Repository of Research and Investigative Information

Repository of Research and Investigative Information

Kurdistan University of Medical Sciences

Amorphous aggregation of tau in the presence of titanium dioxide nanoparticles: Biophysical, computational, and cellular studies

(2019) Amorphous aggregation of tau in the presence of titanium dioxide nanoparticles: Biophysical, computational, and cellular studies. International Journal of Nanomedicine.

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Background: Nanoparticles (NPs) when injected into the body can reach target tissues like nervous system and interact with tau proteins and neurons. This can trigger conformational changes of tau and may affect NP toxicity. Methods: In this study, we used several biophysical techniques (extrinsic and intrinsic fluorescence spectroscopy, circular dichroism (CD) spectroscopy, ultraviolet (UV)-visible spectroscopy), transmission electron microscopy (TEM) investigations, molecular docking and molecular dynamics studies, and cellular assays 3-(4,5-Dimethylthiazol-2-Yl)-2,5-Diphenyltetrazolium Bromide (MTT) and flow cytometry) to reveal how structural changes of tau protein can change the cytotoxicity of titanium dioxide (TiO 2 ) NPs against neuron-like cells (SH-SY5Y) cells. Results: It was shown that TiO 2 NPs result in hydrophilic interactions, secondary and tertiary structural changes, and the formation of amorphous tau aggregates. Conformational changes of tau increased the induced cytotoxicity by TiO 2 NPs. These data revealed that the denatured adsorbed protein on the NP surface may enhance NP cytotoxicity. Conclusion: Therefore, this study provides useful insights on the NP–protein interactions and discusses how the protein corona can increase cytotoxicity to determine the efficacy of targeted delivery of nanosystems. © 2019 Fardanesh et al.

Item Type: Article
Keywords: tau protein; titanium dioxide nanoparticle; 1-anilino-8-naphthalenesulfonate; 8 anilino 1 naphthalenesulfonic acid; benzothiazole derivative; nanoparticle; protein aggregate; tau protein; thioflavine; titanium; titanium dioxide; tryptophan, Article; bioinformatics; biophysics; cell assay; circular dichroism; controlled study; cytology; cytotoxicity; flow cytometry; human; human cell; hydrophilicity; in vitro study; mathematical computing; molecular docking; molecular dynamics; MTT assay; nonhuman; protein aggregation; protein conformation; protein interaction; protein modification; protein secondary structure; protein tertiary structure; SH-SY5Y cell line; spectrofluorometry; transmission electron microscopy; ultraviolet visible spectroscopy; apoptosis; biophysics; chemistry; tumor cell line; ultrastructure; ultraviolet spectrophotometry, Anilino Naphthalenesulfonates; Apoptosis; Benzothiazoles; Biophysical Phenomena; Cell Line, Tumor; Circular Dichroism; Humans; Molecular Docking Simulation; Molecular Dynamics Simulation; Nanoparticles; Protein Aggregates; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; tau Proteins; Titanium; Tryptophan
Page Range: pp. 901-911
Journal or Publication Title: International Journal of Nanomedicine
Volume: 14
Publisher: Dove Medical Press Ltd.
Identification Number: 10.2147/IJN.S194658
ISSN: 11769114
Depositing User: مهندس جمال محمودپور

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