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  • Title: Tetravalent glycocyclopeptide with nanomolar affinity to wheat germ agglutinin.
    Author: Fiore M, Berthet N, Marra A, Gillon E, Dumy P, Dondoni A, Imberty A, Renaudet O.
    Journal: Org Biomol Chem; 2013 Nov 07; 11(41):7113-22. PubMed ID: 24057055.
    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 × 10(6) 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.
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