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Issue 41, 2013
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Tetravalent glycocyclopeptide with nanomolar affinity to wheat germ agglutinin

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Abstract

A series of tetravalent glycocyclopeptides functionalized with GlcNAc was synthesized using copper(I)-catalysed alkyne–azide cycloaddition, oxime ligation and thiol–ene coupling. The binding ability of these compounds towards wheat germ agglutinin was studied by a competitive ELLA test and ITC experiments. While all compounds were able to inhibit WGA binding to GlcNAc-polymer coated surfaces at low concentrations, derivative 17 having an aliphatic spacer and thioether linkage was 4.9 × 106 times more potent on a per sugar basis than GlcNAc. This remarkably strong effect was confirmed by ITC experiments as these revealed an association constant of 9 nM for this compound, therefore presenting a gain of 200 000 times over GlcNAc. These results for compound 17 represent the highest binding properties reported for WGA.

Graphical abstract: Tetravalent glycocyclopeptide with nanomolar affinity to wheat germ agglutinin

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Publication details

The article was received on 11 Jun 2013, accepted on 23 Jul 2013 and first published on 23 Jul 2013


Article type: Paper
DOI: 10.1039/C3OB41203B
Citation: Org. Biomol. Chem., 2013,11, 7113-7122
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    Tetravalent glycocyclopeptide with nanomolar affinity to wheat germ agglutinin

    M. Fiore, N. Berthet, A. Marra, E. Gillon, P. Dumy, A. Dondoni, A. Imberty and O. Renaudet, Org. Biomol. Chem., 2013, 11, 7113
    DOI: 10.1039/C3OB41203B

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