NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells

Wheat germ agglutinin (WGA) binding to the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope, a characteristic disaccharide of highly branched surface N-glycoconjugates that are malignancy markers, is investigated by combination of NMR and molecular modeling approaches. NMR experiments revealed that binding occurred in the region of the N-acetyl group of the terminal sugar residue and the O-methyl group received saturation transfer because of proximity to the protein.