Inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamides
Inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamides
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DOI：
10.1016/j.bmc.2007.10.041
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发表时间：
2008-01-15
影响因子：
3.5
通讯作者：
Groutas, William C.
中科院分区：
文献类型：
--
作者：
Li, Yi;Yang, Qingliang;Groutas, William C.
研究了一系列1,2,5-噻二唑烷-3- 1,1二氧化物基磺酰胺与中性粒细胞衍生丝氨酸蛋白酶的相互作用。氨基酸成分的性质，被认为是面向S'亚位，对酶的选择性有深远的影响。这一系列化合物被发现是有效的，时间依赖性的人中性粒细胞弹性酶（HNE）抑制剂，对中性粒细胞蛋白酶3 （PR 3）和组织蛋白酶G （Cat G）没有任何抑制活性。这些研究的结果表明，利用HNE和PR 3的S'亚位的差异可以导致HNE的高选择性抑制剂。(c) 2007 Elsevier Ltd.版权所有。
The interaction of a series of 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamides with neutrophil-derived serine proteases was investigated. The nature of the amino acid component, believed to be oriented toward the S' subsites, had a profound effect on enzyme selectivity. This series of compounds were found to be potent, time-dependent inhibitors of human neutrophil elastase (HNE) and were devoid of any inhibitory activity toward neutrophil proteinase 3 (PR 3) and cathepsin G (Cat G). The results of these studies demonstrate that exploitation of differences in the S' subsites of HNE and PR 3 can lead to highly selective inhibitors of HNE. (c) 2007 Elsevier Ltd. All rights reserved.