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Biomolecules 2014, 4(1), 101-116; doi:10.3390/biom4010101
Review

Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation

1
 and
1,2,*
1 Department of Biology, University of Waterloo, 200 University Ave, Waterloo, ON N2L 3G1, Canada 2 Department of Physics and Astronomy, University of Waterloo, 200 University Ave, Waterloo, ON N2L 3G1, Canada
* Author to whom correspondence should be addressed.
Received: 7 December 2013 / Revised: 4 January 2014 / Accepted: 7 January 2014 / Published: 10 January 2014
(This article belongs to the Special Issue Metal Binding Proteins)
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Abstract

Metal ions, including copper and zinc, have been implicated in the pathogenesis of Alzheimer’s disease through a variety of mechanisms including increased amyloid-β affinity and redox effects. Recent reports have demonstrated that the amyloid-β monomer does not necessarily travel through a definitive intermediary en-route to a stable amyloid fibril structure. Rather, amyloid-β misfolding may follow a variety of pathways resulting in a fibrillar end-product or a variety of oligomeric end-products with a diversity of structures and sizes. The presence of metal ions has been demonstrated to alter the kinetic pathway of the amyloid-β peptide which may lead to more toxic oligomeric end-products. In this work, we review the contemporary literature supporting the hypothesis that metal ions alter the reaction pathway of amyloid-β misfolding leading to more neurotoxic species.
Keywords: amyloid-metal effects; amyloid aggregation; multiple pathways kinetics; Alzheimer’s disease amyloid-metal effects; amyloid aggregation; multiple pathways kinetics; Alzheimer’s disease
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Hane, F.; Leonenko, Z. Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation. Biomolecules 2014, 4, 101-116.

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