期刊
ORGANIC LETTERS
卷 14, 期 5, 页码 1330-1333出版社
AMER CHEMICAL SOC
DOI: 10.1021/ol3002199
关键词
-
资金
- Australian Research Council
New peptidic templates constrained into a beta-strand geometry by linking acetylene and azide containing P-1 and P-3 residues of a tripeptide by Huisgen cycloaddition are presented. The conformations of the macrocycles are defined by NMR studies and those that best define a beta-strand are shown to be potent inhibitors of the protease calpain. The beta-strand templates presented and defined here are prepared under optimized conditions that should be suitable for targeting a range of proteases and other applications requiring such a geometry.
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