Effect of Metals on Kinetic Pathways of Amyloid-b{eta} Aggregation

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