期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 475, 期 2, 页码 115-120出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.04.020
关键词
carbamylating agents; cyclosulfamide; human neutrophil elastase; activity-based probe
资金
- NHLBI NIH HHS [R01 HL057788-06, R01 HL057788, HL 57788, R01 HL057788-05, R01 HL057788-07, R01 HL057788-08] Funding Source: Medline
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. (C) 2008 Elsevier Inc. All rights reserved.
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