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• W2321378571 abstract "New peptidic templates constrained into a β-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 β-strand are shown to be potent inhibitors of the protease calpain. The β-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." @default.
• W2321378571 created "2016-06-24" @default.
• W2321378571 creator A5033537928 @default.
• W2321378571 creator A5078753655 @default.
• W2321378571 date "2012-02-16" @default.
• W2321378571 modified "2023-09-26" @default.
• W2321378571 title "New β-Strand Templates Constrained by Huisgen Cycloaddition" @default.
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• W2321378571 doi "https://doi.org/10.1021/ol3002199" @default.
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