2. Academic Validation
  3. Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

  • Bioorg Med Chem Lett. 2001 Jan 22;11(2):203-6. doi: 10.1016/s0960-894x(00)00625-9.
A Johansson 1,  I Hubatsch,  E Akerblom,  G Lindeberg,  S Winiwarter,  U H Danielson,  A Hallberg
Affiliations

Affiliation

  • 1 Department of Organic Pharmaceutical Chemistry, Uppsala University, BMC, Sweden.
PMID: 11206459 DOI: 10.1016/s0960-894x(00)00625-9
Abstract

Structure activity relationships (SARs) of product-based inhibitors of hepatitis C virus NS3 protease were evaluated using an in vitro assay system comprising the native bifunctional full-length NS3 (protease-helicase/NTPase). The results were compared to previously reported data derived from the corresponding NS3 protease domain assay. Shortening the length of the Protease Inhibitors from hexapeptides to tripeptides revealed that the decrease in potency was much less when determined in the assay system with the full-length NS3 protein. Disagreements in SARs at different positions (P5 P2) were also discovered. Taken together, the results suggest that the impact of the helicase domain upon protease inhibitor binding is substantial.

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