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PLoS One. 2017 Aug 2;12(8):e0182194. doi: 10.1371/journal.pone.0182194. eCollection 2017.

Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease.

Author information

1
Department of Biology, University of Waterloo, Waterloo, Canada.
2
Waterloo Institute of Nanotechnology, University of Waterloo, Waterloo, Canada.
3
Department of Physiology and Biophysics, Dalhousie University, Halifax, Canada.
4
Department of Physics and Astronomy, University of Waterloo, Waterloo, Canada.
5
Department of Basic Sciences, New York University College of Dentistry, New York, New York, United States of America.

Abstract

Amyloid-beta peptides (Aβ), implicated in Alzheimer's disease (AD), interact with the cellular membrane and induce amyloid toxicity. The composition of cellular membranes changes in aging and AD. We designed multi-component lipid models to mimic healthy and diseased states of the neuronal membrane. Using atomic force microscopy (AFM), Kelvin probe force microscopy (KPFM) and black lipid membrane (BLM) techniques, we demonstrated that these model membranes differ in their nanoscale structure and physical properties, and interact differently with Aβ1-42. Based on our data, we propose a new hypothesis that changes in lipid membrane due to aging and AD may trigger amyloid toxicity through electrostatic mechanisms, similar to the accepted mechanism of antimicrobial peptide action. Understanding the role of the membrane changes as a key activating amyloid toxicity may aid in the development of a new avenue for the prevention and treatment of AD.

PMID:
28767712
PMCID:
PMC5540602
DOI:
10.1371/journal.pone.0182194
[Indexed for MEDLINE]
Free PMC Article

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