Synthesis of potent and highly selective inhibitors of human tryptase

Autor:	Wei Meng, G. A. Jacobs, William A. Schumacher, James C. Sutton, William A. Slusarchyk, Robert Zahler, Martin L. Ogletree, Gregory S. Bisacchi, Steven M. Seiler, Scott A. Bolton, Treuner Uwe D, Zulan Pi, Karen S. Hartl, Guohua Zhao, Ming-Hsing Huang
Rok vydání:	2002
Předmět:	Proteases Serine Proteinase Inhibitors Ovalbumin Clinical Biochemistry Aziridines Guinea Pigs Pharmaceutical Science Tryptase Biochemistry Piperazines Serine Structure-Activity Relationship Drug Stability Drug Discovery medicine Animals Humans Anti-Asthmatic Agents Molecular Biology chemistry.chemical_classification Serine protease biology Organic Chemistry Serine Endopeptidases Stereoisomerism Trypsin In vitro Asthma Enzyme chemistry Enzyme inhibitor biology.protein Molecular Medicine Azetidines Tryptases medicine.drug
Zdroj:	Bioorganicmedicinal chemistry letters. 12(21)
ISSN:	0960-894X
Popis:	The serine protease tryptase has been implicated in allergic and inflammatory diseases and associated with asthma. The synthesis and SAR of a series of N1-activated-4-carboxy azetidinones are described, resulting in identification of BMS-363131 (2) as a potent inhibitor of human tryptase (IC(50)1.7 nM) with high selectivity (3000-fold) for tryptase versus related serine proteases including trypsin.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aa7b9a85d2a88a95d573703b8233fc0 https://pubmed.ncbi.nlm.nih.gov/12372541 Zobrazit plný text záznamu Full Text from ScienceDirect