General Information


DRAVP ID  DRAVPe00126

Peptide Name   VMI5

Sequence  SVSVGMKPSPRP

Sequence Length  12

UniProt ID  No entry found

Source  Synthetic construct(phage display)



Activity Information


Target Organism  HIV

Assay  Affinity binding assay

Activity 

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

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  DRAVPe00126

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C53H92N16O16S

Absent amino acids  ACDEFHILNQTWY

Common amino acids  PS

Mass  1241.47

Pl  11

Basic residues  2

Acidic residues  0

Hydrophobic residues  2

Net charge  2

Boman Index  -1930

Hydrophobicity  -47.5

Aliphatic Index  48.33

Half Life 

  •     Mammalian:1.9 hour
  •     Yeast:>20 hour
  •     E.coli:>10 hour

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  4



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