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

Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation

1email and 1,2,* email
Received: 7 December 2013; in revised form: 4 January 2014 / Accepted: 7 January 2014 / Published: 10 January 2014
(This article belongs to the Special Issue Metal Binding Proteins)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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
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MDPI and ACS Style

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

AMA Style

Hane F, Leonenko Z. Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation. Biomolecules. 2014; 4(1):101-116.

Chicago/Turabian Style

Hane, Francis; Leonenko, Zoya. 2014. "Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation." Biomolecules 4, no. 1: 101-116.

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