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  • Title: Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease.
    Author: Llinàs-Brunet M, Bailey M, Déziel R, Fazal G, Gorys V, Goulet S, Halmos T, Maurice R, Poirier M, Poupart MA, Rancourt J, Thibeault D, Wernic D, Lamarre D.
    Journal: Bioorg Med Chem Lett; 1998 Oct 06; 8(19):2719-24. PubMed ID: 9873610.
    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.
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