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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00107484" target="_blank" >RIV/00216224:14740/19:00107484 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/19:10395492
Result on the web
<a href="https://www.mdpi.com/1420-3049/24/12/2262" target="_blank" >https://www.mdpi.com/1420-3049/24/12/2262</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/molecules24122262" target="_blank" >10.3390/molecules24122262</a>

Result language
angličtina
Original language name
Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
Original language 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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10400 - Chemical sciences

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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