General Information

General Information

DRAVP ID DRAVPe00083

Peptide Name Vpr 49-63

Sequence TYGDTWAGVEAIIRI

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:inhibit the activity of RNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of Rnase H(IC50>>200 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 Reverse Transcriptase

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 Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1.

Structure Information

PDB ID None

Predicted Structure Download DRAVPe00083

Linear/Cyclic Linear

N-terminal Modification Free

C-terminal Modification Free

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C76H117N19O23

Absent amino acids CFHKLMNPQS

Common amino acids I

Mass 1664.88

Pl 4.37

Basic residues 1

Acidic residues 2

Hydrophobic residues 7

Net charge -1

Boman Index -910

Hydrophobicity 36

Aliphatic Index 110.67

Half Life

Mammalian:7.2 hour
Yeast:>20 hour
E.coli:>10 hour

Extinction Coefficient cystines 6990

Absorbance 280nm 499.29

Polar residues 5

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