDEFHIKLMRSWY AGNPQTV 5.52500019073486 0 0 -0.239898385810697 9 6 0.1 0.302 30 hours 15 hours 28 hours 52.67 0 0 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02712 QKKIRIRLSA 10 SB111 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1626.73 H68C105N25O21S0 CDEFIKLMQVY AGHNPRSTW 11.9999677658081 3 0 2.456 11 4 -1.12 0.87 20 hours 15 hours 18 hours 20 5500 3.38101257761268 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02713 QKKIRWRLSA 10 SB112 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1285.56 H152C241N41O43S0 CIMQW ADEFGHKLNPRSTVY 9.69625453948974 5 2 1.82207679832579 18 12 -0.13 0.884 100 hours 60 hours 90 hours 91 1490 0.44493499440009 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02714 QKKFRVRLSA 10 SB113 Synthetic Construct No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None HCMV Herpesviridae EGFP expression No MIC is available in the Article No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Linear Free Free None L Membrane Inhibit the replication of GCV-resistant strains of HCMV 1504.85 H71C123N17O17S0 CDFGHIMNPQRSW AEKLTVY 9.82564258575439 4 1 2.7579170711675 6 7 0.1 1.229 1.3 hours 1.1 hours 1.2 hours 126.92 1490 0.990128551247226 20083141 Antiviral Res. 2010 "Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G." Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparan sulfate. 10.1016/j.antiviral.2010103 Anti-HCMV DRAVPe02715 CNSSSPTAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=61%, p Value=04 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1505.69 H60C106N22O20S1 FHIKLMVW CS 10.8352174758911 3 1 1.79597634799492 10 5 -0.46 0.765 4.4 hours 20 hours 10 hours 65.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02716 CPSHYTQAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=34%, p Value=0.2771 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 951.14 H37C60N10O12S3 FIKLMVW CS 5.51141567230224 0 0 -0.259700366008717 5 4 0.32 0.416 1.2 hours 1 hours 1.1 hours 32.22 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02717 CQPHLPWHC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=68%, p Value=0.3193 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1660.85 H67C115N23O23S1 FIKMTV CS 8.74553928375244 3 2 0.763013836303355 10 5 -1.73 0.985 1.1 hours 1 hours 1 hours 46 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02718 CSPYAKHNC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=50%, p Value=0208 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1225.46 H51C90N20O12S1 FILMTVW CH 11.9999677658081 4 0 2.84625680164488 7 4 -0.58 1.104 3.5 hours 4 hours 3 hours 80 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02719 CYATTLGAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=45%, p Value=0483 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1820.123 H75C136N26O23S1 FHIKMVW CT 10.4793519973754 5 0 4.74619462019428 13 4 -1.29 158 30 hours 15 hours 28 hours 51.76 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02720 CNKQFSAAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=48%, p Value=0.2084 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1725.94 H71C114N22O23S2 HILMTVW CA 4.57755107879638 3 4 -1.24633533294933 8 7 -0.5 153 1.1 hours 1 hours 1 hours 65.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02721 CHSLRNAFC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=56%, p Value=0835 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1906.11 H80C118N28O22S2 IKMTVW CH 6.92409191131591 5 3 2 10 5 -1.44 1.37 1 hours 1 hours 1 hours 19.33 1490 0.781695769882196 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02722 CHVLDPHLC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=21%, p Value=0.5428 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1267.29 H54C80N12O22S0 FIKMTW CH 4.500284 0 4 -4.23472464201695 5 7 0.16 0.682 1.1 hours 1 hours 1 hours 97.5 1490 1.17573228591631 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02723 CQATTARNC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=78%, p Value=0.1741 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 660.82 H27C50N10O6S1 FHIKLMVW CT 11008368 2 0 1.75909261 4 2 -0.58 165 5.5 hours 10 hours 6 hours 65 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02724 CTDNALKAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=15%, p Value=0.1885 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 938.08 H159C265N56O46S1 FHIMVW CA 11.9999677658081 8 1 6.49743944488518 28 6 -1.4 15 30 hours 18 hours 25 hours 376 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02725 CPGHHLSHC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=48%, p