General Information

General Information

DRAVP ID DRAVPe00089

Peptide Name Vpr 33-47

Sequence HFPRIWLHSLGQHIY

Sequence Length 15

UniProt ID No entry found

Source Synthetic construct(derived from HIV-1 viral protein R (Vpr))

Activity Information

Target Organism HIV

Assay Dot-blot binding assay

Activity

[Ref.17490682]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=187 µM);inhibition of strand transfer catalyzed by integrase(IC50=41 µM);inhibition of disintegration catalyzed by integrase(IC50=73 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 The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and thus inhibit the replication of HIV-1.

Structure Information

PDB ID None

Predicted Structure Download DRAVPe00089

Linear/Cyclic Linear

N-terminal Modification Free

C-terminal Modification Free

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C92H130N26O19

Absent amino acids ACDEKMNTV

Common amino acids H

Mass 1904.21

Pl 8.77

Basic residues 4

Acidic residues 0

Hydrophobic residues 6

Net charge 4

Boman Index -1205

Hydrophobicity -21.33

Aliphatic Index 104

Half Life

Mammalian:3.5 hour
Yeast:10 min
E.coli:>10 hour

Extinction Coefficient cystines 6990

Absorbance 280nm 499.29

Polar residues 3

Literature Information

Literature 1

Title Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr).

Pubmed ID 17490682

Reference J Mol Biol. 2007 Jun 22;369(5):1230-43.

Author Gleenberg IO, Herschhorn A, Hizi A.

DOI 10.1016/j.jmb.2007.03.073