| Summary: | Negin Javdani,1 Sayyed Shahryar Rahpeyma,1 Younes Ghasemi,2 Jamshid Raheb1 1National Institute of Genetic Engineering and Biotechnology, Tehran, Iran; 2Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran Background: Most 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 methods: In 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.Results: According 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. Conclusion: The different concentrations of these nanoparticles and special coating of each particle had an effect on the kinetics of β-amyloid and α-synuclein fibrillations. Keywords: SPION, α-synuclein, β-amyloid, fibrillation, Alzheimer’s disease, Parkinson’s disease
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