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Open AccessArticle

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

1
Department of Pharmaceutical Chemistry, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary
2
Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic
3
National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlářská 2, 611 37 Brno, Czech Republic
4
Department of Biochemistry, Faculty of Science, Charles University, Albertov 2030, 128 40 Prague 2, Czech Republic
5
Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 611 37 Brno, Czech Republic
*
Authors to whom correspondence should be addressed.
These two authors contributed equally.
Academic Editor: Monica Fengsrud Brinchmann
Molecules 2019, 24(12), 2262; https://doi.org/10.3390/molecules24122262
Received: 25 April 2019 / Revised: 4 June 2019 / Accepted: 14 June 2019 / Published: 18 June 2019
(This article belongs to the Special Issue Functional Aspects of Lectins)
Series of multivalent α-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, α-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. View Full-Text
Keywords: l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis
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MDPI and ACS Style

Thai Le, S.; Malinovska, L.; Vašková, M.; Mező, E.; Kelemen, V.; Borbás, A.; Hodek, P.; Wimmerová, M.; Csávás, M. Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin. Molecules 2019, 24, 2262.

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