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General Information
DRAVP ID DRAVPe01405
Peptide Name NQW (S-S)
Sequence ACFPWGNQWCGGK
Sequence Length 13
UniProt ID No entry found
Taxon ID None
Source Synthetic construct
Validation Experimentally Validated
Origin Information
Gene Name/ID Not Available
GenBank Not Available
Amino Acid position Not Available
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism HCV
Assay Surface plasmon resonance
Activity
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
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.
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.