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• W2945006902 abstract "The understanding of the interaction between the membrane of neurons and amyloid-β peptides is of crucial importance to shed light on the mechanism of toxicity in Alzheimer’s disease. This paper describes how supercritical angle fluorescence spectroscopy was applied to monitor in real-time the interaction between a supported lipid bilayer (SLB) and the peptide. Different forms of amyloid-β (40 and 42 amino acids composition) were tested, and the interfacial fluorescence was measured to get information about the lipid integrity and mobility. The results show a concentration-dependent damaging process of the lipid bilayer. Prolonged interaction with the peptide up to 48 h lead to an extraction and clustering of lipid molecules from the surface and a potential disruption of the bilayer, correlated with the formation of peptide aggregates. The natural diffusion of the lipid was slightly hindered by the interaction with amyloid-β(1–42) and closely related to the oligomerization of the peptide. The adsorption and desorption of Amyloid-β was also characterized in terms of affinity. Amyloid-β(1–42) exhibited a slightly higher affinity than amyloid-β(1–40). The former was also more prone to aggregate and to adsorb on the bilayer as oligomer." @default.
• W2945006902 created "2019-05-29" @default.
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• W2945006902 date "2019-05-24" @default.
• W2945006902 modified "2023-09-27" @default.
• W2945006902 title "Amyloid-β Peptide–Lipid Bilayer Interaction Investigated by Supercritical Angle Fluorescence" @default.
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• W2945006902 doi "https://doi.org/10.1021/acschemneuro.9b00264" @default.
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