Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis
Free radical–initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a lo...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2019-03, Vol.30 (3), p.538-547 |
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| container_title | Journal of the American Society for Mass Spectrometry |
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| creator | Jang, Inae Jeon, Aeran Lim, Suk Gyu Hong, Duk Ki Kim, Min Soo Jo, Jae Hyeong Lee, Sang Tak Moon, Bongjin Oh, Han Bin |
| description | Free radical–initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a loss of a phosphate group occurred to a limited degree for both phosphoserine and phosphotyrosine peptides, and thus, localization of a phosphorylated site was readily achieved. Considering that FRIPS MS supplies a substantial amount of collisional energy to peptides, this result was quite unexpected because a labile phosphate group was conserved. Analysis of the resulting peptide fragments revealed the extensive production of
a
-,
c
-,
x
-, and
z
-type fragments (with some minor
b
- and
y
-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation.
Graphical Abstract |
| doi_str_mv | 10.1007/s13361-018-2100-1 |
| format | Article |
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a
-,
c
-,
x
-, and
z
-type fragments (with some minor
b
- and
y
-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation.
Graphical Abstract</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1007/s13361-018-2100-1</identifier><identifier>PMID: 30414067</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Analytical Chemistry ; Bioinformatics ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Fragmentation ; Fragments ; Free radicals ; Ions ; Mass spectrometry ; Organic Chemistry ; Peptides ; Phosphorylation ; Positive ions ; Proteomics ; Research Article ; Scientific imaging ; Sequences ; Spectroscopy</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2019-03, Vol.30 (3), p.538-547</ispartof><rights>American Society for Mass Spectrometry 2018</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, (2018). All Rights Reserved.</rights><rights>Copyright Springer Nature B.V. 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-e73ecca1237c85699559e491bd760a9b20825eda38b944cc24dad0b2e54178a63</citedby><cites>FETCH-LOGICAL-c400t-e73ecca1237c85699559e491bd760a9b20825eda38b944cc24dad0b2e54178a63</cites><orcidid>0000-0001-7919-0393</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13361-018-2100-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13361-018-2100-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30414067$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jang, Inae</creatorcontrib><creatorcontrib>Jeon, Aeran</creatorcontrib><creatorcontrib>Lim, Suk Gyu</creatorcontrib><creatorcontrib>Hong, Duk Ki</creatorcontrib><creatorcontrib>Kim, Min Soo</creatorcontrib><creatorcontrib>Jo, Jae Hyeong</creatorcontrib><creatorcontrib>Lee, Sang Tak</creatorcontrib><creatorcontrib>Moon, Bongjin</creatorcontrib><creatorcontrib>Oh, Han Bin</creatorcontrib><title>Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification 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>Free radical–initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a loss of a phosphate group occurred to a limited degree for both phosphoserine and phosphotyrosine peptides, and thus, localization of a phosphorylated site was readily achieved. Considering that FRIPS MS supplies a substantial amount of collisional energy to peptides, this result was quite unexpected because a labile phosphate group was conserved. Analysis of the resulting peptide fragments revealed the extensive production of
a
-,
c
-,
x
-, and
z
-type fragments (with some minor
b
- and
y
-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation.
