Large Scale Discovery and De Novo-Assisted Sequencing of Cationic Antimicrobial Peptides (CAMPs) by Microparticle Capture and Electron-Transfer Dissociation (ETD) Mass Spectrometry
The identification and sequencing of novel cationic antimicrobial peptides (CAMPs) have proven challenging due to the limitations associated with traditional proteomics methods and difficulties sequencing peptides present in complex biomolecular mixtures. We present here a process for large-scale id...
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| Veröffentlicht in: | Journal of proteome research 2015-10, Vol.14 (10), p.4282-4295 |
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| container_title | Journal of proteome research |
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| creator | Juba, Melanie L Russo, Paul S Devine, Megan Barksdale, Stephanie Rodriguez, Carlos Vliet, Kent A Schnur, Joel M van Hoek, Monique L Bishop, Barney M |
| description | The identification and sequencing of novel cationic antimicrobial peptides (CAMPs) have proven challenging due to the limitations associated with traditional proteomics methods and difficulties sequencing peptides present in complex biomolecular mixtures. We present here a process for large-scale identification and de novo-assisted sequencing of newly discovered CAMPs using microparticle capture followed by tandem mass spectrometry equipped with electron-transfer dissociation (ETD). This process was initially evaluated and verified using known CAMPs with varying physicochemical properties. The effective parameters were then applied in the analysis of a complex mixture of peptides harvested from American alligator plasma using custom-made (Bioprospector) functionalized hydrogel particles. Here, we report the successful sequencing process for CAMPs that has led to the identification of 340 unique peptides and the discovery of five novel CAMPs from American alligator plasma. |
| doi_str_mv | 10.1021/acs.jproteome.5b00447 |
| format | Article |
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We present here a process for large-scale identification and de novo-assisted sequencing of newly discovered CAMPs using microparticle capture followed by tandem mass spectrometry equipped with electron-transfer dissociation (ETD). This process was initially evaluated and verified using known CAMPs with varying physicochemical properties. The effective parameters were then applied in the analysis of a complex mixture of peptides harvested from American alligator plasma using custom-made (Bioprospector) functionalized hydrogel particles. 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Proteome Res</addtitle><description>The identification and sequencing of novel cationic antimicrobial peptides (CAMPs) have proven challenging due to the limitations associated with traditional proteomics methods and difficulties sequencing peptides present in complex biomolecular mixtures. We present here a process for large-scale identification and de novo-assisted sequencing of newly discovered CAMPs using microparticle capture followed by tandem mass spectrometry equipped with electron-transfer dissociation (ETD). This process was initially evaluated and verified using known CAMPs with varying physicochemical properties. The effective parameters were then applied in the analysis of a complex mixture of peptides harvested from American alligator plasma using custom-made (Bioprospector) functionalized hydrogel particles. Here, we report the successful sequencing process for CAMPs that has led to the identification of 340 unique peptides and the discovery of five novel CAMPs from American alligator plasma.</description><subject>Alligators and Crocodiles - blood</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antimicrobial Cationic Peptides - blood</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Bacillus cereus - drug effects</subject><subject>Bacillus cereus - growth & development</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - isolation & purification</subject><subject>Blood Proteins - pharmacology</subject><subject>Chromatography, Liquid</subject><subject>Drug Discovery</subject><subject>Electrons</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - growth & development</subject><subject>Hydrogels</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Annotation</subject><subject>Molecular Sequence Data</subject><subject>Particle Size</subject><subject>Proteomics - instrumentation</subject><subject>Proteomics - methods</subject><subject>Pseudomonas aeruginosa - drug effects</subject><subject>Pseudomonas aeruginosa - growth & development</subject><subject>Sequence Analysis, Protein - methods</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - growth & development</subject><subject>Tandem Mass Spectrometry - methods</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctq3DAUNaWhefUTWrScLDyVLMmP5eCZpoWZJDDTtbmWr4OCbbmSHJj_ygdW80i2BYEEOo977omib4zOGU3YD1Bu_jJa49H0OJc1pUJkn6IrJrmMeUGzz-_vvOCX0bVzL5QymVH-JbpMUp5kgqdX0dsa7DOSrYIOyVI7ZV7R7gkMDVkieTCvJl44p53Hhmzx74SD0sMzMS0pwWszaEUWg9e9VtbUGjryhKPXDToyKxebJ3dH6j3ZHH5HsF6r4FLC6CeLR49Vh8pbM8Q7C4Nr0R5mcEbpoziZrXbLO7IB58h2PCJ79HZ_G1200Dn8er5voj8_V7vyV7x-vP9dLtYxcMl83HIBKARjSmBdcEgEZjWkBea5AtlgAk0j8oImKueKyrQuWMFoEw4AY6niN9HspBv2HKI7X_VhQ9h1MKCZXMUylgcGlUmAyhM0JHXOYluNVvdg9xWj1aGwKhRWfRRWnQsLvO9ni6nusflgvTcUAOwEOPLNZIeQ-D-i_wATVqkj</recordid><startdate>20151002</startdate><enddate>20151002</enddate><creator>Juba, Melanie