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Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate
Nanoparticles (NPs) are currently used in chemical, cosmetic, pharmaceutical, and electronic products. Nevertheless, limited safety information is available for many NPs, especially in terms of their interactions with various binding proteins, leading to potential toxic effects. Zinc oxide (ZnO) NPs...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Dove Medical Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279772/ https://www.ncbi.nlm.nih.gov/pubmed/25565839 http://dx.doi.org/10.2147/IJN.S58204 |
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author | Shim, Kyu Hwan Hulme, John Maeng, Eun Ho Kim, Meyoung-Kon An, Seong Soo A |
author_facet | Shim, Kyu Hwan Hulme, John Maeng, Eun Ho Kim, Meyoung-Kon An, Seong Soo A |
author_sort | Shim, Kyu Hwan |
collection | PubMed |
description | Nanoparticles (NPs) are currently used in chemical, cosmetic, pharmaceutical, and electronic products. Nevertheless, limited safety information is available for many NPs, especially in terms of their interactions with various binding proteins, leading to potential toxic effects. Zinc oxide (ZnO) NPs are included in the formulation of new products, such as adhesives, batteries, ceramics, cosmetics, cement, glass, ointments, paints, pigments, and supplementary foods, resulting in increased human exposures to ZnO. Hence, we investigated the potential ZnO nanotoxic pathways by analyzing the adsorbed proteins, called protein corona, from blood and brain from four ZnO NPs, ZnO(SM20(−)), ZnO(SM20(+)), ZnO(AE100(−)), and ZnO(AE100(+)), in order to understand their potential mechanisms in vivo. Through this study, liquid chromatography–mass spectroscopy/mass spectroscopy technology was employed to identify all bound proteins. Totals of 52 and 58 plasma proteins were identified as being bound to ZnO(SM20(−)) and ZnO(SM20(+)), respectively. For ZnO(AE100(−)) and ZnO(AE100(+)), 58 and 44 proteins were bound, respectively. Similar numbers of proteins were adsorbed onto ZnO irrespective of size or surface charge of the nanoparticle. These proteins were further analyzed with ClueGO, a Cytoscape plugin, which provided gene ontology and the biological interaction processes of identified proteins. Interactions between diverse proteins and ZnO nanoparticles could result in an alteration of their functions, conformation, and clearance, eventually affecting many biological processes. |
format | Online Article Text |
id | pubmed-4279772 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-42797722015-01-06 Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate Shim, Kyu Hwan Hulme, John Maeng, Eun Ho Kim, Meyoung-Kon An, Seong Soo A Int J Nanomedicine Original Research Nanoparticles (NPs) are currently used in chemical, cosmetic, pharmaceutical, and electronic products. Nevertheless, limited safety information is available for many NPs, especially in terms of their interactions with various binding proteins, leading to potential toxic effects. Zinc oxide (ZnO) NPs are included in the formulation of new products, such as adhesives, batteries, ceramics, cosmetics, cement, glass, ointments, paints, pigments, and supplementary foods, resulting in increased human exposures to ZnO. Hence, we investigated the potential ZnO nanotoxic pathways by analyzing the adsorbed proteins, called protein corona, from blood and brain from four ZnO NPs, ZnO(SM20(−)), ZnO(SM20(+)), ZnO(AE100(−)), and ZnO(AE100(+)), in order to understand their potential mechanisms in vivo. Through this study, liquid chromatography–mass spectroscopy/mass spectroscopy technology was employed to identify all bound proteins. Totals of 52 and 58 plasma proteins were identified as being bound to ZnO(SM20(−)) and ZnO(SM20(+)), respectively. For ZnO(AE100(−)) and ZnO(AE100(+)), 58 and 44 proteins were bound, respectively. Similar numbers of proteins were adsorbed onto ZnO irrespective of size or surface charge of the nanoparticle. These proteins were further analyzed with ClueGO, a Cytoscape plugin, which provided gene ontology and the biological interaction processes of identified proteins. Interactions between diverse proteins and ZnO nanoparticles could result in an alteration of their functions, conformation, and clearance, eventually affecting many biological processes. Dove Medical Press 2014-11-15 /pmc/articles/PMC4279772/ /pubmed/25565839 http://dx.doi.org/10.2147/IJN.S58204 Text en © 2014 Shim et al. This work is published by Dove Medical Press Limited, and licensed under Creative Commons Attribution – Non Commercial (unported, v3.0) License The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. |
spellingShingle | Original Research Shim, Kyu Hwan Hulme, John Maeng, Eun Ho Kim, Meyoung-Kon An, Seong Soo A Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title | Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title_full | Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title_fullStr | Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title_full_unstemmed | Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title_short | Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
title_sort | analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279772/ https://www.ncbi.nlm.nih.gov/pubmed/25565839 http://dx.doi.org/10.2147/IJN.S58204 |
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