1. Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors.
- Author
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Lee, Shin Jung C., Nam, Eunju, Lee, Hyuck Jin, Savelieff, Masha G., and Lim, Mi Hee
- Subjects
AMYLOID ,ALZHEIMER'S disease ,METASTABLE states ,OLIGOMERS ,OLIGOMERIZATION ,CLUSTERING of particles ,THERAPEUTICS - 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. [ABSTRACT FROM AUTHOR]
- Published
- 2017
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