L</creator><creator>Russo, Paul S</creator><creator>Devine, Megan</creator><creator>Barksdale, Stephanie</creator><creator>Rodriguez, Carlos</creator><creator>Vliet, Kent A</creator><creator>Schnur, Joel M</creator><creator>van Hoek, Monique L</creator><creator>Bishop, Barney M</creator><general>American Chemical Society</general><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>7X8</scope></search><sort><creationdate>20151002</creationdate><title>Large Scale Discovery and De Novo-Assisted Sequencing of Cationic Antimicrobial Peptides (CAMPs) by Microparticle Capture and Electron-Transfer Dissociation (ETD) Mass Spectrometry</title><author>Juba, Melanie L ; Russo, Paul S ; Devine, Megan ; Barksdale, Stephanie ; Rodriguez, Carlos ; Vliet, Kent A ; Schnur, Joel M ; van Hoek, Monique L ; Bishop, Barney M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a351t-f34ae4411c4eb93a24e7ba69e88ca5de2add48902c83c056b91910d10daa116c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Alligators and Crocodiles - blood</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antimicrobial Cationic Peptides - blood</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Bacillus cereus - drug effects</topic><topic>Bacillus cereus - growth & development</topic><topic>Blood Proteins - chemistry</topic><topic>Blood Proteins - isolation & purification</topic><topic>Blood Proteins - pharmacology</topic><topic>Chromatography, Liquid</topic><topic>Drug Discovery</topic><topic>Electrons</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - growth & development</topic><topic>Hydrogels</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Annotation</topic><topic>Molecular Sequence Data</topic><topic>Particle Size</topic><topic>Proteomics - instrumentation</topic><topic>Proteomics - methods</topic><topic>Pseudomonas aeruginosa - drug effects</topic><topic>Pseudomonas aeruginosa - growth & development</topic><topic>Sequence Analysis, Protein - methods</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - growth & development</topic><topic>Tandem Mass Spectrometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Juba, Melanie L</creatorcontrib><creatorcontrib>Russo, Paul S</creatorcontrib><creatorcontrib>Devine, Megan</creatorcontrib><creatorcontrib>Barksdale, Stephanie</creatorcontrib><creatorcontrib>Rodriguez, Carlos</creatorcontrib><creatorcontrib>Vliet, Kent A</creatorcontrib><creatorcontrib>Schnur, Joel M</creatorcontrib><creatorcontrib>van Hoek, Monique L</creatorcontrib><creatorcontrib>Bishop, Barney M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Juba, Melanie L</au><au>Russo, Paul S</au><au>Devine, Megan</au><au>Barksdale, Stephanie</au><au>Rodriguez, Carlos</au><au>Vliet, Kent A</au><au>Schnur, Joel M</au><au>van Hoek, Monique L</au><au>Bishop, Barney M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Large Scale Discovery and De Novo-Assisted Sequencing of Cationic Antimicrobial Peptides (CAMPs) by Microparticle Capture and Electron-Transfer Dissociation (ETD) Mass Spectrometry</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2015-10-02</date><risdate>2015</risdate><volume>14</volume><issue>10</issue><spage>4282</spage><epage>4295</epage><pages>4282-4295</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>The identification and sequencing of novel cationic antimicrobial peptides (CAMPs) have proven challenging due to the limitations associated with traditional proteomics methods and difficulties sequencing peptides present in complex biomolecular mixtures. We present here a process for large-scale identification and de novo-assisted sequencing of newly discovered CAMPs using microparticle capture followed by tandem mass spectrometry equipped with electron-transfer dissociation (ETD). This process was initially evaluated and verified using known CAMPs with varying physicochemical properties. The effective parameters were then applied in the analysis of a complex mixture of peptides harvested from American alligator plasma using custom-made (Bioprospector) functionalized hydrogel particles. Here, we report the successful sequencing process for CAMPs that has led to the identification of 340 unique peptides and the discovery of five novel CAMPs from American alligator plasma.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>26327436</pmid><doi>10.1021/acs.jproteome.5b00447</doi><tpages>14</tpages></addata></record> |
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| subjects | Alligators and Crocodiles - blood Amino Acid Sequence Animals Antimicrobial Cationic Peptides - blood Antimicrobial Cationic Peptides - pharmacology Bacillus cereus - drug effects Bacillus cereus - growth & development Blood Proteins - chemistry Blood Proteins - isolation & purification Blood Proteins - pharmacology Chromatography, Liquid Drug Discovery Electrons Escherichia coli - drug effects Escherichia coli - growth & development Hydrogels Microbial Sensitivity Tests Molecular Sequence Annotation Molecular Sequence Data Particle Size Proteomics - instrumentation Proteomics - methods Pseudomonas aeruginosa - drug effects Pseudomonas aeruginosa - growth & development Sequence Analysis, Protein - methods Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Tandem Mass Spectrometry - methods |
| title | Large Scale Discovery and De Novo-Assisted Sequencing of Cationic Antimicrobial Peptides (CAMPs) by Microparticle Capture and Electron-Transfer Dissociation (ETD) Mass Spectrometry |
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