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Issue 2, 2017

Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

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Abstract

Alzheimer's disease (AD) is characterized by an imbalance between production and clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers into β-stranded fibrils via multiple oligomeric states. Among the various Aβ species, structured oligomers are proposed to be more toxic than fibrils; however, the identification of Aβ oligomers has been challenging due to their heterogeneous and metastable nature. Multiple techniques have recently helped us gain a better understanding of oligomers' assembly details and structural properties. Moreover, some progress on elucidating the mechanisms of oligomer-triggered toxicity has been made. Based on the collection of current findings, there is growing consensus that control of toxic Aβ oligomers could be a valid approach to regulate Aβ-associated toxicity, which could advance development of new diagnostics and therapeutics for amyloid-related diseases. In this review, we summarize the recent understanding of Aβ oligomers' assembly, structural properties, and toxicity, along with inhibitors against Aβ aggregation, including oligomerization.

Graphical abstract: Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

Article information


Submitted
11 Oct 2016
First published
23 Nov 2016

Chem. Soc. Rev., 2017,46, 310-323
Article type
Tutorial Review

Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

S. J. C. Lee, E. Nam, H. J. Lee, M. G. Savelieff and M. H. Lim, Chem. Soc. Rev., 2017, 46, 310 DOI: 10.1039/C6CS00731G

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