DRAVP ID  DRAVPe00130

Peptide Name   vif 155-166

Sequence  KPKQIKPPLPSV

Sequence Length  12

UniProt ID  No entry found

Taxon ID  None

Source  Synthetic construct(derived from the proline-enriched C terminus of Vif)

Validation   Experimentally Validated

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

Target Organism  HIV

Assay  ELISA

Activity 

• [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.

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

Cytotoxicity 

• [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM.

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.

PDB ID  None

Predicted Structure Download  DRAVPe00130

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L

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