Informace o publikaci

Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin

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THAI LE Son MALINOVSKÁ Lenka VAŠKOVÁ Michaela MEZO Erika KELEMEN Viktor BORBÁS Anikó HODEK Petr WIMMEROVÁ Michaela CSÁVÁS Magdolna

Rok publikování 2019
Druh Článek v odborném periodiku
Časopis / Zdroj Molecules
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.mdpi.com/1420-3049/24/12/2262
Doi http://dx.doi.org/10.3390/molecules24122262
Klíčová slova l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis
Popis Series of multivalent alpha-l-fucoside containing glycoclusters and variously decorated l-fucosides were synthesized to find potential inhibitors of fucose-specific lectins and study the structure-binding affinity relationships. Tri- and tetravalent fucoclusters were built using copper-mediated azide-alkyne click chemistry. Series of fucoside monomers and dimers were synthesized using various methods, namely glycosylation, an azide-alkyne click reaction, photoinduced thiol-en addition, and sulfation. The interactions between compounds with six fucolectins of bacterial or fungal origin were tested using a hemagglutination inhibition assay. As a result, a tetravalent, aplha-l-fucose presenting glycocluster showed to be a ligand that was orders of magnitude better than a simple monosaccharide for tested lectins in most cases, which can nominate it as a universal ligand for studied lectins. This compound was also able to inhibit the adhesion of Pseudomonas aeruginosa cells to human epithelial bronchial cells. A trivalent fucocluster with a protected amine functional group also seems to be a promising candidate for designing glycoconjugates and chimeras.
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