Marcelo, Filipa; Javier Canada, Francisco; Andre, Sabine; Colombo, Cinzia; Doro, Fabio; Gabius, Hans-Joachim; Bernardi, Anna; Jiménez-Barbero, Jesús
α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands.
In: Organic & Biomolecular Chemistry, Vol. 10, No. 30: pp. 5916-5923
Natural N-glycosylation involves a β-anomeric linkage connecting the sugar to one asparagine residue of the protein. We herein report NMR- and modelling-based data on glycomimetics containing α-glycosidic linkages. The bioactivity of α-Gal-containing glycopeptides has been documented by revealing binding to two plant lectins, i.e. a potent β-trefoil toxin (Viscum album agglutinin) and β-sandwich lectin (Erythrina corallodendron agglutinin), by NMR protocols. Docking provided insights into the 3D structures of the resulting complexes. These results provide the basis to introduce α-substituted neoglycopeptides to the toolbox of scaffold for the design of potent lectin inhibitors.