α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands

Marcelo, Filipa; Javier Canada, Francisco; André, Sabine; Colombo, Cinzia; Doro, Fabio; Gabius, Hans-Joachim; Bernardi, Anna and Jiménez-Barbero, Jesús (2012): α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands. In: Organic & Biomolecular Chemistry, Vol. 10, No. 30: pp. 5916-5923

Abstract

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.

• Item Type: Journal article
• Form of publication: Publisher's Version
• Faculties: Veterinary Medicine
• Subjects: 500 Science > 540 Chemistry
• ISSN: 1477-0520
• Alliance/National Licence: This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively.
• Language: English