Amyloid β interaction with model cell membranes – What are the toxicity-defining properties of amyloid β?

Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is followed by aggregation via different pathways in which structurally different amyloid β oligomers can be formed. The respective toxic actions of these structurally diverse oligomers can vary significantly. Linking a particular toxic action to a structurally unique kind of amyloid β oligomers and resolving their toxicity-determining feature remains challenging because of their transient stability and heterogeneity. Moreover, the lipids that make up the membrane affect amyloid β oligomers' behavior, thus adding to the problem's complexity. The present review compares and analyzes the latest results to improve understanding of amyloid β oligomers' interaction with lipid bilayers.

P.P. acknowledges the support of the Polish National Science Centre , grant No. OPUS12 2016/23B/ST4/02791 . The research activity of D. M. was supported by funds from the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 711859 and by financial resources for science in the years 2017–2021 awarded by the Polish Ministry of Science and Higher Education for the implementation of an international co-financed project. J.L. acknowledges the support of the Natural Sciences and Engineering Research Council of Canada (NSERC) grant ( RG-03958 ).