Physicochemical interactions of amyloid beta-peptide with lipid bilayers.
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.
Matsuzaki
Katsumi
K
Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan. katsumim@pharm.kyoto-u.ac.jp
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D005732:Gangliosides / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D008956:Models, Chemical
D016229:Amyloid beta-Peptides; D005732:Gangliosides; D008051:Lipid Bilayers