TIO2 NANOPARTICLES AS POTENTIAL PROMOTING AGENTS OF FIBRILLATION OF α-SYNUCLEIN, A PARKINSON’S DISEASE-RELATED PROTEIN

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MOHAMMADI SOHEYLA; NIKKHAH MARYAM

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

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Journal: Iranian Journal of Biotechnology Year:2017 | Volume:15 | Issue:2 Page(s): 0-0

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Title

TIO2 NANOPARTICLES AS POTENTIAL PROMOTING AGENTS OF FIBRILLATION OF α-SYNUCLEIN, A PARKINSON’S DISEASE-RELATED PROTEIN

Author(s)

MOHAMMADI SOHEYLA | NIKKHAH MARYAM | Issue Writer Certificate

Keywords

α-SYNUCLEIN (αS)

NANOPARTICLES (NPS)

PARKINSON’S DISEASE (PD)

TITANIUM DIOXIDE NANOPARTICLES (TIO2-NPS)

Abstract

Background: In recent years, nanomaterials have been widely used in large quantities which make people be more frequently exposed to the chemically synthesized nanoparticles (NPs). When NPs are introduced into an organism, they may interact with a variety of cellular components with yet largely unknown pathological consequences.Objective: It was found that NPs enhance the rate of protein fi brillation in the brain by decreasing the lag time for nucleation. Protein fibrillation is implicated in the pathogenesis of the several neurodegenerative diseases such as Parkinson’s disease (PD). a-Synuclein (aS) is natively an unfolded protein which is involved in the pathogenesis of PD. In the present study, we have analyzed the effects of three different NPs on αS fi brillation.Materials and Methods: αS protein expression and purification was done and fibrils formation was induced in the absence or presence of the three types of NPs (i. e., TiO2, SiO2, and SnO2). The enhancement of the fluorescence emission of Thioflavin T (ThT) and transmission electron microscopy (TEM) were used to monitor the appearance and growth of the fibrils. The adsorption of αS monomers on the surface of NPs was investigated by tyrosine fluorescence emission measurements.Results: We found that TiO2-NPs enhances αS fibril formation even at a concentration of 5 mg.mL-1, while the two other NPs show no significant effect on the kinetics of the fi brillation. Intrinsic tyrosine emission measurement has confirmed that the TiO2-NPs interact with αS fi brillation products. It is suggested that TiO2-NPs may enhance the nucleation of aS protein that leads to protein fi bril formation.Conclusion: The fi brillization process of aS protein is profoundly aff ected by the presence of TiO2-NPs. This finding unveils the neurotoxicity potential of the TiO2-NPs, which may be considered as a probable risk for PD.

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APA: Copy

MOHAMMADI, SOHEYLA, & NIKKHAH, MARYAM. (2017). TIO2 NANOPARTICLES AS POTENTIAL PROMOTING AGENTS OF FIBRILLATION OF α-SYNUCLEIN, A PARKINSON’S DISEASE-RELATED PROTEIN. IRANIAN JOURNAL OF BIOTECHNOLOGY, 15(2), 0-0. SID. https://sid.ir/paper/693361/en

Vancouver: Copy

MOHAMMADI SOHEYLA, NIKKHAH MARYAM. TIO2 NANOPARTICLES AS POTENTIAL PROMOTING AGENTS OF FIBRILLATION OF α-SYNUCLEIN, A PARKINSON’S DISEASE-RELATED PROTEIN. IRANIAN JOURNAL OF BIOTECHNOLOGY[Internet]. 2017;15(2):0-0. Available from: https://sid.ir/paper/693361/en

IEEE: Copy

SOHEYLA MOHAMMADI, and MARYAM NIKKHAH, “TIO2 NANOPARTICLES AS POTENTIAL PROMOTING AGENTS OF FIBRILLATION OF α-SYNUCLEIN, A PARKINSON’S DISEASE-RELATED PROTEIN,” IRANIAN JOURNAL OF BIOTECHNOLOGY, vol. 15, no. 2, pp. 0–0, 2017, [Online]. Available: https://sid.ir/paper/693361/en

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