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Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process

Authors Javdani N, Rahpeyma SS, Ghasemi Y, Raheb J

Received 10 October 2018

Accepted for publication 13 December 2018

Published 23 January 2019 Volume 2019:14 Pages 799—808


Checked for plagiarism Yes

Review by Single-blind

Peer reviewers approved by Dr Govarthanan Muthusamy

Peer reviewer comments 2

Editor who approved publication: Prof. Dr. Anderson Oliveira Lobo

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

Corrigendum for this paper has been published.

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