In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.
Identifieur interne : 000C89 ( Main/Exploration ); précédent : 000C88; suivant : 000C90In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.
Auteurs : RBID : pubmed:23019160English descriptors
- KwdEn :
- Amino Acid Sequence, Caseins (chemistry), Models, Chemical, Molecular Sequence Data, Peptide Fragments (chemistry), Peptide Fragments (isolation & purification), Phosphopeptides (chemistry), Phosphopeptides (isolation & purification), Phosphorylation, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (instrumentation), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (methods), Trehalase (chemistry), Trypsin (chemistry), Zirconium (chemistry).
- MESH :
- chemical , chemistry : Caseins, Peptide Fragments, Phosphopeptides, Trehalase, Trypsin, Zirconium.
- chemical , isolation & purification : Peptide Fragments, Phosphopeptides.
- instrumentation : Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- methods : Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- Amino Acid Sequence, Models, Chemical, Molecular Sequence Data, Phosphorylation.
Abstract
We report substantial in-situ enrichment of phosphopeptides in peptide mixtures using titanium and zirconium dioxide-coated matrix assisted laser desorption-ionization (MALDI) plates prepared by recently reported ambient ion landing deposition technique. The technique was able to modify four common materials currently used for MALDI targets (stainless steel, aluminum, indium-tin oxide glass and polymeric anchor chip). The structure of the deposited dioxide was investigated by electron microscopy, and different surfaces were compared and discussed in this study. Two standard proteins were used to test the enrichment capabilities of modified MALDI plates: casein and in-vitro phosphorylated trehalase. The enrichment of casein tryptic digest resulted in identification of 20 phosphopeptides (including miscleavages). Trehalase was used as a suitable model of larger protein that provided more complex peptide mixture after the trypsin digestion. All four possible phosphorylation sites in trehalase were identified and up to seven phosphopetides were found (including methionine oxidations and miscleavages). Two different mass spectrometers, MALDI-Fourier transform ion cyclotron resonance (FTICR) and MALDI-time of flight, were used to detect the phosphopeptides from modified MALDI plates after the enrichment procedure. It was observed that the desorption-ionization phenomena on the modified surfaces are not critically influenced by the parameters of the different MALDI ion sources (e.g. different pressure, different extraction voltages), and thus the presence of dioxide layer on the standard MALDI plate does not significantly interfere with the main MALDI processes. The detection of phosphopeptides after the enrichment could be done by both instruments. Desorption electrospray ionization coupled to the FTICR was also tested, but, unlike MALDI, it did not provide satisfactory results.
DOI: 10.1002/jms.3081
PubMed: 23019160
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.</title><author><name sortKey="Kr Sn, Luk" uniqKey="Kr Sn L">Lukáš Krásný</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology of the ASCR, vvi, Prague, Czech Republic.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Institute of Microbiology of the ASCR, vvi, Prague</wicri:regionArea></affiliation></author><author><name sortKey="Pompach, Petr" uniqKey="Pompach P">Petr Pompach</name></author><author><name sortKey="Strohalm, Martin" uniqKey="Strohalm M">Martin Strohalm</name></author><author><name sortKey="Obsilova, Veronika" uniqKey="Obsilova V">Veronika Obsilova</name></author><author><name sortKey="Strnadov, Marcela" uniqKey="Strnadov M">Marcela Strnadová</name></author><author><name sortKey="Nov K, Petr" uniqKey="Nov K P">Petr Novák</name></author><author><name sortKey="Voln, Michael" uniqKey="Voln M">Michael Volný</name></author></titleStmt><publicationStmt><date when="2012">2012</date><idno type="doi">10.1002/jms.3081</idno><idno type="RBID">pubmed:23019160</idno><idno type="pmid">23019160</idno><idno type="wicri:Area/Main/Corpus">000A26</idno><idno type="wicri:Area/Main/Curation">000A26</idno><idno type="wicri:Area/Main/Exploration">000C89</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Caseins (chemistry)</term><term>Models, Chemical</term><term>Molecular Sequence Data</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (isolation & purification)</term><term>Phosphopeptides (chemistry)</term><term>Phosphopeptides (isolation & purification)</term><term>Phosphorylation</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (instrumentation)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (methods)</term><term>Trehalase (chemistry)</term><term>Trypsin (chemistry)</term><term>Zirconium (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Caseins</term><term>Peptide Fragments</term><term>Phosphopeptides</term><term>Trehalase</term><term>Trypsin</term><term>Zirconium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Peptide Fragments</term><term>Phosphopeptides</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Chemical</term><term>Molecular Sequence Data</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report substantial in-situ enrichment of phosphopeptides in peptide mixtures using titanium and zirconium dioxide-coated matrix assisted laser desorption-ionization (MALDI) plates prepared by recently reported ambient ion landing deposition technique. The technique was able to modify four common materials currently used for MALDI targets (stainless steel, aluminum, indium-tin oxide glass and polymeric anchor chip). The structure of the deposited dioxide was investigated by electron microscopy, and different surfaces were compared and discussed in this study. Two standard proteins were used to test the enrichment capabilities of modified MALDI plates: casein and in-vitro phosphorylated trehalase. The enrichment of casein tryptic digest resulted in identification of 20 