Azapeptides as inhibitors of the Hepatitis C virus NS3 serine protease

Truncation and substitution SAR studies of azapeptide-based inhibitors of the Hepatitis C virus (HCV) NS3 serine protease have been performed. These azapeptides were designed from the HCV polyprotein's NS5A-NS5B trans cleavage junction and contained an azaamino acid residue at the P1 position....

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2002-04, Vol.12 (7), p.1005-1008
Hauptverfasser:	RUMIN ZHANG, DURKIN, James P, WINDSOR, William T
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Aza Compounds - pharmacology Binding Sites Binding, Competitive Biological and medical sciences Hepacivirus - enzymology Medical sciences Models, Molecular Pharmacology. Drug treatments Serine Endopeptidases - drug effects Serine Endopeptidases - metabolism Serine Proteinase Inhibitors - pharmacology Structure-Activity Relationship Substrate Specificity - genetics Viral Nonstructural Proteins - antagonists & inhibitors Viral Nonstructural Proteins - metabolism
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Beschreibung
Zusammenfassung:	Truncation and substitution SAR studies of azapeptide-based inhibitors of the Hepatitis C virus (HCV) NS3 serine protease have been performed. These azapeptides were designed from the HCV polyprotein's NS5A-NS5B trans cleavage junction and contained an azaamino acid residue at the P1 position. These azapeptides exhibited predominantly non-acylating, competitive inhibition, contrary to classical azapeptides.
ISSN:	0960-894X 1464-3405
DOI:	10.1016/S0960-894X(02)00102-6