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      International Journal of Nanomedicine (submit here)

      This international, peer-reviewed Open Access journal by Dove Medical Press focuses on the application of nanotechnology in diagnostics, therapeutics, and drug delivery systems throughout the biomedical field. Sign up for email alerts here.

      105,621 Monthly downloads/views I 7.033 Impact Factor I 10.9 CiteScore I 1.22 Source Normalized Impact per Paper (SNIP) I 1.032 Scimago Journal & Country Rank (SJR)

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      Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity

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          Abstract

          Aim

          Among therapeutic proposals for amyloid-associated disorders, special attention has been given to the exploitation of nanoparticles (NPs) as promising agents against aggregation.

          Methods

          In this paper, the inhibitory effect of cerium oxide (CeO 2) NPs against α-synuclein (α-syn) amyloid formation was explored by different methods such as Thioflavin T (ThT) and 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence spectroscopy, Congo red adsorption assay, circular dichroism (CD) spectroscopy, transmission electron microscopy (TEM), and bioinformatical approaches. Also, the cytotoxicity of α-syn amyloid either alone or with CeO 2 NPs against neuron-like cells (SH-SY5Y) was examined using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), flow cytometry, and quantitative real-time polymerase chain reaction (Bax and Bcl-2 gene expression) assays.

          Results

          ThT and ANS fluorescence assays indicated that CeO 2 NPs inhibit the formation of aggregated species and hydrophobic patches of α-syn in amyloidogenic conditions, respectively. Congo red and CD assays demonstrated that CeO 2 NPs reduce the formation of amyloid species and β-sheets structures of α-syn molecules, respectively. TEM investigation also confirmed that CeO 2 NPs limited the formation of well-defined fibrillary structures of α-syn molecules. Molecular docking and dynamic studies revealed that CeO 2 NPs could bind with different affinities to α-syn monomer and amyloid species and fibrillar structure of α-syn is disaggregated in the presence of CeO 2 NPs. Moreover, cellular assays depicted that CeO 2 NPs mitigate the cell mortality, apoptosis, and the ratio of Bax/Bcl-2 gene expression associated with α-syn amyloids.

          Conclusion

          It may be concluded that CeO 2 NPs can be used as therapeutic agents to reduce the aggregation of proteins and mitigate the occurrence of neurodegenerative diseases.

          Most cited references28

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          Oxidative stress: A major pathogenesis and potential therapeutic target of antioxidative agents in Parkinson's disease and Alzheimer's disease.

          Tianfang Jiang, Qian Sun, Shengdi Chen (2016)
          Oxidative stress reflects an imbalance between the overproduction and incorporation of free radicals and the dynamic ability of a biosystem to detoxify reactive intermediates. Free radicals produced by oxidative stress are one of the common features in several experimental models of diseases. Free radicals affect both the structure and function of neural cells, and contribute to a wide range of neurodegenerative diseases, including Parkinson's disease and Alzheimer's disease. Although the precise mechanisms that result in the degeneration of neurons and the relevant pathological changes remain unclear, the crucial role of oxidative stress in the pathogenesis of neurodegenerative diseases is associated with several proteins (such as α-synuclein, DJ-1, Amyloid β and tau protein) and some signaling pathways (such as extracellular regulated protein kinases, phosphoinositide 3-kinase/Protein Kinase B pathway and extracellular signal-regulated kinases 1/2) that are tightly associated with the neural damage. In this review, we present evidence, gathered over the last decade, concerning a variety of pathogenic proteins, their important signaling pathways and pathogenic mechanisms associated with oxidative stress in Parkinson's disease and Alzheimer's disease. Proper control and regulation of these proteins' functions and the related signaling pathways may be a promising therapeutic approach to the patients. We also emphasizes antioxidative options, including some new neuroprotective agents that eliminate excess reactive oxygen species efficiently and have a certain therapeutic effect; however, controversy surrounds some of them in terms of the dose and length of therapy. These agents require further investigation by clinical application in patients suffering Parkinson's disease and Alzheimer's disease.
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            Redox-active radical scavenging nanomaterials.

            William Self, Ajay Karakoti, Sanjay Singh … (2010)
            Reactive oxygen and nitrogen species play a critical role in many degenerative diseases and in aging. Nanomaterials, especially modified fullerenes and cerium oxide nanoparticles, have been shown to effectively protect mammalian cells against damage caused by increased reactive oxygen or nitrogen species, likely through their direct reaction with superoxide radical, since each of these materials has been shown to act as effective superoxide dismutase mimetics in vitro. This critical review discusses the chemistry of these nanomaterials and the context in which their radical scavenging activities have been studied in biological model systems. Current studies are focused on determining the uptake, metabolism, distribution, toxicity and fate of these nanomaterials in cell and animal model systems. Ultimately if shown to be safe, these nanomaterials have the potential to be used to reduce the damaging effects of radicals in biological systems (101 references).
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              Ultra-fast FFT protein docking on graphics processors.

