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Analysis of SiO2 nanoparticles binding proteins in rat blood and brain homogenate.

Shim KH, Hulme J, Maeng EH, Kim MK, An SS - Int J Nanomedicine (2014)

Bottom Line: In total, 115 and 48 plasma proteins from the rat were identified as being bound to negatively charged 20 nm and 100 nm SiO2 nanoparticles, respectively, and 50 and 36 proteins were found for 20 nm and 100 nm arginine-coated SiO2 nanoparticles, respectively.When proteins were compared between the two charges, higher numbers of proteins were found for arginine-coated positively charged SiO2 nanoparticles than for the negatively charged nanoparticles.Proteins bound on the surface of nanoparticles may affect functional and conformational properties and distributions in complicated biological processes.

View Article: PubMed Central - PubMed

Affiliation: Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Sungnam-si, South Korea.

ABSTRACT
A multitude of nanoparticles, such as titanium oxide (TiO2), zinc oxide, aluminum oxide, gold oxide, silver oxide, iron oxide, and silica oxide, are found in many chemical, cosmetic, pharmaceutical, and electronic products. Recently, SiO2 nanoparticles were shown to have an inert toxicity profile and no association with an irreversible toxicological change in animal models. Hence, exposure to SiO2 nanoparticles is on the increase. SiO2 nanoparticles are routinely used in numerous materials, from strengthening filler for concrete and other construction composites, to nontoxic platforms for biomedical application, such as drug delivery and theragnostics. On the other hand, recent in vitro experiments indicated that SiO2 nanoparticles were cytotoxic. Therefore, we investigated these nanoparticles to identify potentially toxic pathways by analyzing the adsorbed protein corona on the surface of SiO2 nanoparticles in the blood and brain of the rat. Four types of SiO2 nanoparticles were chosen for investigation, and the protein corona of each type was analyzed using liquid chromatography-tandem mass spectrometry technology. In total, 115 and 48 plasma proteins from the rat were identified as being bound to negatively charged 20 nm and 100 nm SiO2 nanoparticles, respectively, and 50 and 36 proteins were found for 20 nm and 100 nm arginine-coated SiO2 nanoparticles, respectively. Higher numbers of proteins were adsorbed onto the 20 nm sized SiO2 nanoparticles than onto the 100 nm sized nanoparticles regardless of charge. When proteins were compared between the two charges, higher numbers of proteins were found for arginine-coated positively charged SiO2 nanoparticles than for the negatively charged nanoparticles. The proteins identified as bound in the corona from SiO2 nanoparticles were further analyzed with ClueGO, a Cytoscape plugin used in protein ontology and for identifying biological interaction pathways. Proteins bound on the surface of nanoparticles may affect functional and conformational properties and distributions in complicated biological processes.

No MeSH data available.


Related in: MedlinePlus

Visualized biological processes associated with binding of proteins from plasma and brain homogenate with SiO2 nanoparticles. (A) Plasma and negatively charged 20 nm SiO2 nanoparticles, (B) plasma and negatively charged 100 nm SiO2 nanoparticles, (C) brain homogenate and negatively charged 20 nm SiO2 nanoparticles, and (D) brain homogenate and negatively charged 100 nm SiO2 nanoparticles.Abbreviation: BH, brain homogenate.
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f1-ijn-9-207: Visualized biological processes associated with binding of proteins from plasma and brain homogenate with SiO2 nanoparticles. (A) Plasma and negatively charged 20 nm SiO2 nanoparticles, (B) plasma and negatively charged 100 nm SiO2 nanoparticles, (C) brain homogenate and negatively charged 20 nm SiO2 nanoparticles, and (D) brain homogenate and negatively charged 100 nm SiO2 nanoparticles.Abbreviation: BH, brain homogenate.

Mentions: Proteins within the criteria were further analyzed using ClueGO, one of the Cytoscape plugins, which provides the gene ontology and biological processes of proteins. Each biological process was represented by their colored circular dots. In plasma, proteins involved in the acute inflammatory response and cholesterol transport pathways were bound mainly onto SiO2EN20(−) (Figure 1). In brain homogenate, SiO2EN20(−) bound with proteins involved in the acetyl-CoA metabolic process, endocytosis, protein folding, glycolysis, energy-coupled proton transport, protein polymerization, and regulation of neurotransmitters. For plasma proteins bound onto SiO2EN100(−), the result was similar to that for SiO2EN20(−), where proteins involved in the acute inflammatory response and cholesterol transport were found in addition to blood coagulation proteins. Proteins involved in the acetyl-CoA metabolic process, endocytosis, and protein folding from brain homogenate bound to both SiO2EN100(−) and SiO2EN20(−), along with proteins involved in microtubule-based movement, negative regulation of microtubule depolymerization, and RNA splicing.


