The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry
Identifieur interne : 000595 ( Istex/Corpus ); précédent : 000594; suivant : 000596The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry
Auteurs : Sabine Baumgart ; Yvonne Lindner ; Ronald Kühne ; Axel Oberemm ; Holger Wenschuh ; Eberhard KrauseSource :
- Rapid Communications in Mass Spectrometry [ 0951-4198 ] ; 2004-04-30.
Abstract
Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) analysis of complex peptide mixtures is often hampered by signal suppression effects as well as certain intrinsic properties of specific peptides that influence the desorption/ionization behavior. The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.
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DOI: 10.1002/rcm.1416
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Berlin, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: ekrause@fmp‐berlin.de</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Rapid Communications in Mass Spectrometry</title><title level="j" type="alt">RAPID COMMUNICATIONS IN MASS SPECTROMETRY</title><idno type="ISSN">0951-4198</idno><idno type="eISSN">1097-0231</idno><imprint><biblScope unit="vol">18</biblScope><biblScope unit="issue">8</biblScope><biblScope unit="page" from="863">863</biblScope><biblScope unit="page" to="868">868</biblScope><biblScope unit="page-count">8</biblScope><publisher>John Wiley & Sons, Ltd.</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2004-04-30">2004-04-30</date></imprint><idno 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The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. 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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) analysis of complex peptide mixtures is often hampered by signal suppression effects as well as certain intrinsic properties of specific peptides that influence the desorption/ionization behavior. The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.</p></abstract><textClass><keywords rend="articleCategory"><term>Research Article</term></keywords><keywords rend="tocHeading1"><term>Research Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-6MRMBLLB-R/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Ltd.</publisherName><publisherLoc>Chichester, UK</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-0231</doi><issn type="print">0951-4198</issn><issn type="electronic">1097-0231</issn><idGroup><id type="product" value="RCM"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="RAPID COMMUNICATIONS IN MASS SPECTROMETRY">Rapid Communications in Mass Spectrometry</title><title type="short">Rapid Commun. Mass Spectrom.</title></titleGroup></publicationMeta><publicationMeta level="part" position="80"><doi origin="wiley" registered="yes">10.1002/rcm.v18:8</doi><numberingGroup><numbering type="journalVolume" number="18">18</numbering><numbering type="journalIssue">8</numbering></numberingGroup><coverDate startDate="2004-04-30">30 April 2004</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="6" status="forIssue"><doi origin="wiley" registered="yes">10.1002/rcm.1416</doi><idGroup><id type="unit" value="RCM1416"></id></idGroup><countGroup><count type="pageTotal" number="8"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">Research Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2004 John Wiley & Sons, Ltd.</copyright><eventGroup><event type="manuscriptReceived" date="2003-11-20"></event><event type="manuscriptRevised" date="2004-02-13"></event><event type="manuscriptAccepted" date="2004-02-13"></event><event type="firstOnline" date="2004-03-17"></event><event type="publishedOnlineFinalForm" date="2004-03-17"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.1 mode:FullText source:FullText result:FullText" date="2010-02-20"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-07"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-03"></event></eventGroup><numberingGroup><numbering type="pageFirst">863</numbering><numbering type="pageLast">868</numbering></numberingGroup><correspondenceTo>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:RCM.RCM1416.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="3"></count><count type="tableTotal" number="1"></count><count type="referenceTotal" number="35"></count></countGroup><titleGroup><title type="main" xml:lang="en">The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry</title><title type="short" xml:lang="en">Amino acid contributions to MALDI intensities of peptides</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" currentRef="#curr1"><personName><givenNames>Sabine</givenNames><familyName>Baumgart</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Yvonne</givenNames><familyName>Lindner</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Ronald</givenNames><familyName>Kühne</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Axel</givenNames><familyName>Oberemm</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Holger</givenNames><familyName>Wenschuh</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Eberhard</givenNames><familyName>Krause</familyName></personName><contactDetails><email normalForm="ekrause@fmp-berlin.de">ekrause@fmp‐berlin.de</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="DE" type="organization"><unparsedAffiliation>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="DE" type="organization"><unparsedAffiliation>Bundesinstitut für Risikobewertung, Thielallee 88–92, 14195 Berlin, Germany</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="DE" type="organization"><unparsedAffiliation>Jerini AG, Invalidenstr. 130, 10115 Berlin, Germany</unparsedAffiliation></affiliation><affiliation xml:id="curr1"><unparsedAffiliation>Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.</unparsedAffiliation></affiliation></affiliationGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) analysis of complex peptide mixtures is often hampered by signal suppression effects as well as certain intrinsic properties of specific peptides that influence the desorption/ionization behavior. The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Amino acid contributions to MALDI intensities of peptides</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry</title></titleInfo><name type="personal"><namePart type="given">Sabine</namePart><namePart type="family">Baumgart</namePart><affiliation>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany</affiliation><affiliation>Current Address: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yvonne</namePart><namePart type="family">Lindner</namePart><affiliation>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ronald</namePart><namePart type="family">Kühne</namePart><affiliation>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Axel</namePart><namePart type="family">Oberemm</namePart><affiliation>Bundesinstitut für Risikobewertung, Thielallee 88–92, 14195 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Holger</namePart><namePart type="family">Wenschuh</namePart><affiliation>Jerini AG, Invalidenstr. 130, 10115 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eberhard</namePart><namePart type="family">Krause</namePart><affiliation>Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany</affiliation><affiliation>E-mail: ekrause@fmp‐berlin.de</affiliation><affiliation>Correspondence address: Forschungsinstitut für Molekulare Pharmakologie, Robert‐Rössle‐Str. 10, 13125 Berlin, Germany.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>John Wiley & Sons, Ltd.</publisher><place><placeTerm type="text">Chichester, UK</placeTerm></place><dateIssued encoding="w3cdtf">2004-04-30</dateIssued><dateCaptured encoding="w3cdtf">2003-11-20</dateCaptured><dateValid encoding="w3cdtf">2004-02-13</dateValid><copyrightDate encoding="w3cdtf">2004</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">3</extent><extent unit="tables">1</extent><extent unit="references">35</extent></physicalDescription><abstract lang="en">Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) analysis of complex peptide mixtures is often hampered by signal suppression effects as well as certain intrinsic properties of specific peptides that influence the desorption/ionization behavior. The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.</abstract><relatedItem type="host"><titleInfo><title>Rapid Communications in Mass Spectrometry</title></titleInfo><titleInfo type="abbreviated"><title>Rapid Commun. 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Mass Spectrom. 2003; 17: 1626.</note><name type="personal"><namePart type="given">S</namePart><namePart type="family">Mezzache</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C</namePart><namePart type="family">Afonso</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C</namePart><namePart type="family">Pepe</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P</namePart><namePart type="family">Karoyan</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">F</namePart><namePart type="family">Fournier</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">JC</namePart><namePart type="family">Tabet</namePart><role><roleTerm type="text">author</roleTerm></role></name><part><date>2003</date><detail type="volume"><caption>vol.</caption><number>17</number></detail><extent unit="pages"><start>1626</start></extent></part></relatedItem><identifier type="istex">664BB80E5A71259819AC9DB479A18CC286BC3EC5</identifier><identifier type="ark">ark:/67375/WNG-6MRMBLLB-R</identifier><identifier type="DOI">10.1002/rcm.1416</identifier><identifier type="ArticleID">RCM1416</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2004 John Wiley & Sons, Ltd.</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Converted from (version ) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2019-11-16</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-6MRMBLLB-R/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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