Effect of Metals on Kinetic Pathways of Amyloid-\beta Aggregation

2017/04/26 by Francis Hane, Zoya Leonenko, Hane, Francis +1
Chemistry · Medicine · #Alzheimer's disease research and treatments #Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #Cholinesterase and Neurodegenerative Diseases #FOS: Biological sciences #FOS: Physical sciences #Molecular Sensors and Ion Detection

paper · pdf · doi:10.48550/arxiv.1704.08315

openalex publication_date 2017/04/26 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

Abstract

Metal ions, including copper and zinc, have been implicated in the pathogenesis of Alzheimers disease through a variety of mechanisms including increased amyloid \beta affinity and redox effects. Recent reports have demonstrated that the amyloid \beta monomer does not necessarily travel through a definitive intermediary en-route to a stable amyloid fibril structure. Rather, amyloid \beta 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 \beta 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 \beta misfolding leading to more neurotoxic species.

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