Combinatorial synthesis of SSAO inhibitors using sonogashira coupling: SAR of aryl propargylic amines.

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dc.contributor.author Conn, C
dc.contributor.author Shimmon, R
dc.contributor.author Cordaro, F
dc.contributor.author Hargraves, TL
dc.contributor.author Ibrahim, P
dc.date.accessioned 2009-11-12T04:41:07Z
dc.date.issued 2001-10
dc.identifier.citation Bioorganic & medicinal chemistry letters, 2001, 11 (19), pp. 2565 - 2568
dc.identifier.issn 0960-894X
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/3210
dc.description.abstract The structure-activity relationships for semicarbazide-sensitive amine oxidase (SSAO) inhibitors based on arylpropynylamines was investigated using solution-phase combinatorial Sonogashira coupling. The results suggest that binding to the active site occurs by coordination of the amine to the proximal copper(II) and formation of a pi-complex between topaquinone and the electron-rich aryl group of the inhibitor.
dc.format Print
dc.language eng
dc.relation.isbasedon 10.1016/s0960-894x(01)00506-6
dc.title Combinatorial synthesis of SSAO inhibitors using sonogashira coupling: SAR of aryl propargylic amines.
dc.type Journal Article
dc.parent Bioorganic & medicinal chemistry letters
dc.journal.volume 19
dc.journal.volume 11
dc.journal.number 19 en_US
dc.publocation Oxford, England en_US
dc.identifier.startpage 2565 en_US
dc.identifier.endpage 2568 en_US
dc.cauo.name Chemistry, Materials and Forensic Sciences en_US
dc.personcode 910833
dc.personcode 980366
dc.description.keywords Pargyline
dc.description.keywords Amine Oxidase (Copper-Containing)
dc.description.keywords Enzyme Inhibitors
dc.description.keywords Molecular Conformation
dc.description.keywords Structure-Activity Relationship
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Faculty of Science/School of Chemistry and Forensic Science
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
utslib.collection.history Closed (ID: 3)


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