Show simple item record Folk, DS Franz, KJ
dc.coverage.spatial United States 2011-06-21T17:25:57Z 2010-04-14
dc.identifier.citation J Am Chem Soc, 2010, 132 (14), pp. 4994 - 4995
dc.description.abstract The intersection of the amyloid cascade hypothesis and the implication of metal ions in Alzheimer's disease progression has sparked an interest in using metal-binding compounds as potential therapeutic agents. In the present work, we describe a prochelator SWH that is enzymatically activated by beta-secretase to produce a high affinity copper chelator CP. Because beta-secretase is responsible for the amyloidogenic processing of the amyloid precursor protein, this prochelator strategy imparts disease specificity toward copper chelation not possible with general metal chelators. Furthermore, once activated, CP efficiently sequesters copper from amyloid-beta, prevents and disassembles copper-induced amyloid-beta aggregation, and diminishes copper-promoted reactive oxygen species formation.
dc.format.extent 4994 - 4995
dc.language eng
dc.language.iso en_US en_US
dc.relation.ispartof J Am Chem Soc
dc.relation.isversionof 10.1021/ja100943r
dc.subject Amyloid Precursor Protein Secretases
dc.subject Amyloid beta-Peptides
dc.subject Chelating Agents
dc.subject Copper
dc.subject Organometallic Compounds
dc.subject Reactive Oxygen Species
dc.subject Structure-Activity Relationship
dc.title A prochelator activated by beta-secretase inhibits Abeta aggregation and suppresses copper-induced reactive oxygen species formation.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US 2010-4-14 en_US
duke.description.endpage + en_US
duke.description.issue 14 en_US
duke.description.startpage 4994 en_US
duke.description.volume 132 en_US
dc.relation.journal Journal of the American Chemical Society en_US
pubs.issue 14
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Chemistry
pubs.publication-status Published
pubs.volume 132
dc.identifier.eissn 1520-5126

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