Journal
ORGANIC LETTERS
Volume 14, Issue 5, Pages 1330-1333Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ol3002199
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- Australian Research Council
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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.
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