期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 10, 期 15, 页码 1771-1773出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0960-894X(00)00340-1
关键词
-
We have utilized previously known substrate and inhibitor specificity profiles for the lysosomal cysteine protease, cathepsin L, to design a new series of putative inhibitors of this enzyme, based on di- and tri-peptidyl alpha-keto-beta-aldehydes. Kinetic evaluation of those compounds revealed Z-Phe-Tyr(OBut)-COCHO, with a K-i=0.6 nM, to be the most potent, synthetic reversible inhibitor of cathepsin L reported to date. (C) 2000 Elsevier Science Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据