Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size
Nanoparticle biological activity, biocompatibility and fate can be directly affected by layers of readily adsorbed host proteins in biofluids. Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using...
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| Veröffentlicht in: | Proteomics 2011-12, Vol.11 (23), p.4569-4577 |
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| creator | Zhang, Haizhen Burnum, Kristin E. Luna, Maria L. Petritis, Brianne O. Kim, Jong-Seo Qian, Wei-Jun Moore, Ronald J. Heredia-Langner, Alejandro Webb-Robertson, Bobbie-Jo M. Thrall, Brian D. Camp II, David G. Smith, Richard D. Pounds, Joel G. Liu, Tao |
| description | Nanoparticle biological activity, biocompatibility and fate can be directly affected by layers of readily adsorbed host proteins in biofluids. Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using 18O‐labeling and LC‐MS‐based quantitative proteomics. We developed a novel protocol to both simplify isolation of nanoparticle bound proteins and improve reproducibility. LC‐MS analysis identified and quantified 88 human plasma proteins associated with polystyrene nanoparticles consisting of three different surface chemistries and two sizes, as well as, for four different exposure times (for a total of 24 different samples). Quantitative comparison of relative protein abundances was achieved by spiking an 18O‐labeled “universal” reference into each individually processed unlabeled sample as an internal standard, enabling simultaneous application of both label‐free and isotopic labeling quantification across the entire sample set. Clustering analysis of the quantitative proteomics data resulted in distinctive patterns that classified the nanoparticles based on their surface properties and size. In addition, temporal data indicated that the formation of the stable protein corona was at equilibrium within 5 min. The comprehensive quantitative proteomics results obtained in this study provide rich data for computational modeling and have potential implications towards predicting nanoparticle biocompatibility. |
| doi_str_mv | 10.1002/pmic.201100037 |
| format | Article |
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Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using 18O‐labeling and LC‐MS‐based quantitative proteomics. We developed a novel protocol to both simplify isolation of nanoparticle bound proteins and improve reproducibility. LC‐MS analysis identified and quantified 88 human plasma proteins associated with polystyrene nanoparticles consisting of three different surface chemistries and two sizes, as well as, for four different exposure times (for a total of 24 different samples). Quantitative comparison of relative protein abundances was achieved by spiking an 18O‐labeled “universal” reference into each individually processed unlabeled sample as an internal standard, enabling simultaneous application of both label‐free and isotopic labeling quantification across the entire sample set. Clustering analysis of the quantitative proteomics data resulted in distinctive patterns that classified the nanoparticles based on their surface properties and size. In addition, temporal data indicated that the formation of the stable protein corona was at equilibrium within 5 min. The comprehensive quantitative proteomics results obtained in this study provide rich data for computational modeling and have potential implications towards predicting nanoparticle biocompatibility.</description><identifier>ISSN: 1615-9853</identifier><identifier>ISSN: 1615-9861</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.201100037</identifier><identifier>PMID: 21956884</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>60 APPLIED LIFE SCIENCES ; Adsorption ; Analysis of Variance ; Analytical, structural and metabolic biochemistry ; BASIC BIOLOGICAL SCIENCES ; Biocompatibility ; Biological and medical sciences ; BLOOD PLASMA ; Blood Proteins - analysis ; Blood Proteins - metabolism ; Chromatography, Liquid - methods ; Cluster Analysis ; Corona ; Environmental Molecular Sciences Laboratory ; Fundamental and