The Highly Selective Capture of Phosphopeptides by Zirconium Phosphonate-Modified Magnetic Nanoparticles for Phosphoproteome Analysis
The highly selective capture of phosphopeptides from proteolytic digests is a great challenge for the identification of phosphoproteins by mass spectrometry. In this work, the zirconium phosphonate-modified magnetic Fe 3O 4/SiO 2 core/shell nanoparticles have been synthesized and successfully applie...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2008-08, Vol.19 (8), p.1176-1186 |
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| creator | Zhao, Liang Wu, Ren'an Han, Guanghui Zhou, Houjiang Ren, Lianbing Tian, Ruijun Zou, Hanfa |
| description | The highly selective capture of phosphopeptides from proteolytic digests is a great challenge for the identification of phosphoproteins by mass spectrometry. In this work, the zirconium phosphonate-modified magnetic Fe
3O
4/SiO
2 core/shell nanoparticles have been synthesized and successfully applied for the selective capture of phosphopeptides from complex tryptic digests of proteins before the analysis of MALDI-TOF mass spectrometry with the desired convenience of sample handling. The ratio of magnetic nanoparticle to protein and the incubation time for capturing phosphopeptides from complex proteolytic digests were investigated, and the optimized nanoparticle-to-protein ratio and incubation time were between 15:1 to 30:1 and 30 min, respectively. The excellent detection limit of 0.5 fmol β-casein has been achieved by MALDI-TOF mass spectrometry with the specific capture of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles. The great specificity of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles to phosphopeptides was demonstrated by the selective capture of phosphopeptides from a complex tryptic digest of the mixture of α-casein and bovine serum albumin at molar ratio of 1 to 100 in MALDI-TOF-MS analysis. An application of the magnetic nanoparticles to selective capture phosphopeptides from a tryptic digest of mouse liver lysate was further carried out by combining with nano-LC-MS/MS and MS/MS/MS analyses, and a total of 194 unique phosphopeptides were successfully identified. |
| doi_str_mv | 10.1016/j.jasms.2008.04.027 |
| format | Article |
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3O
4/SiO
2 core/shell nanoparticles have been synthesized and successfully applied for the selective capture of phosphopeptides from complex tryptic digests of proteins before the analysis of MALDI-TOF mass spectrometry with the desired convenience of sample handling. The ratio of magnetic nanoparticle to protein and the incubation time for capturing phosphopeptides from complex proteolytic digests were investigated, and the optimized nanoparticle-to-protein ratio and incubation time were between 15:1 to 30:1 and 30 min, respectively. The excellent detection limit of 0.5 fmol β-casein has been achieved by MALDI-TOF mass spectrometry with the specific capture of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles. The great specificity of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles to phosphopeptides was demonstrated by the selective capture of phosphopeptides from a complex tryptic digest of the mixture of α-casein and bovine serum albumin at molar ratio of 1 to 100 in MALDI-TOF-MS analysis. An application of the magnetic nanoparticles to selective capture phosphopeptides from a tryptic digest of mouse liver lysate was further carried out by combining with nano-LC-MS/MS and MS/MS/MS analyses, and a total of 194 unique phosphopeptides were successfully identified.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1016/j.jasms.2008.04.027</identifier><identifier>PMID: 18502663</identifier><language>eng</language><publisher>New York: Elsevier Inc</publisher><subject>Analytical Chemistry ; Analytical, structural and metabolic biochemistry ; Animals ; Bioinformatics ; Biological and medical sciences ; Biotechnology ; Casein ; Caseins - chemistry ; Chemistry ; Chemistry and Materials Science ; Data Interpretation, Statistical ; Databases, Protein ; Desorption ; Ferrous Compounds - chemistry ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods ; Glass ; Hydrolysis ; Indicators and Reagents ; Ions ; Iron oxides ; Liver ; Liver - chemistry ; Magnetics ; Mass spectrometry ; Mice ; Nanoparticles ; Nanoparticles - chemistry ; Organic Chemistry ; Organophosphonates - chemistry ; Ovalbumin - chemistry ; Phosphoproteins - chemistry ; Proteins ; Proteome - chemistry ; Proteomics ; Scientific imaging ; Serum albumin ; Silicon dioxide ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spectroscopy ; Trypsin ; Zirconium ; Zirconium - chemistry</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2008-08, Vol.19 (8), p.1176-1186</ispartof><rights>2008 American Society for Mass Spectrometry</rights><rights>American Society for Mass Spectrometry 2008</rights><rights>2008 INIST-CNRS</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, 2008.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-e72db90f37aad539e7e179d21f2a8e10d6c27d7946b39eb86031ab91bdea310f3</citedby><cites>FETCH-LOGICAL-c536t-e72db90f37aad539e7e179d21f2a8e10d6c27d7946b39eb86031ab91bdea310f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1016/j.jasms.2008.04.027$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1016/j.jasms.2008.04.027$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20589036$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18502663$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Liang</creatorcontrib><creatorcontrib>Wu, Ren'an</creatorcontrib><creatorcontrib>Han, Guanghui</creatorcontrib><creatorcontrib>Zhou, Houjiang</creatorcontrib><creatorcontrib>Ren, Lianbing</creatorcontrib><creatorcontrib>Tian, Ruijun</creatorcontrib><creatorcontrib>Zou, Hanfa</creatorcontrib><title>The Highly Selective Capture of Phosphopeptides by Zirconium Phosphonate-Modified Magnetic Nanoparticles for Phosphoproteome Analysis</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J Am Soc Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>The highly selective capture of phosphopeptides from proteolytic digests is a great challenge for the identification of phosphoproteins by mass spectrometry. In this work, the zirconium phosphonate-modified magnetic Fe