Value=0.5794 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 990.12 H124C198N36O40S1 FIKMTVW CH 6.67007846832275 6 4 -0.36163872244312 18 7 -0.968 1.21 1.9 hours 2 hours 1.8 hours 70 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02726 CKPSTSGQC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=45%, p Value=0151 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 910.03 H171C286N48O56S0 FHILMVW CS 4.86373538970947 4 5 -1.23293318084274 21 15 6.11 0.852 1.3 hours 1.1 hours 1.2 hours 127.22 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02727 CLPTPHHVC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=41%, p Value=0002 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1006.21 H83C116N19O22S1 FIKMW CH 4.42658672332763 1 3 -2.22792942105694 8 7 -0.86 0.983 48 mins 42 mins 36 mins 52 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02728 CDLLLPGRC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=35%, p Value=NA inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 989.02 H150C196N41O38S0 FHIKMTVW CL 8.74553928375244 3 2 0.763013836303355 17 8 -1.332 1.381 1.3 hours 1.1 hours 1.2 hours 15.6 16500 5.1490609454712 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02729 CQWPGQSGC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=60%, p Value=0982 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 909.1 H35C58N10O11S3 FHIKLMTV CQ 8.583707 1 0 0.739300632992282 6 3 -0.24 0.582 1.2 hours 1 hours 1.1 hours 0 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02730 CTQSGLLSC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=61%, p Value=0063 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 911.06 H144C209N34O38S1 FHIKMVW CL 6.78716678619384 2 1 -0.117828464949483 14 15 0.71 0.652 4.4 hours 20 hours 10 hours 87.24 6990 2.27280649136945 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02731 CSTTNATWC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=36%, p Value=0.6621 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1963.33 H92C145N29O18S0 FHIKLMV CS 11.7443506240844 7 0 5.84324979874788 10 5 -1.26 1.591 1.1 hours 30 mins 54 mins 52 1490 0.758913000251002 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02732 CKSFTTTRC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=61%, p Value=0005 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1930 H37C55N11O12S2 HILMVW CS 5.51141567230224 0 0 -0.259700366008717 7 2 -0.87 0.616 1.2 hours 1 hours 1.1 hours 0 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02733 CKHHNWWTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=12%, p Value=0.8981 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1617.93 H66C118N24O18S2 FILMV CS 11.6990293502807 3 1 1.76119237542914 7 8 0.34 0.738 30 hours 15 hours 28 hours 97.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02734 CVMSKHQHC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=30%, p Value=0.4882 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1072.28 H174C294N47O56S1 FILTW CS 8.8860649 7 6 0.755691985870815 22 13 -0.75 1.222 20 hours 15 hours 18 hours 100.29 1490 0.373287141262602 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02735 CQGSPYRHC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=59%, p Value=0717 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 805.94 H31C57N13O9S1 FIKLMTVW CS 10.6191921 3 0 2.74819262219229 6 2 -1.2 1.111 1.2 hours 1 hours 1.1 hours 12.5 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02736 CYRTQFTQC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=39%, p Value=0.3021 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 896.98 H33C53N10O14S2 HIKLMVW CS 45002841949462 0 1 -1.25857960506887 4 5 0.478 0.482 1.2 hours 1 hours 1.1 hours 54.44 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02737 CLVRNLAWC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=83%, p Value=0.2326 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1017.24 H42C66N10O12S3 FHIKMT CS 5.51073360443115 0 0 -0.260699367007718 2 7 1.18 0.614 1.2 hours 1 hours 1.1 hours 97.78 1490 1.46474299707848 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02738 CNPMHSRTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=44%, p Value=0563 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1070.15 H42C60N13O15S2 FIKLVW CS 5.51141567230224 0 0 -0.259700366008717 6 3 -0.94 0.891 1.2 hours 1 hours 1.1 hours 0 5500 5.13943233194453 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02739 CNSPKGKPC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=53%, p Value=0.6765 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1528.87 