To analyze the interaction between glycopeptides and receptor proteins, we synthesize peptides and glycopeptides to elucidate the function of the carbohydrates on the receptor-ligand interaction. Here, the glycopeptides mimic sections of the glycoproteins that cannot easily be handled as a ligand. We found a number of interactions where a mixed peptide-carbohydrate epitope is responsible for the binding process. We utilize microwave assisted peptide and glycopeptide synthesis on the solid phase as a routine protocol. These projects are aimed at identifying and characterizing protein-protein interactions that are involving carbohydrate components in the recognition by the receptor protein.
Epitope Mapping and Conformational Analysis of MUC-1 Glycopeptides and Peptides Bound to the Breast Cancer-selective Monoclonal Antibody SM3.
Heiko Möller, Nida Serttas, Hans Paulsen, Joyce Taylor-Papadimitriou, and Bernd Meyer,
Eur. J. Biochem. 269,1444-1455, (2002).
Synthesis and characterization of highly glycosylated glycopeptides with Tn antigenic structures of the human glycophorin AN.
G. Klich, H. Paulsen, B. Meyer, M. Meldal, K. Bock,
Carbohydr. Res. 299, 33-48 (1997).