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

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.

journal_name

Bioorg Med Chem Lett

authors

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

doi

10.1016/s0960-894x(98)00480-6

subject

Has Abstract

pub_date

1998-10-06 00:00:00

pages

2719-24

issue

19

eissn

0960-894X

issn

1464-3405

pii

S0960894X98004806

journal_volume

8

pub_type

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