              Craig W Ritchie, Vishwesh Venkatraman (2010)
              Modelling protein-protein interactions (PPIs) is an increasingly important aspect of structural bioinformatics. However, predicting PPIs using in silico docking techniques is computationally very expensive. Developing very fast protein docking tools will be useful for studying large-scale PPI networks, and could contribute to the rational design of new drugs. The Hex spherical polar Fourier protein docking algorithm has been implemented on Nvidia graphics processor units (GPUs). On a GTX 285 GPU, an exhaustive and densely sampled 6D docking search can be calculated in just 15 s using multiple 1D fast Fourier transforms (FFTs). This represents a 45-fold speed-up over the corresponding calculation on a single CPU, being at least two orders of magnitude times faster than a similar CPU calculation using ZDOCK 3.0.1, and estimated to be at least three orders of magnitude faster than the GPU-accelerated version of PIPER on comparable hardware. Hence, for the first time, exhaustive FFT-based protein docking calculations may now be performed in a matter of seconds on a contemporary GPU. Three-dimensional Hex FFT correlations are also accelerated by the GPU, but the speed-up factor of only 2.5 is much less than that obtained with 1D FFTs. Thus, the Hex algorithm appears to be especially well suited to exploit GPUs compared to conventional 3D FFT docking approaches. http://hex.loria.fr/ and http://hexserver.loria.fr/.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Nanomedicine
                Journal ID (iso-abbrev): Int J Nanomedicine
                Journal ID (publisher-id): IJN
                Journal ID (pmc): intjnano
                Title: International Journal of Nanomedicine
                Publisher: Dove
                ISSN (Print): 1176-9114
                ISSN (Electronic): 1178-2013
                Publication date (Electronic): 29 August 2019
                Publication date Collection: 2019
                Volume: 14
                Pages: 6989-7000
                Affiliations
                [1 ]Department of Biochemistry and Biophysics, Faculty of Advanced Science and Technology, Tehran Medical Sciences, Islamic Azad University , Tehran, Iran
                [2 ]Department of Molecular Genetics, Faculty of Advanced Science and Technology, Tehran Medical Sciences, Islamic Azad University , Tehran, Iran
                [3 ]Department of Biology, College of Science, Salahaddin University-Erbil , Kurdistan Region, Iraq
                [4 ]Department of Medical Analysis, Faculty of Science, Tishk International University , Erbil, Iraq
                [5 ]Department of Nanomedicine, Faculty of Advanced Science and Technology, Tehran Medical Sciences, Islamic Azad University , Tehran, Iran
                [6 ]Department of Animal Science, Faculty of Agriculture, University of Tabriz , Tabriz, Iran
                [7 ]Department of Biology, College of Science, Cihan University-Erbil , Kurdistan Region, Iraq
                [8 ]Department of Biology, College of Education, Salahaddin University-Erbil , Kurdistan Region, Iraq
                [9 ]Anatomy, Biology and Histology Unit, College of Medicine, University of Duhok , Kurdistan Region, Iraq
                [10 ]Department of Brain and Cognitive Sciences, Cell Science Research Center, Royan Institute for Stem Cell Biology and Technology, ACECR , Tehran, Iran
                [11 ]Department of Mechanical and Industrial Engineering, College of Engineering, Qatar University , Doha 2713, Qatar
                [12 ]Biomedical Research Center, Qatar University , Doha 2713, Qatar
                Author notes
                Correspondence: Mojtaba FalahatiDepartment of Nanomedicine, Faculty of Advanced Science and Technology, Tehran Medical Sciences, Islamic Azad University , Tehran, IranEmail mojtaba.falahati@alumni.ut.ac.ir
                Anwarul HasanDepartment of Mechanical and Industrial Engineering, College of Engineering, Qatar University , Doha2713, QatarEmail hasan.anwarul.mit@gmail.com
                [*]

                These authors contributed equally to this work

                Article
                Publisher ID: 220380
                DOI: 10.2147/IJN.S220380
                PMC ID: 6718255
                PubMed ID: 31695369
                SO-VID: 3a441702-b435-4f98-8d74-5fc954189c89
                Copyright © © 2019 Zand et al.
                License:

                This work is published and licensed by Dove Medical Press Limited. The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License ( http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms ( https://www.dovepress.com/terms.php).

                History
                Date received : 21 June 2019
                Date accepted : 09 August 2019
                Page count
                Figures: 6, Tables: 2, References: 43, Pages: 12
                Categories
                Subject: Original Research

                ScienceOpen disciplines: Molecular medicine
                Keywords: cerium oxide,nanoparticle,amyloid,cytotoxicity,spectroscopy,cellular assay,inhibition
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: cerium oxide, nanoparticle, amyloid, cytotoxicity, spectroscopy, cellular assay, inhibition

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