Mechanism-Based Inhibitors of Serine Proteinases Based on the Gabriel-Colman Rearrangement
| Autor: | Radhika Venkataraman, He Huang, Nadene Houser-Archield, Lee S. Chong, Jeffrey B. Epp, Jerald J. McClenahan, Rongze Kuang, Michael J. Brubaker, William C. Groutas |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Cathepsin
Cathepsin G Pancreatic Elastase Molecular Sequence Data Serine Endopeptidases Elastase Biophysics Cell Biology Cathepsins Biochemistry Molecular biology Cathepsin A Serine chemistry.chemical_compound Cathepsin O chemistry Proteinase 3 Drug Design Cathepsin L1 Leukocytes Humans Amino Acid Sequence Molecular Biology |
| Zdroj: | Biochemical and Biophysical Research Communications. 194:1491-1499 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1993.1993 |
| Popis: | Neutrophil-derived mediators such as, for example, the serine proteinase elastase, cathepsin G and proteinase 3, play a critical role in inflammatory lung disease. This report describes the design, synthesis and in vitro inhibitory activity of some novel mechanism-based inhibitors of human leukocyte elastase and cathepsin G. The design of the inhibitors is based on the Gabriel-Colman rearrangement. The behavior of the synthesized compounds toward elastase and cathepsin G with respect to inhibitory prowess, mode of interaction, specificity, etc., has been found to be dependent on the recognition and reactivity elements present in each inhibitor. |
| Databáze: | OpenAIRE |
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