General Information

General Information

DRAVP ID DRAVPe01115

Peptide Name HCVB(1484-1500)

Sequence STQRRGRTGRGRRGIYR

Sequence Length 17

UniProt ID P26663

Source Synthetic construct(derived from HCV 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=24.3±1.8 μM);
West Nile virus (WNV): inhibition of WNV helicase activity(IC50=33.6±3.5 μM);
Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=47.2±4.7 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 DRAVPe01115

Linear/Cyclic Linear

N-terminal Modification Free

C-terminal Modification Free

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C81H145N39O23

Absent amino acids ACDEFHKLMNPVW

Common amino acids R

Mass 2033.29

Pl 12.4

Basic residues 7

Acidic residues 0

Hydrophobic residues 1

Net charge 7

Boman Index -10998

Hydrophobicity -209.41

Aliphatic Index 22.94

Half Life

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

Extinction Coefficient cystines 1490

Absorbance 280nm 93.13

Polar residues 8

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