H76C119N17O15S0 FHILMTVW CS 10.1768663406372 4 0 3.75510660919429 5 8 0.32 1.212 1.3 hours 1.1 hours 1.2 hours 82.31 1490 0.97457089447294 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02740 CQTTNWNTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=74%, p Value=0.4673 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1070.16 H180C273N45O52S0 FHIKLMV CS 4.65684146881103 4 6 -2.23142002093317 18 14 -0.73125 1.3 20 hours 15 hours 18 hours 109.69 13980 3.56687739478949 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02741 CTFHSPRFC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=43%, p Value=0.9021 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 912.4 H35C59N9O14S2 IKLMVW CS 5.51141567230224 0 0 -0.259700366008717 6 3 0.38 0.279 1.2 hours 1 hours 1.1 hours 43.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02742 CTTHISQTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=9%, p Value=0.5428 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1280.47 H55C95N19O15S0 FKLMVW CS 11.9999677658081 3 0 2.45912745841859 10 2 -1 0.818 1.9 hours 2 hours 1.8 hours 48.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02743 CYKMDNHTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=19%, p Value=1 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 855.97 H37C63N11O11S0 FILVW CS 5.83636417388916 1 1 -0.238787624770853 4 4 0.199999999999999 0.699 1.1 hours 1 hours 1 hours 122.5 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02744 CERLNLPQC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=14%, p Value=0.1709 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1696.81 H84C99N19O19S0 FHIKMTVW CS 4.50028 0 1 -1.23977662586985 5 7 -0.967 1.512 1.4 hours 1.2 hours 1.3 hours 56.67 23490 13.8435768926716 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02745 CLMGSSHSC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=32%, p Value=0038 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1006.2 H40C68N13O12S2 FIKTVW CS 8.5837 1 0 0.739300632992282 4 5 -2.47 0.998 1.2 hours 1 hours 1.1 hours 97.78 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02746 CTYPYPKFC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=64%, p Value=0053 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1340.43 H63C83N15O17S0 HILMVW CS 5.99994678497314 1 1 -0.240094926734491 7 5 -1.15 0.927 2.8 hours 3 hours 2.5 hours 16.67 4470 3.33472939379693 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02747 CSQWLQGS 8 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=22%, p Value=0011 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 2263.56 H106C153N23O29S1 FHIKMTV CS 9.11094608306885 2 0 1.72009139586013 10 10 0.305 0.777 100 hours 60 hours 90 hours 53.5 2980 1.31650701883789 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02748 CGPSLRGVC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=45%, p Value=0006 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1067.28 H48C84N14O12S0 FHIKMTW CS 8.74773120880127 2 1 0.760213374230145 6 4 0.199999999999999 0.856 20 hours 15 hours 18 hours 146 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02749 CTPLSTLQC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=40%, p Value=0142 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1404.73 H66C115N17O15S0 FHIKMVW CS 10.1768663406372 4 0 3.75510660919429 6 7 0.15 182 1.3 hours 1.1 hours 1.2 hours 112.31 1490 1.60695 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02750 CHADQLPMC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=39%, p Value=0138 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1246.5 H56C96N19O12S0 FIKTVW CS 11.9999677658081 4 0 3.75808361239129 6 4 -0.82 1.463 48 mins 42 mins 36 mins 88 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02751 CFSSARLSC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=13%, p Value=0.8836 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 973.13 H144C232N44O44S2 HIKMTVW CS 6.49137668609619 5 4 -0.444156206367342 17 15 -0.46 0.837 1.9 hours 2 hours 1.8 hours 67.5 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02752 CHPSKALQC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=13%, p Value=0095 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 951.12 H37C63N12O12S2 FIMTVW CS 8.5837 1 0 0.739300632992282 4 5 0.167 0.806 1.2 hours 1 hours 1.1 hours 65.56 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02753 CKSTFSPNC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=65%, p Value=0.3406 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 986.13 H141C208N34O51S2 HILMVW CS 4.5002 1 7 -6.16297940359521 21 9 -0.486 