Cu 2 + -induced modification of the kinetics of A�(1-42)channels
Date
2003
Authors
Bahadi, Randa
Farrelly, Peter
Kenna, Bronwyn
Curtain, Cyril
Masters, Colin
Cappai, Roberto
Barnham, Kevin
Kourie, Joseph
Journal Title
Journal ISSN
Volume Title
Publisher
American Physiological Society
Abstract
We found that the amyloid β peptide Aβ(1-42) is capable of interacting with membrane and forming heterogeneous ion channels in the absence of any added Cu2+ or biological redox agents that have been reported to mediate Aβ(1-42) toxicity. The Aβ(1-42)-
Description
Keywords
Keywords: amyloid beta protein; chelating agent; clioquinol; copper ion; prion protein; zinc ion; amyloid beta protein (1 42); amyloid beta-protein (1-42); chelating agent; clioquinol; copper; ion channel; peptide fragment; Alzheimer disease; article; binding site; Calcium homeostasis; Ion channel pathologies; Membrane injuries; Neurodegenerative diseases; Transitional metals
Citation
Collections
Source
American Journal of Physiology - Cell Physiology
Type
Journal article