General Information


DRAVP ID  DRAVPe00132

Peptide Name   vif 41-55

Sequence  RHHYESTHPRISSEV

Sequence Length  15

UniProt ID  No entry found

Source  Synthetic construct(derived from HIV-1 Vif protein)



Activity Information


Target Organism  HIV

Assay  ELISA

Activity 

  • [Ref.12480936]HIV-1:inhibit vif-vif binding.

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  Vif proteins

Mechanism  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.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe00132

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C78H119N27O25

Absent amino acids  ACDFGKLMNQW

Common amino acids  HS

Mass  1834.97

Pl  7.03

Basic residues  5

Acidic residues  2

Hydrophobic residues  2

Net charge  3

Boman Index  -6139

Hydrophobicity  -152.67

Aliphatic Index  45.33

Half Life 

  •     Mammalian:1 hour
  •     Yeast:2 min
  •     E.coli:2 min

Extinction Coefficient cystines  1490

Absorbance 280nm  106.43

Polar residues  5



Literature Information


Literature 1

Title   Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.

Pubmed ID   12480936

Reference   J Biol Chem. 2003 Feb 21;278(8):6596-602.

Author   Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H.

DOI   10.1074/jbc.M210164200