Mass spectrometric analysis of combinatorial peptide libraries derived from the tandem repeat unit of MUC2 mucin

Gitta Schlosser, Zoltán Takátz, Károly Vékey, Gabriella Pócsfalvi, Antonio Malorni, Emöke Windberg, Andrea Kiss, Ferenc Hudecz

Research output: Contribution to journalReview article

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)361-374
Number of pages14
JournalJournal of Peptide Science
Issue number6
Publication statusPublished - Jun 1 2003



  • Combinatorial chemistry
  • Mass spectrometry
  • Mucin-2 glycoprotein
  • Partioning-mixing
  • Peptide library
  • Tandem mass spectrometry

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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