title: Effect of metals on kinetic pathways of amyloid-β aggregation.
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.
authors: Department of Biology, University of Waterloo, 200 University Ave, Waterloo, ON N2L 3G1, Canada. francishane@gmail.com.
authors: Francis
authors: F
authors: Hane
authors: Department of Biology, University of Waterloo, 200 University Ave, Waterloo, ON N2L 3G1, Canada. zleonenk@uwaterloo.ca.
authors: Zoya
authors: Z
authors: Leonenko
mesh_terms: D000544:Alzheimer Disease / Q000235:genetics / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D006801:Humans; D007700:Kinetics; D008670:Metals / Q000378:metabolism*; D066329:Protein Aggregates; D017510:Protein Folding
chemical_list: D016229:Amyloid beta-Peptides; D008670:Metals; D066329:Protein Aggregates