Publication details

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

Authors

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

Year of publication 2019
Type Article in Periodical
Magazine / Source Molecules
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://www.mdpi.com/1420-3049/24/12/2262
Doi http://dx.doi.org/10.3390/molecules24122262
Keywords l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis
Description 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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