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

Abstract

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

View correction statement:

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

Acknowledgments

This work was supported by the Presidency of Islamic Republic of Iran for Science and Technology, Iran National Science Foundation (grant number 91059044).

Disclosure

The authors report no conflicts of interest in this work.