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Structural and kinetic features of amyloid β-protein fibrillogenesis

Abstract

Alzheimer's disease (AD) is an archetype of a class of diseases characterized by abnormal protein deposition. In each case, deposition manifests itself in the form of amyloid deposits composed of fibrils of otherwise normal, soluble proteins or peptides. An ever-increasing body of genetic, physiologic, and biochemical data supports the hypothesis that fibrillogenesis of the amyloid β-protein is a seminal event in Alzheimer's disease. Inhibiting Aβ fibrillogenesis is thus an important strategy for AD therapy. However, before this strategy can be implemented, a mechanistic understanding of the fibrillogenesis process must be achieved and appropriate steps selected as therapeutic targets. Following a brief introduction to AD, I review here the current state of knowledge of Aβ fibrillogenesis. Special emphasis is placed on the morphologic, structural, and kinetic aspects of this complex process.

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