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Issue 30, 2012
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α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands

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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

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Publication details

The article was received on 19 Dec 2011, accepted on 29 Feb 2012 and first published on 01 Mar 2012


Article type: Paper
DOI: 10.1039/C2OB07135E
Citation: Org. Biomol. Chem., 2012,10, 5916-5923
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    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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