Repository of Research and Investigative Information

Repository of Research and Investigative Information

Kurdistan University of Medical Sciences

α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency

(2019) α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency. International Journal of Nanomedicine.

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Aim: It has been indicated that NPs may change the amyloidogenic steps of proteins and relevant cytotoxicity. Therefore, this report assigned to explore the impact of ZVFe NPs on the amyloidogenicity and cytotoxicity of α-synuclein as one of the many known amyloid proteins. Methods: The characterization of α-synuclein at amyloidogenic condition either alone or with ZVFe NPs was carried out by fluorescence, CD, UV-visible spectroscopic methods, TEM study, docking, and molecular modeling. The cytotoxicity assay of α-synuclein amyloid in the absence and presence of ZVFe NPs was also done by MTT, LDH, and flow cytometry analysis. Results: ThT fluorescence spectroscopy revealed that ZVFe NPs shorten the lag phase and accelerate the fibrillation rate of α-synuclein. Nile red and intrinsic fluorescence spectroscopy, CD, Congo red adsorption, and TEM studies indicated that ZVFe NP increased the propensity of α-synuclein into the amyloid fibrillation. Molecular docking study revealed that hydrophilic residues, such as Ser-9 and Lys-12 provide proper sites for hydrogen bonding and electrostatic interactions with adsorbed water molecules on ZVFe NPs, respectively. Molecular dynamics study determined that the interacted protein shifted from a natively discorded conformation toward a more packed structure. Cellular assay displayed that the cytotoxicity of α-synuclein amyloid against SH-SY5Y cells in the presence of ZVFe NPs is greater than the results obtained without ZVFe NPs. Conclusion: In conclusion, the existence of ZVFe NPs promotes α-synuclein fibrillation at amyloidogenic conditions by forming a potential template for nucleation, the growth of α- synuclein fibrillation and induced cytotoxicity. © 2019 Tahaei Gilan et al.

Item Type: Article
Keywords: alpha synuclein; amyloid protein; congo red; iron nanoparticle; lactate dehydrogenase; lysine; nile red; reagent; serine; unclassified drug; water; alpha synuclein; amyloid; benzothiazole derivative; iron; lactate dehydrogenase; metal nanoparticle; oxazine derivative; protein aggregate; thioflavine; tyrosine, amino acid sequence; amyloidogenicity; Article; cell assay; circular dichroism; controlled study; cytotoxicity; cytotoxicity assay; flow cytometry; human; human cell; hydrogen bond; molecular docking; molecular dynamics; molecular model; MTT assay; protein conformation; protein function; protein interaction; protein structure; SH-SY5Y cell line; spectrofluorometry; static electricity; transmission electron microscopy; ultraviolet visible spectroscopy; cell death; chemistry; kinetics; metabolism; protein secondary structure; tumor cell line; ultrastructure, alpha-Synuclein; Amyloid; Benzothiazoles; Cell Death; Cell Line, Tumor; Congo Red; Humans; Iron; Kinetics; L-Lactate Dehydrogenase; Metal Nanoparticles; Molecular Docking Simulation; Molecular Dynamics Simulation; Oxazines; Protein Aggregates; Protein Structure, Secondary; Spectrometry, Fluorescence; Tyrosine
Page Range: pp. 4637-4648
Journal or Publication Title: International Journal of Nanomedicine
Volume: 14
Identification Number: 10.2147/IJN.S212387
Depositing User: مهندس جمال محمودپور

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