The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease.
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Ontoria JM, Di Marco S, Conte I, Di Francesco ME, Gardelli C, Koch U, Matassa VG, Poma M, Steinkuhler C, Volpari C, Harper S
The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease.
J Med Chem. 2004 Dec 16;47(26):6443-6.
- PubMed ID
- 15588076 [ View in PubMed]
- Abstract
The design of a series of peptidomimetic inhibitors of the hepatitis C virus NS3 protease is described. These inhibitors feature an indoline-2-carboxamide as a novel heterocyclic replacement for the P3 amino acid residue and N-terminal capping group of tripeptide based inhibitors. The crystal structure of the ternary NS3/NS4A/inhibitor complex for the most active molecule in this series highlights its suitability as an N-terminal capping group of a dipeptide inhibitor of the NS3 protease.