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|Title:||New β-strand templates constrained by Huisgen cycloaddition|
|Other Titles:||New beta-strand templates constrained by Huisgen cycloaddition|
|Citation:||Organic Letters, 2012; 14(5):1330-1333|
|Publisher:||Amer Chemical Soc|
|Ashok D. Pehere and Andrew D. Abell|
|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.|
|Keywords:||Aldehydes; Macrocyclic Compounds; Calpain; Peptides; Protease Inhibitors; Protein Structure, Secondary; Structure-Activity Relationship; Cyclization|
|Rights:||Copyright © 2012 American Chemical Society|
|Appears in Collections:||IPAS publications|
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