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Cu 2 + -induced modification of the kinetics of A�(1-42)channels

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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

URI

http://hdl.handle.net/1885/86075

Collections

Open Access Research

Source

American Journal of Physiology - Cell Physiology

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

Restricted until

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