Analysis of SiO2 nanoparticles binding proteins in rat blood and brain homogenate.

Shim KH, Hulme J, Maeng EH, Kim MK, An SS - Int J Nanomedicine (2014)

Visualized biological processes associated with binding of proteins from plasma and brain homogenate with SiO2 nanoparticles. (A) Plasma and negatively charged 20 nm SiO2 nanoparticles, (B) plasma and negatively charged 100 nm SiO2 nanoparticles, (C) brain homogenate and negatively charged 20 nm SiO2 nanoparticles, and (D) brain homogenate and negatively charged 100 nm SiO2 nanoparticles.Abbreviation: BH, brain homogenate.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4279766&req=5

f1-ijn-9-207: Visualized biological processes associated with binding of proteins from plasma and brain homogenate with SiO2 nanoparticles. (A) Plasma and negatively charged 20 nm SiO2 nanoparticles, (B) plasma and negatively charged 100 nm SiO2 nanoparticles, (C) brain homogenate and negatively charged 20 nm SiO2 nanoparticles, and (D) brain homogenate and negatively charged 100 nm SiO2 nanoparticles.Abbreviation: BH, brain homogenate.
Mentions: Proteins within the criteria were further analyzed using ClueGO, one of the Cytoscape plugins, which provides the gene ontology and biological processes of proteins. Each biological process was represented by their colored circular dots. In plasma, proteins involved in the acute inflammatory response and cholesterol transport pathways were bound mainly onto SiO2EN20(−) (Figure 1). In brain homogenate, SiO2EN20(−) bound with proteins involved in the acetyl-CoA metabolic process, endocytosis, protein folding, glycolysis, energy-coupled proton transport, protein polymerization, and regulation of neurotransmitters. For plasma proteins bound onto SiO2EN100(−), the result was similar to that for SiO2EN20(−), where proteins involved in the acute inflammatory response and cholesterol transport were found in addition to blood coagulation proteins. Proteins involved in the acetyl-CoA metabolic process, endocytosis, and protein folding from brain homogenate bound to both SiO2EN100(−) and SiO2EN20(−), along with proteins involved in microtubule-based movement, negative regulation of microtubule depolymerization, and RNA splicing.

Bottom Line: In total, 115 and 48 plasma proteins from the rat were identified as being bound to negatively charged 20 nm and 100 nm SiO2 nanoparticles, respectively, and 50 and 36 proteins were found for 20 nm and 100 nm arginine-coated SiO2 nanoparticles, respectively.When proteins were compared between the two charges, higher numbers of proteins were found for arginine-coated positively charged SiO2 nanoparticles than for the negatively charged nanoparticles.Proteins bound on the surface of nanoparticles may affect functional and conformational properties and distributions in complicated biological processes.

View Article: PubMed Central - PubMed

Affiliation: Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Sungnam-si, South Korea.

ABSTRACT
A multitude of nanoparticles, such as titanium oxide (TiO2), zinc oxide, aluminum oxide, gold oxide, silver oxide, iron oxide, and silica oxide, are found in many chemical, cosmetic, pharmaceutical, and electronic products. Recently, SiO2 nanoparticles were shown to have an inert toxicity profile and no association with an irreversible toxicological change in animal models. Hence, exposure to SiO2 nanoparticles is on the increase. SiO2 nanoparticles are routinely used in numerous materials, from strengthening filler for concrete and other construction composites, to nontoxic platforms for biomedical application, such as drug delivery and theragnostics. On the other hand, recent in vitro experiments indicated that SiO2 nanoparticles were cytotoxic. Therefore, we investigated these nanoparticles to identify potentially toxic pathways by analyzing the adsorbed protein corona on the surface of SiO2 nanoparticles in the blood and brain of the rat. Four types of SiO2 nanoparticles were chosen for investigation, and the protein corona of each type was analyzed using liquid chromatography-tandem mass spectrometry technology. In total, 115 and 48 plasma proteins from the rat were identified as being bound to negatively charged 20 nm and 100 nm SiO2 nanoparticles, respectively, and 50 and 36 proteins were found for 20 nm and 100 nm arginine-coated SiO2 nanoparticles, respectively. Higher numbers of proteins were adsorbed onto the 20 nm sized SiO2 nanoparticles than onto the 100 nm sized nanoparticles regardless of charge. When proteins were compared between the two charges, higher numbers of proteins were found for arginine-coated positively charged SiO2 nanoparticles than for the negatively charged nanoparticles. The proteins identified as bound in the corona from SiO2 nanoparticles were further analyzed with ClueGO, a Cytoscape plugin used in protein ontology and for identifying biological interaction pathways. Proteins bound on the surface of nanoparticles may affect functional and conformational properties and distributions in complicated biological processes.

No MeSH data available.


Related in: MedlinePlus