Alzheimer’s disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-β (Aβ), a peptide of 39–42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein. There is a growing body of evidence that Aβ aggregates are ordered oligomers and the cause rather than a product of AD. The analysis of the assembly pathway of Aβ in vitro and biochemical characterization of Aβ deposits isolated from AD brains indicate that Aβ oligomerization occurs via distinct intermediates, including oligomers of 3–50 Aβ monomers, annular oligomers, protofibrils, fibrils and plaques. Of these, the most toxic species appear to be small Aβ oligomers. This article reviews the current knowledge of the mechanism of Aβ assembly in vivo and in vitro, as well as the influence of inherited amino acid replacements in Aβ and experimental conditions on Aβ aggregation. Challenges regarding the reproducible handling of the Aβ peptide for in vitro assembly studies are discussed.

Keywords:
Amyloid-β, Alzheimer’s disease, Protein misfolding, Neurodegeneration, Oligomers
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© 2007 S. Karger AG, Basel
2007
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