| Literature DB >> 12643923 |
Wei Han1, Zilun Hu, Xiangjun Jiang, Zelda R Wasserman, Carl P Decicco.
Abstract
Using a tetrapeptide-based alpha-ketoamide template, various amines and amino acids were incorporated to explore the prime side of the HCV NS3 protease catalytic site. Glycine carboxylic acid was found to be the most effective prime group. Further optimization yielded an inhibitor with IC(50) of 0.060 microM.Entities:
Mesh：
Substances：
Year: 2003 PMID： 12643923 DOI： 10.1016/s0960-894x(03)00031-3
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823