The Bsmoc group as a novel scaffold for the design of irreversible inhibitors of cysteine proteases
| Autor: | Luísa M. D. R. S. Martins, Rui Moreira, Cláudio M. Soares, Jim Iley, Rita C. Guedes |
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| Přispěvatelé: | Repositório da Universidade de Lisboa |
| Rok vydání: | 2006 |
| Předmět: |
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Molecular Proteases Stereochemistry Clinical Biochemistry Chemistry Organic Pharmaceutical Science Chemistry Medicinal Cysteine Proteinase Inhibitors Biochemistry Cathepsin B chemistry.chemical_compound Carbamic acid Drug Discovery Molecular Biology Pancreatic elastase Serine protease biology Chemistry Organic Chemistry Hydrogen Bonding General Medicine Kinetics Papain Enzyme inhibitor Drug Design Michael reaction biology.protein Molecular Medicine Cysteine |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| ISSN: | 0960-894X |
| DOI: | 10.1016/j.bmcl.2006.02.007 |
| Popis: | Carbamate and ester derivatives of the 1,1-dioxobenzo[b]thiophen-2-ylmethyloxycarbonyl (Bsmoc) scaffold react readily with thiols via a Michael addition at rates not significantly affected by the nature of the carboxylic or carbamic acid leaving group. These Michael acceptors are irreversible inhibitors of the cysteine proteases papain and human liver cathepsin B, displaying first-order kinetics with respect to inhibitor concentration. In contrast, none of the Bsmoc derivatives inhibited porcine pancreatic elastase, a serine protease. (C) 2006 Elsevier Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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