applied biological sciences. Psychology ; Human plasma ; Humans ; interaction ; LABELLING ; LAYERS ; LC-MS ; LIQUID COLUMN CHROMATOGRAPHY ; mass spectrometry ; Mass Spectrometry - methods ; MASS SPECTROSCOPY ; Miscellaneous ; Nanoparticle ; Nanoparticles ; Nanoparticles - chemistry ; Nanoproteomics ; NANOSTRUCTURES ; O labeling ; Particle Size ; PARTICLES ; PLASMA ; POLYSTYRENE ; Polystyrenes - chemistry ; Protein Binding ; PROTEINS ; Proteomics ; Proteomics - methods ; Quantitation ; Quantitative proteomics ; SIZE ; STABLE ISOTOPES ; SURFACE PROPERTIES</subject><ispartof>Proteomics, 2011-12, Vol.11 (23), p.4569-4577</ispartof><rights>Copyright © 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5957-f2b4b27edd116ec6be321d4799ab8d9763115cedcad7c7baa2faaf84d5bfc0de3</citedby><cites>FETCH-LOGICAL-c5957-f2b4b27edd116ec6be321d4799ab8d9763115cedcad7c7baa2faaf84d5bfc0de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpmic.201100037$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpmic.201100037$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25282190$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21956884$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1032415$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Haizhen</creatorcontrib><creatorcontrib>Burnum, Kristin E.</creatorcontrib><creatorcontrib>Luna, Maria L.</creatorcontrib><creatorcontrib>Petritis, Brianne O.</creatorcontrib><creatorcontrib>Kim, Jong-Seo</creatorcontrib><creatorcontrib>Qian, Wei-Jun</creatorcontrib><creatorcontrib>Moore, Ronald J.</creatorcontrib><creatorcontrib>Heredia-Langner, Alejandro</creatorcontrib><creatorcontrib>Webb-Robertson, Bobbie-Jo M.</creatorcontrib><creatorcontrib>Thrall, Brian D.</creatorcontrib><creatorcontrib>Camp II, David G.</creatorcontrib><creatorcontrib>Smith, Richard D.</creatorcontrib><creatorcontrib>Pounds, Joel G.</creatorcontrib><creatorcontrib>Liu, Tao</creatorcontrib><creatorcontrib>Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)</creatorcontrib><title>Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size</title><title>Proteomics</title><addtitle>Proteomics</addtitle><description>Nanoparticle biological activity, biocompatibility and fate can be directly affected by layers of readily adsorbed host proteins in biofluids. Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using 18O‐labeling and LC‐MS‐based quantitative proteomics. We developed a novel protocol to both simplify isolation of nanoparticle bound proteins and improve reproducibility. LC‐MS analysis identified and quantified 88 human plasma proteins associated with polystyrene nanoparticles consisting of three different surface chemistries and two sizes, as well as, for four different exposure times (for a total of 24 different samples). Quantitative comparison of relative protein abundances was achieved by spiking an 18O‐labeled “universal” reference into each individually processed unlabeled sample as an internal standard, enabling simultaneous application of both label‐free and isotopic labeling quantification across the entire sample set. Clustering analysis of the quantitative proteomics data resulted in distinctive patterns that classified the nanoparticles based on their surface properties and size. In addition, temporal data indicated that the formation of the stable protein corona was at equilibrium within 5 min. The comprehensive quantitative proteomics results obtained in this study provide rich data for computational modeling and have potential implications towards predicting nanoparticle biocompatibility.