Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/71356
Citations
Scopus Web of Science® Altmetric
?
?
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPehere, A.en
dc.contributor.authorAbell, A.en
dc.date.issued2012en
dc.identifier.citationOrganic Letters, 2012; 14(5):1330-1333en
dc.identifier.issn1523-7060en
dc.identifier.issn1523-7052en
dc.identifier.urihttp://hdl.handle.net/2440/71356-
dc.description.abstractNew 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.en
dc.description.statementofresponsibilityAshok D. Pehere and Andrew D. Abellen
dc.language.isoenen
dc.publisherAmer Chemical Socen
dc.rightsCopyright © 2012 American Chemical Societyen
dc.subjectAldehydes; Macrocyclic Compounds; Calpain; Peptides; Protease Inhibitors; Protein Structure, Secondary; Structure-Activity Relationship; Cyclizationen
dc.titleNew β-strand templates constrained by Huisgen cycloadditionen
dc.title.alternativeNew beta-strand templates constrained by Huisgen cycloadditionen
dc.typeJournal articleen
dc.identifier.rmid0020117099en
dc.identifier.doi10.1021/ol3002199en
dc.identifier.pubid25616-
pubs.library.collectionIPAS publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]en
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.