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Electric Field Disrupts Amyloid Aggregation; Potential Non-invasive Therapy for Alzheimer's Disease.

ACS Chemical Neuroscience 2019 Februrary 2
Aggregation of β-amyloid peptides is a key event in the formative stages of Alzheimer's disease. Promoting folding and inhibiting aggregation was reported as an effective strategy in reducing Aβ-elicited toxicity. This study experimentally investigates the influence of the external electric field (EF) and magnetic field (MF) of varying strengths on the in-vitro fibrillogenesis of hydrophobic core sequence Aβ16-22 and its parent peptide Aβ1-42. Biophysical methods such as ThT fluorescence, static light scattering, Circular Dichroism (CD) and Infrared spectroscopy suggest that EF has a stabilizing effect on the secondary structure, initiating a conformational switch of Aβ16-22 and Aβ1-42 from beta to non-beta conformation. This observation was further corroborated by Dynamic Light Scattering (DLS) and Transmission Electron Microscopic studies. To mimic in-vivo conditions, we repeated ThT fluorescence assay with Aβ1-42 in human Cerebrospinal Fluid (CSF) to verify EF mediated modulation. Self-seeding of Aβ1-42 and cross-seeding with Aβ1-40 to verify auto-catalytic amplification of self-assembly as a result of secondary nucleation, also yield comparable results in EF exposed and unexposed samples. Aβ elicited toxicity of EF treated samples in two neuroblastoma cell lines (SH-SY5Y and IMR-32) and human embryonic kidney cell line (HEK293) were found to be 15-38% less toxic than the EF untreated ones under identical conditions. Experiments with fluorescent-labelled Aβ1-42 to correlate reduced cytotoxicity and cell internalization, suggest comparatively lesser uptake of the EF treated peptides. Our results provide a scientific roadmap for future non-invasive, therapeutic solutions for the treatment of Alzheimer's disease.

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