Inhibition of serine proteases by a new class of cyclosulfamide-based carbamylating agents
Autor: | William C. Groutas, Todd D. Williams, Jiaying Zhong, Dengfeng Dou, Zhong Lai, Xiangdong Gan, Christopher S. Groutas, Swathi Mohan, Yi Li, Laura E. Stevenson, Kevin R. Alliston, Qingliang Yang |
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Rok vydání: | 2008 |
Předmět: |
Scaffold
Proteases Sulfonamides Serine Proteinase Inhibitors Time Factors Elastase Serine Endopeptidases Biophysics Biology Biochemistry Article Serine Pathogenesis Structure-Activity Relationship Proteinase 3 Cyclization Drug Design Structure–activity relationship Humans Leukocyte Elastase Molecular Biology |
Zdroj: | Archives of biochemistry and biophysics. 475(2) |
ISSN: | 1096-0384 |
Popis: | A new class of carbamylating agents based on the cyclosulfamide scaffold is reported. These compounds were found to be efficient time-dependent inhibitors of human neutrophil elastase (HNE). Exploitation of the three sites of diversity present in the cyclosulfamide scaffold yielded compounds which inhibited HNE but not proteinase 3 (PR 3) or bovine trypsin. The findings reported herein suggest that the introduction of appropriate recognition elements into the cyclosulfamide scaffold may lead to highly selective agents of potential value in the design of activity-based probes suitable for investigating proteases associated with the pathogenesis of chronic obstructive pulmonary disease. |
Databáze: | OpenAIRE |
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