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

Filipa Marcelo, Francisco Javier Cañada, Sabine André, Cinzia Colombo, Fabio Doro, Hans Joachim Gabius, Anna Bernardi, Jesús Jiménez-Barbero

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7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)5916-5923
Number of pages8
JournalOrganic and Biomolecular Chemistry
Volume10
Issue number30
DOIs
Publication statusPublished - 14 Aug 2012

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Marcelo, F., Cañada, F. J., André, S., Colombo, C., Doro, F., Gabius, H. J., ... Jiménez-Barbero, J. (2012). α-N-Linked glycopeptides: Conformational analysis and bioactivity as lectin ligands. Organic and Biomolecular Chemistry, 10(30), 5916-5923. https://doi.org/10.1039/c2ob07135e