Hepatitis C virus NS3-4A serine protease inhibitors: SAR of P'2 moiety with improved potency

Autor:	A, Arasappan, F G, Njoroge, T-Y, Chan, F, Bennett, S L, Bogen, K, Chen, H, Gu, L, Hong, E, Jao, Y-T, Liu, R G, Lovey, T, Parekh, R E, Pike, P, Pinto, B, Santhanam, S, Venkatraman, H, Vaccaro, H, Wang, X, Yang, Z, Zhu, B, Mckittrick, A K, Saksena, V, Girijavallabhan, J, Pichardo, N, Butkiewicz, R, Ingram, B, Malcolm, A, Prongay, N, Yao, B, Marten, V, Madison, S, Kemp, O, Levy, M, Lim-Wilby, S, Tamura, A K, Ganguly
Rok vydání:	2005
Předmět:	Structure-Activity Relationship Binding Sites Serine Proteinase Inhibitors Molecular Structure Hepacivirus Viral Nonstructural Proteins Crystallography X-Ray Protein Binding
Zdroj:	Bioorganicmedicinal chemistry letters. 15(19)
ISSN:	0960-894X
Popis:	We have discovered that introduction of appropriate amino acid derivatives at P'2 position improved the binding potency of P3-capped alpha-ketoamide inhibitors of HCV NS3 serine protease. X-ray crystal structure of one of the inhibitors (43) bound to the protease revealed the importance of the P'2 moiety.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::58a75cc30fd2fcc888c1c51c0f4669e1 https://pubmed.ncbi.nlm.nih.gov/16087332 Zobrazit plný text záznamu Full Text from ScienceDirect