General Information

General Information

DRAVP ID DRAVPe01129

Peptide Name JEV(1959-1975)

Sequence AAQRRGRVGRNPNQVGD

Sequence Length 17

UniProt ID P27395

Source Synthetic construct(derived from JEV NS3 helicase protein)

Activity Information

Target Organism HCV,WNV,JEV

Assay Helicase assay

Activity

[Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=442±17.7 μM);
West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);
Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM).

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

Cytotoxicity No cytotoxicity information found in the reference(s) presented

Binding Target NTPase/helicase

Mechanism The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism.

Structure Information

PDB ID None

Predicted Structure Download DRAVPe01129

Linear/Cyclic Linear

N-terminal Modification Free

C-terminal Modification Free

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C73H127N33O24

Absent amino acids CEFHIKLMSTWY

Common amino acids R

Mass 1851.02

Pl 12

Basic residues 4

Acidic residues 1

Hydrophobic residues 4

Net charge 3

Boman Index -7824

Hydrophobicity -154.71

Aliphatic Index 45.88

Half Life

Mammalian:4.4 hour
Yeast:>20 hour
E.coli:>10 hour

Extinction Coefficient cystines 0

Absorbance 280nm 0

Polar residues 5

Literature Information

Literature 1

Title Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI).

Pubmed ID 18479669

Reference Biochem Pharmacol. 2008 Jul 1;76(1):28-38.

Author Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A.

DOI 10.1016/j.bcp.2008.03.018