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Mass spectrometric analysis of combinatorial peptide libraries derived from the tandem repeat unit of MUC2 mucin
Author(s) -
Schlosser Gitta,
Takáts Zoltán,
Vékey Károly,
Pócsfalvi Gabriella,
Malorni Antonio,
Windberg Emöke,
Kiss Andrea,
Hudecz Ferenc
Publication year - 2003
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.462
Subject(s) - chemistry , peptide , protein mass spectrometry , mass spectrometry , tandem mass spectrometry , electrospray ionization , molecular mass , chromatography , isobaric labeling , peptide synthesis , combinatorial chemistry , biochemistry , enzyme
Four 19‐member synthetic peptide libraries, based on the TX 1 TX 2 T 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 (1000–10 000) 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. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.