Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
| Authors | |
|---|---|
| Year of publication | 2019 |
| Type | Article in Periodical |
| Magazine / Source | Molecules |
| MU Faculty or unit | |
| 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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