Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/71356
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: New β-strand templates constrained by Huisgen cycloaddition
Other Titles: New beta-strand templates constrained by Huisgen cycloaddition
Author: Pehere, A.
Abell, A.
Citation: Organic Letters, 2012; 14(5):1330-1333
Publisher: Amer Chemical Soc
Issue Date: 2012
ISSN: 1523-7060
1523-7052
Statement of
Responsibility: 
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
RMID: 0020117099
DOI: 10.1021/ol3002199
Appears in Collections:IPAS publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.