Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate

Kyu Hwan Shim,1 John Hulme,1 Eun Ho Maeng,2 Meyoung-Kon Kim,3 Seong Soo A An1 1Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Sungnam-si, Gyeonggi-do, South Korea; 2Department of Analysis, KTR, Kimpo, Gyeonggi-do, South Korea; 3Department of Biochemistry and...

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Autores principales: Shim KH, Hulme J, Maeng EH, Kim MK, An SSA
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Publicado: Dove Medical Press 2014
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spelling oai:doaj.org-article:0f6bed58febf4cdbb6313574e29e43632021-12-02T07:37:03ZAnalysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate1178-2013https://doaj.org/article/0f6bed58febf4cdbb6313574e29e43632014-12-01T00:00:00Zhttp://www.dovepress.com/analysis-of-zinc-oxide-nanoparticles-binding-proteins-in-rat-blood-and-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013 Kyu Hwan Shim,1 John Hulme,1 Eun Ho Maeng,2 Meyoung-Kon Kim,3 Seong Soo A An1 1Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Sungnam-si, Gyeonggi-do, South Korea; 2Department of Analysis, KTR, Kimpo, Gyeonggi-do, South Korea; 3Department of Biochemistry and Molecular Biology, Korea University Medical School and College, Seoul, South Korea Abstract: 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, ZnOSM20(-), ZnOSM20(+), ZnOAE100(-), and ZnOAE100(+), 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 ZnOSM20(-) and ZnOSM20(+), respectively. For ZnOAE100(-) and ZnOAE100(+), 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. Keywords: brain homogenate, nanotoxicity, plasma, protein coronaShim KHHulme JMaeng EHKim MKAn SSADove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2014, Iss Supplement 2, Pp 217-224 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine (General)
R5-920
spellingShingle Medicine (General)
R5-920
Shim KH
Hulme J
Maeng EH
Kim MK
An SSA
Analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate
description Kyu Hwan Shim,1 John Hulme,1 Eun Ho Maeng,2 Meyoung-Kon Kim,3 Seong Soo A An1 1Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Sungnam-si, Gyeonggi-do, South Korea; 2Department of Analysis, KTR, Kimpo, Gyeonggi-do, South Korea; 3Department of Biochemistry and Molecular Biology, Korea University Medical School and College, Seoul, South Korea Abstract: 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, ZnOSM20(-), ZnOSM20(+), ZnOAE100(-), and ZnOAE100(+), 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 ZnOSM20(-) and ZnOSM20(+), respectively. For ZnOAE100(-) and ZnOAE100(+), 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. Keywords: brain homogenate, nanotoxicity, plasma, protein corona
format article
author Shim KH
Hulme J
Maeng EH
Kim MK
An SSA
author_facet Shim KH
Hulme J
Maeng EH
Kim MK
An SSA
author_sort Shim KH
title 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_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_sort analysis of zinc oxide nanoparticles binding proteins in rat blood and brain homogenate
publisher Dove Medical Press
publishDate 2014
url https://doaj.org/article/0f6bed58febf4cdbb6313574e29e4363
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