3O
4/SiO
2 core/shell nanoparticles have been synthesized and successfully applied for the selective capture of phosphopeptides from complex tryptic digests of proteins before the analysis of MALDI-TOF mass spectrometry with the desired convenience of sample handling. The ratio of magnetic nanoparticle to protein and the incubation time for capturing phosphopeptides from complex proteolytic digests were investigated, and the optimized nanoparticle-to-protein ratio and incubation time were between 15:1 to 30:1 and 30 min, respectively. The excellent detection limit of 0.5 fmol β-casein has been achieved by MALDI-TOF mass spectrometry with the specific capture of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles. The great specificity of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles to phosphopeptides was demonstrated by the selective capture of phosphopeptides from a complex tryptic digest of the mixture of α-casein and bovine serum albumin at molar ratio of 1 to 100 in MALDI-TOF-MS analysis. An application of the magnetic nanoparticles to selective capture phosphopeptides from a tryptic digest of mouse liver lysate was further carried out by combining with nano-LC-MS/MS and MS/MS/MS analyses, and a total of 194 unique phosphopeptides were successfully identified.</description><subject>Analytical Chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Casein</subject><subject>Caseins - chemistry</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Data Interpretation, Statistical</subject><subject>Databases, Protein</subject><subject>Desorption</subject><subject>Ferrous Compounds - chemistry</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>General aspects, investigation methods</topic><topic>Glass</topic><topic>Hydrolysis</topic><topic>Indicators and Reagents</topic><topic>Ions</topic><topic>Iron oxides</topic><topic>Liver</topic><topic>Liver - chemistry</topic><topic>Magnetics</topic><topic>Mass spectrometry</topic><topic>Mice</topic><topic>Nanoparticles</topic><topic>Nanoparticles - chemistry</topic><topic>Organic Chemistry</topic><topic>Organophosphonates - chemistry</topic><topic>Ovalbumin - chemistry</topic><topic>Phosphoproteins - chemistry</topic><topic>Proteins</topic><topic>Proteome - chemistry</topic><topic>Proteomics</topic><topic>Scientific imaging</topic><topic>Serum albumin</topic><topic>Silicon dioxide</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Spectroscopy</topic><topic>Trypsin</topic><topic>Zirconium</topic><topic>Zirconium - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Liang</creatorcontrib><creatorcontrib>Wu, Ren'an</creatorcontrib><creatorcontrib>Han, Guanghui</creatorcontrib><creatorcontrib>Zhou, Houjiang</creatorcontrib><creatorcontrib>Ren, Lianbing</creatorcontrib><creatorcontrib>Tian, Ruijun</creatorcontrib><creatorcontrib>Zou, Hanfa</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni 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Spectrom</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>19</volume><issue>8</issue><spage>1176</spage><epage>1186</epage><pages>1176-1186</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>The highly selective capture of phosphopeptides from proteolytic digests is a great challenge for the identification of phosphoproteins by mass spectrometry. In this work, the zirconium phosphonate-modified magnetic Fe
3O
4/SiO
2 core/shell nanoparticles have been synthesized and successfully applied for the selective capture of phosphopeptides from complex tryptic digests of proteins before the analysis of MALDI-TOF mass spectrometry with the desired convenience of sample handling. The ratio of magnetic nanoparticle to protein and the incubation time for capturing phosphopeptides from complex proteolytic digests were investigated, and the optimized nanoparticle-to-protein ratio and incubation time were between 15:1 to 30:1 and 30 min, respectively. The excellent detection limit of 0.5 fmol β-casein has been achieved by MALDI-TOF mass spectrometry with the specific capture of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles. The great specificity of zirconium phosphonate-modified magnetic Fe
3O
4 nanoparticles to phosphopeptides was demonstrated by the selective capture of phosphopeptides from a complex tryptic digest of the mixture of α-casein and bovine serum albumin at molar ratio of 1 to 100 in MALDI-TOF-MS analysis. An application of the magnetic nanoparticles to selective capture phosphopeptides from a tryptic digest of mouse liver lysate was further carried out by combining with nano-LC-MS/MS and MS/MS/MS analyses, and a total of 194 unique phosphopeptides were successfully identified.</abstract><cop>New York</cop><pub>Elsevier Inc</pub><pmid>18502663</pmid><doi>10.1016/j.jasms.2008.04.027</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Journal of the American Society for Mass Spectrometry, 2008-08, Vol.19 (8), p.1176-1186 |
| issn | 1044-0305 1879-1123 |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; SpringerLink Journals - AutoHoldings |
| subjects | Analytical Chemistry Analytical, structural and metabolic biochemistry Animals Bioinformatics Biological and medical sciences Biotechnology Casein Caseins - chemistry Chemistry Chemistry and Materials Science Data Interpretation, Statistical Databases, Protein Desorption Ferrous Compounds - chemistry Fundamental and applied biological sciences. Psychology General aspects, investigation methods Glass Hydrolysis Indicators and Reagents Ions Iron oxides Liver Liver - chemistry Magnetics Mass spectrometry Mice Nanoparticles Nanoparticles - chemistry Organic Chemistry Organophosphonates - chemistry Ovalbumin - chemistry Phosphoproteins - chemistry Proteins Proteome - chemistry Proteomics Scientific imaging Serum albumin Silicon dioxide Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectroscopy Trypsin Zirconium Zirconium - chemistry |
| title | The Highly Selective Capture of Phosphopeptides by Zirconium Phosphonate-Modified Magnetic Nanoparticles for Phosphoproteome Analysis |
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