Literature DB >> 11909704

Azapeptides as inhibitors of the hepatitis C virus NS3 serine protease.

Rumin Zhang1, James P Durkin, William T Windsor.   

Abstract

Truncation and substitution SAR studies of azapeptide-based inhibitors of the Hepatitis C virus (HCV) NS3 serine protease have been performed. These azapeptides were designed from the HCV polyprotein's NS5A-NS5B trans cleavage junction and contained an azaamino acid residue at the P1 position. These azapeptides exhibited predominantly non-acylating, competitive inhibition, contrary to classical azapeptides.

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Year:  2002        PMID: 11909704     DOI: 10.1016/s0960-894x(02)00102-6

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  1 in total

1.  Structure-activity relationship studies on anti-HCV activity of ring-expanded ('fat') nucleobase analogues containing the imidazo[4,5-e][1,3]diazepine-4,8-dione ring system.

Authors:  Peng Zhang; Ning Zhang; Brent E Korba; Ramachandra S Hosmane
Journal:  Bioorg Med Chem Lett       Date:  2007-02-02       Impact factor: 2.823

  1 in total

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