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Adsorption</subject><subject>Analysis of Variance</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biocompatibility</subject><subject>Biological and medical sciences</subject><subject>BLOOD PLASMA</subject><subject>Blood Proteins - analysis</subject><subject>Blood Proteins - metabolism</subject><subject>Chromatography, Liquid - methods</subject><subject>Cluster Analysis</subject><subject>Corona</subject><subject>Environmental Molecular Sciences Laboratory</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Human plasma</subject><subject>Humans</subject><subject>interaction</subject><subject>LABELLING</subject><subject>LAYERS</subject><subject>LC-MS</subject><subject>LIQUID COLUMN CHROMATOGRAPHY</subject><subject>mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>MASS SPECTROSCOPY</subject><subject>Miscellaneous</subject><subject>Nanoparticle</subject><subject>Nanoparticles</subject><subject>Nanoparticles - chemistry</subject><subject>Nanoproteomics</subject><subject>NANOSTRUCTURES</subject><subject>O labeling</subject><subject>Particle Size</subject><subject>PARTICLES</subject><subject>PLASMA</subject><subject>POLYSTYRENE</subject><subject>Polystyrenes - chemistry</subject><subject>Protein Binding</subject><subject>PROTEINS</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Quantitation</subject><subject>Quantitative proteomics</subject><subject>SIZE</subject><subject>STABLE ISOTOPES</subject><subject>SURFACE PROPERTIES</subject><issn>1615-9853</issn><issn>1615-9861</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0k1v1DAQBuAIgWgpXDmiCITEZRd_xHFyqYRW0Fa0fEggjtbEHrMu2TjY3pblxE_HS5alcOGUjPLM60kyRfGQkjklhD0fV07PGaG5IFzeKg5pTcWsbWp6e38v-EFxL8ZLQqhsWnm3OGC0FXXTVIfFj_drGJJLkNwVlmPwCX2OjCUM0G-ii6W3JZjoQ4emHHuIK5iYG2Kpcx2ddRjLAQY_QkhO97m6dmlZGmctBhxSGdfBgv6VP2I2uM03ZXTf8X5xx0If8cHuelR8fPXyw-J0dv725Gzx4nymRSvkzLKu6phEYyitUdcdckZNJdsWusa0suaUCo1Gg5FadgDMAtimMqKzmhjkR8XxlDuuu1V2eawAvRqDW0HYKA9O_f1kcEv12V8pzgRjXOSAx1OAj8mpqF1CvdR-GFAnRQlnFd2iZ7tTgv-6xpjUykWNfQ8D-nXMjsq24bza0if_0Eu_DvmrZ1VVTUVIw9qs5pPSwccY0O4npkRtN0BtN0DtNyA3PLr5nnv--5dn8HQHIGrobYBBu_jHCdZkS7JrJ3ftetz851j17uJscXOI2dTrYsJv-14IX1QtuRTq05sTddoKftGw14rznz2b3lE</recordid><startdate>201112</startdate><enddate>201112</enddate><creator>Zhang, Haizhen</creator><creator>Burnum, Kristin E.</creator><creator>Luna, Maria L.</creator><creator>Petritis, Brianne O.</creator><creator>Kim, Jong-Seo</creator><creator>Qian, Wei-Jun</creator><creator>Moore, Ronald J.</creator><creator>Heredia-Langner, Alejandro</creator><creator>Webb-Robertson, Bobbie-Jo M.</creator><creator>Thrall, Brian D.</creator><creator>Camp II, David G.</creator><creator>Smith, Richard D.</creator><creator>Pounds, Joel G.</creator><creator>Liu, Tao</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley-VCH</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>201112</creationdate><title>Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size</title><author>Zhang, Haizhen ; Burnum, Kristin E. ; Luna, Maria L. ; Petritis, Brianne O. ; Kim, Jong-Seo ; Qian, Wei-Jun ; Moore, Ronald J. ; Heredia-Langner, Alejandro ; Webb-Robertson, Bobbie-Jo M. ; Thrall, Brian D. ; Camp II, David G. ; Smith, Richard D. ; Pounds, Joel G. ; Liu, Tao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5957-f2b4b27edd116ec6be321d4799ab8d9763115cedcad7c7baa2faaf84d5bfc0de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Adsorption</topic><topic>Analysis of Variance</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Biocompatibility</topic><topic>Biological and medical sciences</topic><topic>BLOOD PLASMA</topic><topic>Blood Proteins - analysis</topic><topic>Blood Proteins - metabolism</topic><topic>Chromatography, Liquid - methods</topic><topic>Cluster Analysis</topic><topic>Corona</topic><topic>Environmental Molecular Sciences Laboratory</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Human plasma</topic><topic>Humans</topic><topic>interaction</topic><topic>LABELLING</topic><topic>LAYERS</topic><topic>LC-MS</topic><topic>LIQUID COLUMN CHROMATOGRAPHY</topic><topic>mass spectrometry</topic><topic>Mass Spectrometry - methods</topic><topic>MASS SPECTROSCOPY</topic><topic>Miscellaneous</topic><topic>Nanoparticle</topic><topic>Nanoparticles</topic><topic>Nanoparticles - chemistry</topic><topic>Nanoproteomics</topic><topic>NANOSTRUCTURES</topic><topic>O labeling</topic><topic>Particle Size</topic><topic>PARTICLES</topic><topic>PLASMA</topic><topic>POLYSTYRENE</topic><topic>Polystyrenes - chemistry</topic><topic>Protein Binding</topic><topic>PROTEINS</topic><topic>Proteomics</topic><topic>Proteomics - methods</topic><topic>Quantitation</topic><topic>Quantitative proteomics</topic><topic>SIZE</topic><topic>STABLE ISOTOPES</topic><topic>SURFACE PROPERTIES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Haizhen</creatorcontrib><creatorcontrib>Burnum, Kristin E.