General Information


DRAVP ID  DRAVPe00077

Peptide Name   Env4-4

Sequence  TNWLWYIKIFIMIV

Sequence Length  14

UniProt ID  No entry found

Source  Synthetic construct



Activity Information


Target Organism  HIV

Assay  Luciferase assay

Activity 

  • [Ref.20586421]HIV-1:inhibition of strand transfer catalyzed by integrase(IC50=1.9 µM).

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

Cytotoxicity 

  • No cytotoxicity information or data found in the reference(s) presented in this entry

Binding Target  Integrase

Mechanism  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.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe00077

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C94H138N18O18S

Absent amino acids  ACDEGHPQRS

Common amino acids  I

Mass  1840.3

Pl  8.26

Basic residues  1

Acidic residues  0

Hydrophobic residues  9

Net charge  1

Boman Index  2373

Hydrophobicity  139.29

Aliphatic Index  160

Half Life 

  •     Mammalian:7.2 hour
  •     Yeast:>20 hour
  •     E.coli:>10 hour

Extinction Coefficient cystines  12490

Absorbance 280nm  960.77

Polar residues  3



Literature Information


Literature 1

Title   Peptide HIV-1 integrase inhibitors from HIV-1 gene products.

Pubmed ID   20586421

Reference   J Med Chem. 2010 Jul 22;53(14):5356-60.

Author   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. 

DOI   10.1021/jm1003528