General Information


DRAVP ID  DRAVPe01405

Peptide Name   NQW (S-S)

Sequence  ACFPWGNQWCGGK

Sequence Length  13

UniProt ID  No entry found

Source  Synthetic construct



Activity Information


Target Organism  HCV

Assay  Surface plasmon resonance

Activity 

  • [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=6.0 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  RNA-dependent RNA polymerase

Mechanism  The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe01405

Linear/Cyclic  Cyclic

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  Disulfide bond between Cys2 and Cys10

Stereochemistry  L



Physicochemical Information


Formula  C66H88N18O16S2

Absent amino acids  DEHILMRSTVY

Common amino acids  G

Mass  1453.66

Pl  8.1

Basic residues  1

Acidic residues  0

Hydrophobic residues  4

Net charge  1

Boman Index  -290

Hydrophobicity  -45.38

Aliphatic Index  7.69

Half Life 

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

Extinction Coefficient cystines  11125

Absorbance 280nm  927.08

Polar residues  6



Literature Information


Literature 1

Title   Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase.

Pubmed ID   12951030

Reference   Virology. 2003 Aug 15;313(1):158-69.

Author   Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P.

DOI   10.1016/s0042-6822(03)00313-1