</creatorcontrib><creatorcontrib>Luna, Maria L.</creatorcontrib><creatorcontrib>Petritis, Brianne O.</creatorcontrib><creatorcontrib>Kim, Jong-Seo</creatorcontrib><creatorcontrib>Qian, Wei-Jun</creatorcontrib><creatorcontrib>Moore, Ronald J.</creatorcontrib><creatorcontrib>Heredia-Langner, Alejandro</creatorcontrib><creatorcontrib>Webb-Robertson, Bobbie-Jo M.</creatorcontrib><creatorcontrib>Thrall, Brian D.</creatorcontrib><creatorcontrib>Camp II, David G.</creatorcontrib><creatorcontrib>Smith, Richard D.</creatorcontrib><creatorcontrib>Pounds, Joel G.</creatorcontrib><creatorcontrib>Liu, Tao</creatorcontrib><creatorcontrib>Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Haizhen</au><au>Burnum, Kristin E.</au><au>Luna, Maria L.</au><au>Petritis, Brianne O.</au><au>Kim, Jong-Seo</au><au>Qian, Wei-Jun</au><au>Moore, Ronald J.</au><au>Heredia-Langner, Alejandro</au><au>Webb-Robertson, Bobbie-Jo M.</au><au>Thrall, Brian D.</au><au>Camp II, David G.</au><au>Smith, Richard D.</au><au>Pounds, Joel G.</au><au>Liu, Tao</au><aucorp>Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size</atitle><jtitle>Proteomics</jtitle><addtitle>Proteomics</addtitle><date>2011-12</date><risdate>2011</risdate><volume>11</volume><issue>23</issue><spage>4569</spage><epage>4577</epage><pages>4569-4577</pages><issn>1615-9853</issn><issn>1615-9861</issn><eissn>1615-9861</eissn><abstract>Nanoparticle biological activity, biocompatibility and fate can be directly affected by layers of readily adsorbed host proteins in biofluids. Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using 18O‐labeling and LC‐MS‐based quantitative proteomics. We developed a novel protocol to both simplify isolation of nanoparticle bound proteins and improve reproducibility. LC‐MS analysis identified and quantified 88 human plasma proteins associated with polystyrene nanoparticles consisting of three different surface chemistries and two sizes, as well as, for four different exposure times (for a total of 24 different samples). Quantitative comparison of relative protein abundances was achieved by spiking an 18O‐labeled “universal” reference into each individually processed unlabeled sample as an internal standard, enabling simultaneous application of both label‐free and isotopic labeling quantification across the entire sample set. Clustering analysis of the quantitative proteomics data resulted in distinctive patterns that classified the nanoparticles based on their surface properties and size. In addition, temporal data indicated that the formation of the stable protein corona was at equilibrium within 5 min. The comprehensive quantitative proteomics results obtained in this study provide rich data for computational modeling and have potential implications towards predicting nanoparticle biocompatibility.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>21956884</pmid><doi>10.1002/pmic.201100037</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proteomics, 2011-12, Vol.11 (23), p.4569-4577 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | 60 APPLIED LIFE SCIENCES Adsorption Analysis of Variance Analytical, structural and metabolic biochemistry BASIC BIOLOGICAL SCIENCES Biocompatibility Biological and medical sciences BLOOD PLASMA Blood Proteins - analysis Blood Proteins - metabolism Chromatography, Liquid - methods Cluster Analysis Corona Environmental Molecular Sciences Laboratory Fundamental and applied biological sciences. Psychology Human plasma Humans interaction LABELLING LAYERS LC-MS LIQUID COLUMN CHROMATOGRAPHY mass spectrometry Mass Spectrometry - methods MASS SPECTROSCOPY Miscellaneous Nanoparticle Nanoparticles Nanoparticles - chemistry Nanoproteomics NANOSTRUCTURES O labeling Particle Size PARTICLES PLASMA POLYSTYRENE Polystyrenes - chemistry Protein Binding PROTEINS Proteomics Proteomics - methods Quantitation Quantitative proteomics SIZE STABLE ISOTOPES SURFACE PROPERTIES |
| title | Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size |
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