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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...

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Autores principales: Shim, Kyu Hwan, Hulme, John, Maeng, Eun Ho, Kim, Meyoung-Kon, An, Seong Soo A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2014
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.
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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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