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pubmed-article:9873610pubmed:abstractTextReplacement 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.lld:pubmed
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pubmed-article:9873610pubmed:articleTitleStudies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease.lld:pubmed
pubmed-article:9873610pubmed:affiliationBoehringer Ingelheim (Canada) Ltd, Bio-Méga Research Division, Laval, Québec, Canada.lld:pubmed
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