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

Replacememt 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...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 1998-10, Vol.8 (19), p.2719-2724
Main Authors: Llinàs-Brunet, Montse, Bailey, Murray, Déziel, Robert, Fazal, Gulrez, Gorys, Vida, Goulet, Sylvie, Halmos, Ted, Maurice, Roger, Poirier, Martin, Poupart, Marc-André, Rancourt, Jean, Thibeault, Diane, Wernic, Dominik, Lamarre, Daniel
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Language:English
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Summary:Replacememt 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.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(98)00480-6