The state of folding of individual Amyloid-β oligomers in a lipid membrane correlates with their toxicity

Arpan Dey; Sudipta Maiti

doi:10.1117/12.3012974

13 March 2024 The state of folding of individual amyloid-β oligomers in a lipid membrane correlates with their toxicity

Arpan Dey, Sudipta Maiti

Proceedings Volume PC12849, Single Molecule Spectroscopy and Superresolution Imaging XVII; PC1284908 (2024) https://doi.org/10.1117/12.3012974
Event: SPIE BiOS, 2024, San Francisco, California, United States

Abstract

Oligomers of disease-causing amyloid proteins (such as Alzheimer’s Amyloid beta or ’Aβ’) are generally amphiphilic and their interactions with lipid membranes are possibly the origin of their toxicity. However, how oligomers of different stoichiometries or different mutants differ in their interaction with the membrane, and how these differences correlate with their toxicity, has largely remained beyond the reach of existing experimental techniques. Here we use Q-SLIP, a single-molecule tool that can resolve the surface exposure of different parts of individual oligomers, and different radical-labeled lipids that act as quenchers, to address these questions.

Conference Presentation

Citation Download Citation

Arpan Dey and Sudipta Maiti "The state of folding of individual amyloid-β oligomers in a lipid membrane correlates with their toxicity", Proc. SPIE PC12849, Single Molecule Spectroscopy and Superresolution Imaging XVII, PC1284908 (13 March 2024); https://doi.org/10.1117/12.3012974

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