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Updated: Jul 16, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Physicochemical interactions of amyloid beta-peptide with lipid bilayers
1Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan. katsumim@pharm.kyoto-u.ac.jp
Abstract:
The aggregation and deposition onto neuronal cells of amyloid beta-peptide (Abeta) is central to the pathogenesis of Alzheimer's disease. Accumulating evidence suggests that membranes play a catalytic role in the aggregation of Abeta. This article summarizes the structures and properties of Abeta in solution and the physicochemical interaction of Abeta with lipid bilayers of various compositions. Reasons for discrepancies between results by different research groups are discussed. The importance of ganglioside clusters in the aggregation of Abeta is emphasized. Finally, a hypothetical physicochemical cascade in the pathogenesis of the disease is proposed.
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