  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.
