BackgroundMost of nanoparticles are nontoxic and have high absorption capability. Therefore, nanoparticles binding can effectively restrain fibrillation of β-amyloid and α-synuclein proteins and eventually prevent the toxicity of pathogenesis peptide of Alzheimer. Super paramagnetic iron oxide nanoparticles (SPIONs) contain iron oxide core which can be connected to a special part through magnetic coating.Materials and methodsIn this study, the effect of SPIONs with different charges was simultaneously examined on the fibrillation of both β-amyloid and α-synuclein proteins by applying Thioflavin-T assay.ResultsAccording to the results of the investigation on amyloid-fibrillation mechanism in both β-amyloids and α-synucleins, it was revealed that negatively-charged nanoparticles encoded to –COOH by dextran-coating were able to have a considerable absorption decrease from 17,000–12,000 after 320 minutes delay to lag phase and decrease in binding level of thioflavin-T particles to β-sheets.ConclusionThe different concentrations of these nanoparticles and special coating of each particle had an effect on the kinetics of β-amyloid and α-synuclein fibrillations.

The data provided in this article are related to the research article entitled “Effect of Super Magnetic Nanoparticles Coated with Various Electric Charges on α-Synuclein Protein Fibrillation Process” (Javdani et al.). This article describes how electrically different charged and concentrated iron oxide nanoparticles synthesized using reverse co-precipitation method affects the fibrillation of albumin protein.

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