A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.
Identifieur interne : 002739 ( PubMed/Curation ); précédent : 002738; suivant : 002740A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.
Auteurs : Z H Huang [États-Unis] ; J. Wu ; K D Roth ; Y. Yang ; D A Gage ; J T WatsonSource :
- Analytical chemistry [ 0003-2700 ] ; 1997.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptides.
- chemical , chemistry : Peptides.
- chemical : Indicators and Reagents.
- methods : Sequence Analysis.
- Amino Acid Sequence, Mass Spectrometry, Molecular Sequence Data.
Abstract
A highly activated ester containing a fixed positive charge, S-pentafluorophenyl [tris(2,4,6-trimethoxyphenyl)phosphonium]acetate bromide (TMPP-AcSC6F5 bromide), has been synthesized as a reagent for N-terminal modification of peptides. Stable in aqueous acetonitrile solution during extended storage, TMPP-AcSC6F5 bromide reacts with unprotected peptides through p-(dimethylamino)pyridine (DMAP)-promoted amidation in aqueous acetonitrile (15 min, ambient temperature) to form N-TMPP-Ac derivatives of peptides. These peptide derivatives are readily amenable to analysis by fast atom bombardment (FAB) and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. Greater than 90% conversion has been observed in transforming low-nanomole quantities of analyte using molar ratios of 1:5:10 (peptide/reagent/ DMAP). For reactions at the picomole level a slightly modified stoichiometry, with molar ratios of 1:10:500, is employed. Owing to the high reaction efficiency and the tolerance to moderate excess reagent and base during analysis by FAB- and MALDI-MS, the reaction mixture containing the modified peptides can be analyzed directly in most cases, without sample cleanup. Examples of the preparation and analysis of a variety of N-TMPP-acetyl-peptides (TMPP-Ac-peptides) ranging from hexamers to 15-mers are given. Collisionally activated dissociation tandem mass spectrometry of TMPP-Ac-derivatives showed dominant a-type ions, accompanied by d- and c-type ions in some cases, allowing sequence determination to be made in a straightforward manner.
DOI: 10.1021/ac9608578
PubMed: 8997893
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :002739
Links to Exploration step
pubmed:8997893Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.</title><author><name sortKey="Huang, Z H" sort="Huang, Z H" uniqKey="Huang Z" first="Z H" last="Huang">Z H Huang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing 48824</wicri:regionArea></affiliation></author><author><name sortKey="Wu, J" sort="Wu, J" uniqKey="Wu J" first="J" last="Wu">J. Wu</name></author><author><name sortKey="Roth, K D" sort="Roth, K D" uniqKey="Roth K" first="K D" last="Roth">K D Roth</name></author><author><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></author><author><name sortKey="Gage, D A" sort="Gage, D A" uniqKey="Gage D" first="D A" last="Gage">D A Gage</name></author><author><name sortKey="Watson, J T" sort="Watson, J T" uniqKey="Watson J" first="J T" last="Watson">J T Watson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:8997893</idno><idno type="pmid">8997893</idno><idno type="doi">10.1021/ac9608578</idno><idno type="wicri:Area/PubMed/Corpus">002739</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002739</idno><idno type="wicri:Area/PubMed/Curation">002739</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002739</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.</title><author><name sortKey="Huang, Z H" sort="Huang, Z H" uniqKey="Huang Z" first="Z H" last="Huang">Z H Huang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing 48824</wicri:regionArea></affiliation></author><author><name sortKey="Wu, J" sort="Wu, J" uniqKey="Wu J" first="J" last="Wu">J. Wu</name></author><author><name sortKey="Roth, K D" sort="Roth, K D" uniqKey="Roth K" first="K D" last="Roth">K D Roth</name></author><author><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></author><author><name sortKey="Gage, D A" sort="Gage, D A" uniqKey="Gage D" first="D A" last="Gage">D A Gage</name></author><author><name sortKey="Watson, J T" sort="Watson, J T" uniqKey="Watson J" first="J T" last="Watson">J T Watson</name></author></analytic><series><title level="j">Analytical chemistry</title><idno type="ISSN">0003-2700</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Indicators and Reagents</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Peptides (analysis)</term><term>Peptides (chemistry)</term><term>Sequence Analysis (methods)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence ()</term><term>Données de séquences moléculaires</term><term>Indicateurs et réactifs</term><term>Peptides ()</term><term>Peptides (analyse)</term><term>Spectrométrie de masse</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Indicators and Reagents</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Sequence Analysis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence</term><term>Données de séquences moléculaires</term><term>Indicateurs et réactifs</term><term>Peptides</term><term>Spectrométrie de masse</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A highly activated ester containing