General Information


DRAVP ID  DRAVPe00132

Peptide Name   vif 41-55

Sequence  RHHYESTHPRISSEV

Sequence Length  15

UniProt ID  No entry found

Taxon ID  None

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

Validation   Experimentally Validated



Origin Information


Gene Name/ID  Not Available

GenBank  Not Available

Amino Acid position  Not Available

Domain Accession ID  Not Available

Nucleotide sequence ID  Not Available

Molecular Type  Not Available

Chromosomal Position  Not available



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