Mass spectrometric analysis of combinatorial peptide libraries derived from the tandem repeat unit of MUC2 mucin.
Identifieur interne : 002448 ( PubMed/Corpus ); précédent : 002447; suivant : 002449Mass spectrometric analysis of combinatorial peptide libraries derived from the tandem repeat unit of MUC2 mucin.
Auteurs : Gitta Schlosser ; Zoltán Takáts ; Károly Vékey ; Gabriella P Csfalvi ; Antonio Malorni ; Emöke Windberg ; Andrea Kiss ; Ferenc HudeczSource :
- Journal of peptide science : an official publication of the European Peptide Society [ 1075-2617 ] ; 2003.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Mucins.
- chemical , chemistry : Mucins.
- methods : Mass Spectrometry.
- Amino Acid Sequence, Combinatorial Chemistry Techniques, Humans, Molecular Sequence Data, Peptide Library, Repetitive Sequences, Amino Acid, Time Factors.
Abstract
Four 19-member synthetic peptide libraries, based on the TX1TX2T epitope motif of the mucin-2 gastrointestinal glycoprotein (MUC2) and ranging in peptide length from dipeptides to 15-mers (XT, TXT, TQTXT and KVTPTPTPTGTQTXT), were synthesized by combinatorial solid phase peptide synthesis using the portioning-mixing combinatorial approach, and analysed by electrospray ionization mass spectrometry at different (1000-10000) resolutions. Most of the components of the individual libraries could be easily identified in a single-stage molecular mass screening experiment. The resolving power of the instrument becomes an important factor above 800-1000 Da molecular mass, when predominantly multiply charged molecular ions are formed. Approaches to the identification of isobars (glutamine/lysine), isomers leucine/isoleucine) and sequence variations by tandem mass spectrometry, and/or by high-performance liquid chromatography-mass spectrometry are outlined.
DOI: 10.1002/psc.462
PubMed: 12846482
Links to Exploration step
pubmed:12846482Le document en format XML
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<author><name sortKey="Takats, Zoltan" sort="Takats, Zoltan" uniqKey="Takats Z" first="Zoltán" last="Takáts">Zoltán Takáts</name>
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<author><name sortKey="Vekey, Karoly" sort="Vekey, Karoly" uniqKey="Vekey K" first="Károly" last="Vékey">Károly Vékey</name>
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<author><name sortKey="P Csfalvi, Gabriella" sort="P Csfalvi, Gabriella" uniqKey="P Csfalvi G" first="Gabriella" last="P Csfalvi">Gabriella P Csfalvi</name>
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<author><name sortKey="Windberg, Emoke" sort="Windberg, Emoke" uniqKey="Windberg E" first="Emöke" last="Windberg">Emöke Windberg</name>
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<author><name sortKey="Kiss, Andrea" sort="Kiss, Andrea" uniqKey="Kiss A" first="Andrea" last="Kiss">Andrea Kiss</name>
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<term>Mucins (analysis)</term>
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<term>Peptide Library</term>
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<front><div type="abstract" xml:lang="en">Four 19-member synthetic peptide libraries, based on the TX1TX2T epitope motif of the mucin-2 gastrointestinal glycoprotein (MUC2) and ranging in peptide length from dipeptides to 15-mers (XT, TXT, TQTXT and KVTPTPTPTGTQTXT), were synthesized by combinatorial solid phase peptide synthesis using the portioning-mixing combinatorial approach, and analysed by electrospray ionization mass spectrometry at different (1000-10000) resolutions. Most of the components of the individual libraries could be easily identified in a single-stage molecular mass screening experiment. The resolving power of the instrument becomes an important factor above 800-1000 Da molecular mass, when predominantly multiply charged molecular ions are formed. Approaches to the identification of isobars (glutamine/lysine), isomers leucine/isoleucine) and sequence variations by tandem mass spectrometry, and/or by high-performance liquid chromatography-mass spectrometry are outlined.</div>
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<Abstract><AbstractText>Four 19-member synthetic peptide libraries, based on the TX1TX2T epitope motif of the mucin-2 gastrointestinal glycoprotein (MUC2) and ranging in peptide length from dipeptides to 15-mers (XT, TXT, TQTXT and KVTPTPTPTGTQTXT), were synthesized by combinatorial solid phase peptide synthesis using the portioning-mixing combinatorial approach, and analysed by electrospray ionization mass spectrometry at different (1000-10000) resolutions. Most of the components of the individual libraries could be easily identified in a single-stage molecular mass screening experiment. The resolving power of the instrument becomes an important factor above 800-1000 Da molecular mass, when predominantly multiply charged molecular ions are formed. Approaches to the identification of isobars (glutamine/lysine), isomers leucine/isoleucine) and sequence variations by tandem mass spectrometry, and/or by high-performance liquid chromatography-mass spectrometry are outlined.</AbstractText>
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