Peroxides as oxidative enzyme inhibitors: Mechanism-based inhibition of a cysteine protease by an amino acid ozonide

被引：15
作者：
Dussault, PH [1 ]
George, AD
Trullinger, TK
机构：
[1] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA
[2] Nebraska Weslayan Univ, Dept Chem, Lincoln, NE 68504 USA
来源：
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1999年 / 9卷 / 22期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/S0960-894X(99)00563-6
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
A stable ozonide derived from Cbz-L-Phe accomplishes rapid and stoichiometric inhibition of papain at less than 100 mu M concentration under conditions where formation of the corresponding aldehyde is negligible. Oxidation of the active site thiolate by the bound peroxide is believed to lead to formation of an inactive sulfenate or sulfenic acid. Reduction of the ozonide in excess DMSO provides a convenient method for in situ generation of a peptide aldehyde. (C) 1999 Elsevier Science Ltd. All rights reserved.
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页码：3255 / 3258
页数：4
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