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    Interaction of Amyloid-beta-(1-42) Peptide and Its Aggregates with Lipid/Water Interfaces Probed by Vibrational Sum-Frequency Generation Spectroscopy

    Year: 2021

    Journal: J. Phys. Chem. B, Volume 125, OCT 14, page 11208–11218

    Authors: Strazdaite, S.; Roeters, S. J.; Sakalauskas, A.; Sneideris, T.; Kirschner, J.; Pedersen, K. B.; Schiott, B.; Jensen, F.; Weidner, T.; Smirnovas, V; Niaura, G.

    Organizations: European Union [792508]; Lundbeck Foundation [R303-2018-349]; European Research Council (ERC) [819039]; Novo Nordisk Foundation [NNF18OC0032608]

    In this study, we use surface-sensitive vibrational sum-frequency generation (VSFG) spectroscopy to investigate the interaction between model lipid monolayers and A beta(1-42) in its monomeric and aggregated states. Combining VSFG with atomic force microscopy (AFM) and thioflavin T (ThT) fluorescence measurements, we found that only small aggregates with probably beta-hairpin-like structure adsorbed to the zwitterionic lipid monolayer (DOPC). In contrast, larger aggregates with an extended beta-sheet structure adsorbed to a negatively charged lipid monolayer (DOPG). The adsorption of small, initially formed aggregates strongly destabilized both monolayers, but only the DOPC monolayer was completely disrupted. We showed that the intensity of the amide-II' band in achiral (SSP) and chiral (SPP) polarization combinations increased in time when A beta(1-42) aggregates accumulated at the DOPG monolayer. Nevertheless, almost no adsorption of preformed mature fibrils to DOPG monolayers was detected. By performing spectral VSFG calculations, we revealed a clear correlation between the amide-II' signal and the degree of amyloid aggregates (e.g., oligomers or (proto)fibrils) of various A beta(1 -42) structures. The calculations showed that only structures with a significant amyloid beta-sheet content have a strong amide-II' intensity, in line with previous Raman studies. The combination of the presented results substantiates the amide-II(') band as a legitimate amyloid marker.
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