Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/101051
Title: The toxicity of amyloid ß oligomers
Authors: Zhao, Li Na
Long, Hon Wai
Mu, Yuguang
Chew, Lock Yue
Issue Date: 2012
Source: Zhao, L. N., Long, H. W., Mu, Y., & Chew, L. Y. (2012). The Toxicity of Amyloid ß Oligomers. International Journal of Molecular Sciences, 13(6), 7303-7327.
Series/Report no.: International journal of molecular sciences
Abstract: In this review, we elucidate the mechanisms of Aβ oligomer toxicity which may contribute to Alzheimer’s disease (AD). In particular, we discuss on the interaction of Aβ oligomers with the membrane through the process of adsorption and insertion. Such interaction gives rises to phase transitions in the sub-structures of the Aβ peptide from α-helical to β-sheet structure. By means of a coarse-grained model, we exhibit the tendency of β-sheet structures to aggregate, thus providing further insights to the process of membrane induced aggregation. We show that the aggregated oligomer causes membrane invagination, which is a precursor to the formation of pore structures and ion channels. Other pathological progressions to AD due to Aβ oligomers are also covered, such as their interaction with the membrane receptors, and their direct versus indirect effects on oxidative stress and intraneuronal accumulation. We further illustrate that the molecule curcumin is a potential Aβ toxicity inhibitor as a β-sheet breaker by having a high propensity to interact with certain Aβ residues without binding to them. The comprehensive understanding gained from these current researches on the various toxicity mechanisms show promises in the provision of better therapeutics and treatment strategies in the near future.
URI: https://hdl.handle.net/10356/101051
http://hdl.handle.net/10220/11059
ISSN: 1422-0067
DOI: 10.3390/ijms13067303
Rights: © 2012 The Author(s) (published by MDPI). This paper was published in International Journal of Molecular Sciences and is made available as an electronic reprint (preprint) with permission of the author(s) (published by MDPI). The paper can be found at the following official open URL: [http://dx.doi.org/10.3390/ijms13067303]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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