phosphopeptides (including miscleavages). Trehalase was used as a suitable model of larger protein that provided more complex peptide mixture after the trypsin digestion. All four possible phosphorylation sites in trehalase were identified and up to seven phosphopetides were found (including methionine oxidations and miscleavages). Two different mass spectrometers, MALDI-Fourier transform ion cyclotron resonance (FTICR) and MALDI-time of flight, were used to detect the phosphopeptides from modified MALDI plates after the enrichment procedure. It was observed that the desorption-ionization phenomena on the modified surfaces are not critically influenced by the parameters of the different MALDI ion sources (e.g. different pressure, different extraction voltages), and thus the presence of dioxide layer on the standard MALDI plate does not significantly interfere with the main MALDI processes. The detection of phosphopeptides after the enrichment could be done by both instruments. Desorption electrospray ionization coupled to the FTICR was also tested, but, unlike MALDI, it did not provide satisfactory results.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">23019160</PMID><DateCreated><Year>2012</Year><Month>09</Month><Day>28</Day></DateCreated><DateCompleted><Year>2013</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1096-9888</ISSN><JournalIssue CitedMedium="Internet"><Volume>47</Volume><Issue>10</Issue><PubDate><Year>2012</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of mass spectrometry : JMS</Title><ISOAbbreviation>J Mass Spectrom</ISOAbbreviation></Journal><ArticleTitle>In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.</ArticleTitle><Pagination><MedlinePgn>1294-302</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/jms.3081</ELocationID><Abstract><AbstractText>We report substantial in-situ enrichment of phosphopeptides in peptide mixtures using titanium and zirconium dioxide-coated matrix assisted laser desorption-ionization (MALDI) plates prepared by recently reported ambient ion landing deposition technique. The technique was able to modify four common materials currently used for MALDI targets (stainless steel, aluminum, indium-tin oxide glass and polymeric anchor chip). The structure of the deposited dioxide was investigated by electron microscopy, and different surfaces were compared and discussed in this study. Two standard proteins were used to test the enrichment capabilities of modified MALDI plates: casein and in-vitro phosphorylated trehalase. The enrichment of casein tryptic digest resulted in identification of 20 phosphopeptides (including miscleavages). Trehalase was used as a suitable model of larger protein that provided more complex peptide mixture after the trypsin digestion. All four possible phosphorylation sites in trehalase were identified and up to seven phosphopetides were found (including methionine oxidations and miscleavages). Two different mass spectrometers, MALDI-Fourier transform ion cyclotron resonance (FTICR) and MALDI-time of flight, were used to detect the phosphopeptides from modified MALDI plates after the enrichment procedure. It was observed that the desorption-ionization phenomena on the modified surfaces are not critically influenced by the parameters of the different MALDI ion sources (e.g. different pressure, different extraction voltages), and thus the presence of dioxide layer on the standard MALDI plate does not significantly interfere with the main MALDI processes. The detection of phosphopeptides after the enrichment could be done by both instruments. Desorption electrospray ionization coupled to the FTICR was also tested, but, unlike MALDI, it did not provide satisfactory results.</AbstractText><CopyrightInformation>Copyright © 2012 John Wiley & Sons, Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Krásný</LastName><ForeName>Lukáš</ForeName><Initials>L</Initials><Affiliation>Institute of Microbiology of the ASCR, vvi, Prague, Czech Republic.</Affiliation></Author><Author ValidYN="Y"><LastName>Pompach</LastName><ForeName>Petr</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Strohalm</LastName><ForeName>Martin</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Obsilova</LastName><ForeName>Veronika</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Strnadová</LastName><ForeName>Marcela</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Novák</LastName><ForeName>Petr</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Volný</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mass Spectrom</MedlineTA><NlmUniqueID>9504818</NlmUniqueID><ISSNLinking>1076-5174</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Caseins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Phosphopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>C6V6S92N3C</RegistryNumber><NameOfSubstance>Zirconium</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.28</RegistryNumber><NameOfSubstance>Trehalase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance>Trypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>S38N85C5G0</RegistryNumber><NameOfSubstance>zirconium oxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Caseins</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName><QualifierName MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Phosphopeptides</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName><QualifierName MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName><QualifierName MajorTopicYN="Y">instrumentation</QualifierName><QualifierName MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Trehalase</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Trypsin</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Zirconium</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>9</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>9</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1002/jms.3081</ArticleId><ArticleId IdType="pubmed">23019160</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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