Issue 30, 2012

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

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.

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

Supplementary files

Article information

Article type
Paper
Submitted
19 dec 2011
Accepted
29 feb 2012
First published
01 mar 2012

Org. Biomol. Chem., 2012,10, 5916-5923

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 and J. Jiménez-Barbero, Org. Biomol. Chem., 2012, 10, 5916 DOI: 10.1039/C2OB07135E

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