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Bioorg Med Chem Lett. 1998 Oct 6;8(19):2719-24.

Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease.

Author information

1
Boehringer Ingelheim (Canada) Ltd, Bio-Méga Research Division, Laval, Québec, Canada.

Abstract

Replacement of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities.

PMID:
9873610
[Indexed for MEDLINE]

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