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.

α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands / F. Marcelo, F.J. Cañada, S. André, C. Colombo, F. Doro, H. Gabius, A. Bernardi, J. Jiménez Barbero. - In: ORGANIC & BIOMOLECULAR CHEMISTRY. - ISSN 1477-0520. - 2012:30(2012), pp. 5916-5923. [10.1039/c2ob07135e]

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

C. Colombo;F. Doro;A. Bernardi;
2012

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.
Settore CHIM/06 - Chimica Organica
http://pubs.rsc.org/en/Content/ArticleLanding/2012/OB/c2ob07135e
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/220233
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