General Information


DRAVP ID  DRAVPe01879

Peptide Name   Pep19-4

Sequence  GKKYRRFRWKFKFGKWFWFG

Sequence Length  20

UniProt ID  No entry found

Source  Synthetic construct



Activity Information


Target Organism  HIV, HSV-1, HCV

Assay  luciferase infection assay

Activity 

  • [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).

Hemolytic Activity  No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity 

  • [Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL.

Binding Target  membrane

Mechanism  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.



Structure Information


PDB ID  None

Predicted Structure Download  No predicted structure available

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C141H191N37O22

Absent amino acids  ACDEHILMNPQSTV

Common amino acids  FK

Mass  2756.3

Pl  11.76

Basic residues  8

Acidic residues  0

Hydrophobic residues  8

Net charge  8

Boman Index  -4794

Hydrophobicity  -121

Aliphatic Index  0

Half Life 

  •     Mammalian:30 hour
  •     Yeast:>20 hour
  •     E.coli:>10 hour

Extinction Coefficient cystines  17990

Absorbance 280nm  946.84

Polar residues  4



Literature Information


Literature 1

Title   A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses.

Pubmed ID   22457281

Reference   J Infect Dis. 2012 Jun;205(11):1654-64.

Author   Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U.

DOI   10.1093/infdis/jis273