0.765 1.3 hours 1 hours 1 hours 48.67 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02754 CQRTTEANC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=16%, p Value=0078 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 922.1 H35C57N11O11S3 FHIKLMVW CS 6.72305240631103 1 0 -0.17252617775413 3 6 1.11 0.476 1.2 hours 1 hours 1.1 hours 54.44 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02755 CNSMWVRNC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=25%, p Value=0.1999 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1616.83 H67C114N21O22S1 FHIKLT CS 5.8065237045288 1 1 -0.264900849005004 7 8 0.46 0.649 100 hours 60 hours 90 hours 123.33 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02756 CTSAAVHMC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=68%, p Value=003 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 922.1 H121C190N32O33S0 FIKLW CS 8.43028888702392 5 4 0.765637757252772 12 10 -0.56 1.315 1.1 hours 30 mins 54 mins 93.18 6990 2.64871753189545 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02757 CTPGRSATC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=40%, p Value=0077 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 964.12 H37C62N13O12S2 FHIKLMVW C 8.72 1 0 0.740289634091281 5 4 -6.667 0.714 1.2 hours 1 hours 1.1 hours 54.44 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02758 CTGYHNNTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=16%, p Value=0001 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1089.31 H43C68N14O12S3 FIKLMVW C 6.72305240631103 1 0 -0.17252617775413 4 5 8.88 119 1.2 hours 1 hours 1.1 hours 86.67 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02759 CHQLMQNLC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=65%, p Value=0219 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1853 H78C126N23O26S1 FIKTVW C 7.9405870437622 1 0 0.449236468219587 10 8 0.18 0.563 1.9 hours 2 hours 1.8 hours 86.67 1490 0.80407477031928 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02760 CSASTESLC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=75%, p Value=0711 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 3340 H157C244N45O33S1 FHIKMVW C 11.9999677658081 5 1 4 18 10 -0.45 0.975 20 hours 15 hours 18 hours 93.93 5500 1.64622011399625 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02761 CSLRTYAAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=12%, p Value=0353 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1745 H80C119N21O20S1 FHIKMVW C 7.88649806976318 2 1 0.388407364308461 8 7 -0.14 0.941 7.2 hours 6 hours 6.5 hours 64.67 11000 6.30368952655739 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02762 CSRNHILTC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=25%, p Value=0015 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 1046.23 H69C119N17O17S0 FKMVW C 9.82564258575439 4 1 2.7579170711675 6 7 -8.46 1.237 1.3 hours 1.1 hours 1.2 hours 112.31 1490 1.08936 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02763 CFNTHTANC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=47%, p Value=0347 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 868.93 H31C50N10O14S2 IKLMVW C 5.51141567230224 0 0 -0.259700366008717 6 3 -0.15 0.356 1.2 hours 1 hours 1.1 hours 11.11 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02764 CHGSTKWAC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=39%, p Value=0011 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 992.14 H143C220N37O37S0 FILMV C 9.99435634613037 3 0 1.84526780054588 15 14 0.56 0.697 5.5 hours 10 hours 6 hours 104.48 1490 0.485575269658034 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV DRAVPe02765 CQLSLAPYC 9 - Synthetic-Construct(phage display selection of cyclic nonapeptides) No Entry Found Experimentally Validated None Not Available Not Available Not Available Not Available Not Available Not Available Not Available None SNV Bunyaviridae Focus reduction assay "[Ref:18391034]SNV:IC50=41%, p Value=0.399 inhibition in Vero E6 cells" No hemolysis information or data found in the reference(s) presented in this entry No cytotoxicity information found in the reference(s) presented No predicted structure available Cyclic Free Free None L Membrane Inhibit Virus Entry 997.19 H23C36N8O5S0 FHIKMTVW C 10.1800252914428 1 0 0.958518867678354 5 0 -1.94 0.784 20 hours 15 hours 18 hours 0 0 0 18391034 Antimicrob Agents Chemother. 2008 "Hall PR, Hjelle B, Brown DC, Ye C, Bondu-Hawkins V, Kilpatrick KA, Larson RS." Multivalent presentation of antihantavirus peptides on nanoparticles enhances infection blockade.  10.1128/AAC1415-07 Anti-SNV