a fixed positive charge, S-pentafluorophenyl [tris(2,4,6-trimethoxyphenyl)phosphonium]acetate bromide (TMPP-AcSC6F5 bromide), has been synthesized as a reagent for N-terminal modification of peptides. Stable in aqueous acetonitrile solution during extended storage, TMPP-AcSC6F5 bromide reacts with unprotected peptides through p-(dimethylamino)pyridine (DMAP)-promoted amidation in aqueous acetonitrile (15 min, ambient temperature) to form N-TMPP-Ac derivatives of peptides. These peptide derivatives are readily amenable to analysis by fast atom bombardment (FAB) and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. Greater than 90% conversion has been observed in transforming low-nanomole quantities of analyte using molar ratios of 1:5:10 (peptide/reagent/ DMAP). For reactions at the picomole level a slightly modified stoichiometry, with molar ratios of 1:10:500, is employed. Owing to the high reaction efficiency and the tolerance to moderate excess reagent and base during analysis by FAB- and MALDI-MS, the reaction mixture containing the modified peptides can be analyzed directly in most cases, without sample cleanup. Examples of the preparation and analysis of a variety of N-TMPP-acetyl-peptides (TMPP-Ac-peptides) ranging from hexamers to 15-mers are given. Collisionally activated dissociation tandem mass spectrometry of TMPP-Ac-derivatives showed dominant a-type ions, accompanied by d- and c-type ions in some cases, allowing sequence determination to be made in a straightforward manner.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8997893</PMID><DateCompleted><Year>1997</Year><Month>02</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-2700</ISSN><JournalIssue CitedMedium="Print"><Volume>69</Volume><Issue>2</Issue><PubDate><Year>1997</Year><Month>Jan</Month><Day>15</Day></PubDate></JournalIssue><Title>Analytical chemistry</Title><ISOAbbreviation>Anal. Chem.</ISOAbbreviation></Journal><ArticleTitle>A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.</ArticleTitle><Pagination><MedlinePgn>137-44</MedlinePgn></Pagination><Abstract><AbstractText>A highly activated ester containing a fixed positive charge, S-pentafluorophenyl [tris(2,4,6-trimethoxyphenyl)phosphonium]acetate bromide (TMPP-AcSC6F5 bromide), has been synthesized as a reagent for N-terminal modification of peptides. Stable in aqueous acetonitrile solution during extended storage, TMPP-AcSC6F5 bromide reacts with unprotected peptides through p-(dimethylamino)pyridine (DMAP)-promoted amidation in aqueous acetonitrile (15 min, ambient temperature) to form N-TMPP-Ac derivatives of peptides. These peptide derivatives are readily amenable to analysis by fast atom bombardment (FAB) and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. Greater than 90% conversion has been observed in transforming low-nanomole quantities of analyte using molar ratios of 1:5:10 (peptide/reagent/ DMAP). For reactions at the picomole level a slightly modified stoichiometry, with molar ratios of 1:10:500, is employed. Owing to the high reaction efficiency and the tolerance to moderate excess reagent and base during analysis by FAB- and MALDI-MS, the reaction mixture containing the modified peptides can be analyzed directly in most cases, without sample cleanup. Examples of the preparation and analysis of a variety of N-TMPP-acetyl-peptides (TMPP-Ac-peptides) ranging from hexamers to 15-mers are given. Collisionally activated dissociation tandem mass spectrometry of TMPP-Ac-derivatives showed dominant a-type ions, accompanied by d- and c-type ions in some cases, allowing sequence determination to be made in a straightforward manner.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Z H</ForeName><Initials>ZH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Roth</LastName><ForeName>K D</ForeName><Initials>KD</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Gage</LastName><ForeName>D A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Watson</LastName><ForeName>J T</ForeName><Initials>JT</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>RR00480</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Chem</MedlineTA><NlmUniqueID>0370536</NlmUniqueID><ISSNLinking>0003-2700</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007202">Indicators and Reagents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007202" MajorTopicYN="N">Indicators and Reagents</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017421" MajorTopicYN="N">Sequence Analysis</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>1</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>1</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>1</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8997893</ArticleId><ArticleId IdType="doi">10.1021/ac9608578</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002739 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 002739 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:8997893
|texte= A picomole-scale method for charge derivatization of peptides for sequence analysis by mass spectrometry.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:8997893" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |