Solution structure of the all l- and d-amino acid-substituted mucin 2 epitope peptides

Orsolya Toke, Regina Tugyi, Katalin Uray, Ferenc Hudecz

Research output: Contribution to journalArticle

4 Citations (Scopus)


High-molecular-weight mucin 2 (MUC2) glycoproteins show an aberrant glycosylation pattern when expressed in human colon carcinoma: the oligosaccharide chains are shorter and some are missing. In our ongoing effort of MUC2 vaccine development, we have solved the NMR structure of the all l-amino acid and various d-amino acid-substituted derivatives of the peptide TPTPTGTQTPT, previously identified as an epitope within the tandem repeat unit of the MUC2 glycoprotein. In the all l-amino acid containing peptide and in peptide tpTPTGTQtpt (where lowercase letters mark the position of d-amino acids) we identified a type I β-turn spanning through residues 3TPTG6 and 5TGTQ8, respectively. Our structural findings are in good agreement with the antibody recognition properties of the investigated peptides and demonstrate that peptides with good stability against enzymatic degradation can be designed with good antibody binding characteristics.

Original languageEnglish
Pages (from-to)739-742
Number of pages4
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - Jul 6 2007



  • Antibody binding
  • Enzymatic stability
  • Epitope
  • MUC2
  • Mucin
  • NMR spectroscopy
  • Synthetic peptides
  • Synthetic vaccines
  • d-Amino acid substitution
  • β-Turn conformation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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