Graphical Abstract</description><subject>Analytical Chemistry</subject><subject>Bioinformatics</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Fragmentation</subject><subject>Fragments</subject><subject>Free radicals</subject><subject>Ions</subject><subject>Mass spectrometry</subject><subject>Organic Chemistry</subject><subject>Peptides</subject><subject>Phosphorylation</subject><subject>Positive ions</subject><subject>Proteomics</subject><subject>Research Article</subject><subject>Scientific imaging</subject><subject>Sequences</subject><subject>Spectroscopy</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kcFuFDEMhkcIREvhAbigSFy4hNpJZjJzrKq2VGrVVVvOUSbjbVPNToYke9gb78Ab8iTNaheQkOAUx_7829ZfVe8RPiOAPk4oZYMcsOWiJDi-qA6x1R1HFPJliUEpDhLqg-pNSk8AqKHTr6sDCQoVNPqw2pxHInZrB-_s-PP7j8vJZ28zDWxBc_YDsTv6tqbJ-emBXduU2N1MLsewohw3bBkiWzyGND-Gec8vQso8Rzul0WYfJjuy6zD4ZRmw_bKTktkkn95Wr5Z2TPRu_x5VX8_P7k-_8Kubi8vTkyvuFEDmpCU5Z8tB2rV103V13ZHqsB90A7brBbSipsHKtu-Uck6owQ7QC6oV6tY28qj6tNOdYyiXpGxWPjkaRztRWCcjUApRixq36Me_0KewjmXfQkmUoIXo1H8plFjLVipRKNxRLoaUIi3NHP3Kxo1BMFv3zM49U9wzW_cMlp4Pe-V1v6Lhd8cvuwogdkAqpemB4p_R_1Z9BoSbpdQ</recordid><startdate>20190301</startdate><enddate>20190301</enddate><creator>Jang, Inae</creator><creator>Jeon, Aeran</creator><creator>Lim, Suk Gyu</creator><creator>Hong, Duk Ki</creator><creator>Kim, Min Soo</creator><creator>Jo, Jae Hyeong</creator><creator>Lee, Sang Tak</creator><creator>Moon, Bongjin</creator><creator>Oh, Han Bin</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-7919-0393</orcidid></search><sort><creationdate>20190301</creationdate><title>Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis</title><author>Jang, Inae ; Jeon, Aeran ; Lim, Suk Gyu ; Hong, Duk Ki ; Kim, Min Soo ; Jo, Jae Hyeong ; Lee, Sang Tak ; Moon, Bongjin ; Oh, Han Bin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-e73ecca1237c85699559e491bd760a9b20825eda38b944cc24dad0b2e54178a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Analytical Chemistry</topic><topic>Bioinformatics</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Fragmentation</topic><topic>Fragments</topic><topic>Free radicals</topic><topic>Ions</topic><topic>Mass spectrometry</topic><topic>Organic Chemistry</topic><topic>Peptides</topic><topic>Phosphorylation</topic><topic>Positive ions</topic><topic>Proteomics</topic><topic>Research Article</topic><topic>Scientific imaging</topic><topic>Sequences</topic><topic>Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jang, Inae</creatorcontrib><creatorcontrib>Jeon, Aeran</creatorcontrib><creatorcontrib>Lim, Suk Gyu</creatorcontrib><creatorcontrib>Hong, Duk Ki</creatorcontrib><creatorcontrib>Kim, Min Soo</creatorcontrib><creatorcontrib>Jo, Jae Hyeong</creatorcontrib><creatorcontrib>Lee, Sang Tak</creatorcontrib><creatorcontrib>Moon, Bongjin</creatorcontrib><creatorcontrib>Oh, Han Bin</creatorcontrib><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 Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jang, Inae</au><au>Jeon, Aeran</au><au>Lim, Suk Gyu</au><au>Hong, Duk Ki</au><au>Kim, Min Soo</au><au>Jo, Jae Hyeong</au><au>Lee, Sang Tak</au><au>Moon, Bongjin</au><au>Oh, Han Bin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><stitle>J. Am. Soc. Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2019-03-01</date><risdate>2019</risdate><volume>30</volume><issue>3</issue><spage>538</spage><epage>547</epage><pages>538-547</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>Free radical–initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a loss of a phosphate group occurred to a limited degree for both phosphoserine and phosphotyrosine peptides, and thus, localization of a phosphorylated site was readily achieved. Considering that FRIPS MS supplies a substantial amount of collisional energy to peptides, this result was quite unexpected because a labile phosphate group was conserved. Analysis of the resulting peptide fragments revealed the extensive production of
a
-,
c
-,
x
-, and
z
-type fragments (with some minor
b
- and
y
-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation.
Graphical Abstract</abstract><cop>New York</cop><pub>Springer US</pub><pmid>30414067</pmid><doi>10.1007/s13361-018-2100-1</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-7919-0393</orcidid></addata></record> |
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| subjects | Analytical Chemistry Bioinformatics Biotechnology Chemistry Chemistry and Materials Science Fragmentation Fragments Free radicals Ions Mass spectrometry Organic Chemistry Peptides Phosphorylation Positive ions Proteomics Research Article Scientific imaging Sequences Spectroscopy |
| title | Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis |
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