General Information


DRAVP ID  DRAVPe01118

Peptide Name   HCV(1493-1500)

Sequence  RGRRGIYR

Sequence Length  8

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=313±11.3 μM);
  • West Nile virus (WNV): inhibition of WNV helicase activity(IC50=397±10.6 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  DRAVPe01118

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C43H76N20O10

Absent amino acids  ACDEFHKLMNPQSTVW

Common amino acids  R

Mass  1033.2

Pl  12

Basic residues  4

Acidic residues  0

Hydrophobic residues  1

Net charge  4

Boman Index  -5302

Hydrophobicity  -195

Aliphatic Index  48.75

Half Life 

  •     Mammalian:1 hour
  •     Yeast:2 min
  •     E.coli:2 min

Extinction Coefficient cystines  1490

Absorbance 280nm  212.86

Polar residues  3



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