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

Arasappan, A; Njoroge, F G; Chan, T-Y; Bennett, F; Bogen, S L; Chen, K; Gu, H; Hong, L; Jao, E; Liu, Y-T; Lovey, R G; Parekh, T; Pike, R E; Pinto, P; Santhanam, B; Venkatraman, S; Vaccaro, H; Wang, H; Yang, X; Zhu, Z; Mckittrick, B; Saksena, A K; Girijavallabhan, V; Pichardo, J; Butkiewicz, N; Ingram, R; Malcolm, B; Prongay, A; Yao, N; Marten, B; Madison, V; Kemp, S; Levy, O; Lim-Wilby, M; Tamura, S; Ganguly, A K.

Bioorg Med Chem Lett ; 15(19): 4180-4, 2005 Oct 01.

Article in English | MEDLINE | ID: mdl-16087332

ABSTRACT

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.

Subject(s)

Hepacivirus/chemistry , Serine Proteinase Inhibitors/chemistry , Viral Nonstructural Proteins/antagonists & inhibitors , Binding Sites , Crystallography, X-Ray , Molecular Structure , Protein Binding , Structure-Activity Relationship , Viral Nonstructural Proteins/chemistry

ABSTRACT

Subject(s)

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