Succinimide and saccharin-based enzyme-activated inhibitors of serine proteases

被引：0

作者：

Martyn, DC ^{[1
]}

Moore, MJB ^{[1
]}

Abell, AD ^{[1
]}

机构：

[1] Univ Canterbury, Dept Chem, Christchurch 1, New Zealand

来源：

CURRENT PHARMACEUTICAL DESIGN | 1999年 / 5卷 / 06期

关键词：

D O I：

暂无

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The inhibition of human leukocyte elastase (HLE). and other serine proteases, by succinimide and saccharin-based compounds is reviewed. The succinimide compounds are unique in that the inactivating species is generated within the enzyme active site via a molecular rearrangement. The related saccharin derivatives also inactivate serine proteases by an enzyme-activated mechanism. Those factors effecting the potency, selectivity and stability of these important classes of inhibitor are discussed.

引用

页码：405 / 415

页数：11

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