Identification of amyloid beta in small extracellular vesicles <i>via</i> Raman spectroscopy
Meruyert Imanbekova, Sorina Suarasan, Tatu Rojalin, Rachel R. Mizenko, Silvia Hilt, Meghna Mathur, Paula Lépine, Michaël Nicouleau, Nguyen‐Vi Mohamed, Thomas M. Durcan, Randy P. Carney, John C. Voss, Sebastian Wachsmann‐Hogiu
Abstract
attributable to the Aβ peptide incorporated in sEVs produced by the Alzheimer's cell culture model. Subsequent analysis of the spectra by principal component analysis differentiated the sEVs of the Alzheimer's disease cell culture model from the control groups of sEVs. Moreover, the results indicate that Aβ associated with secreted sEVs has a α-helical secondary structure and the size of a monomer or small oligomer. Furthermore, by analyzing the lipid content of sEVs we identified altered fatty acid chain lengths in sEVs that carry Aβ that may affect the fluidity of the EV membrane. Overall, our findings provide evidence supporting the use of Raman spectroscopy for the identification and characterization of sEVs associated with potential biomarkers of neurological disorders such as toxic proteins.