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

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-al...

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Autores principales: Thai Le, Son, Malinovska, Lenka, Vašková, Michaela, Mező, Erika, Kelemen, Viktor, Borbás, Anikó, Hodek, Petr, Wimmerová, Michaela, Csávás, Magdolna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6631993/
https://www.ncbi.nlm.nih.gov/pubmed/31216664
http://dx.doi.org/10.3390/molecules24122262
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author Thai Le, Son
Malinovska, Lenka
Vašková, Michaela
Mező, Erika
Kelemen, Viktor
Borbás, Anikó
Hodek, Petr
Wimmerová, Michaela
Csávás, Magdolna
author_facet Thai Le, Son
Malinovska, Lenka
Vašková, Michaela
Mező, Erika
Kelemen, Viktor
Borbás, Anikó
Hodek, Petr
Wimmerová, Michaela
Csávás, Magdolna
author_sort Thai Le, Son
collection PubMed
description 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.
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spelling pubmed-66319932019-08-19 Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin Thai Le, Son Malinovska, Lenka Vašková, Michaela Mező, Erika Kelemen, Viktor Borbás, Anikó Hodek, Petr Wimmerová, Michaela Csávás, Magdolna Molecules Article 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. MDPI 2019-06-18 /pmc/articles/PMC6631993/ /pubmed/31216664 http://dx.doi.org/10.3390/molecules24122262 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Thai Le, Son
Malinovska, Lenka
Vašková, Michaela
Mező, Erika
Kelemen, Viktor
Borbás, Anikó
Hodek, Petr
Wimmerová, Michaela
Csávás, Magdolna
Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title_full Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title_fullStr Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title_full_unstemmed Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title_short Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
title_sort investigation of the binding affinity of a broad array of l-fucosides with six fucose-specific lectins of bacterial and fungal origin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6631993/
https://www.ncbi.nlm.nih.gov/pubmed/31216664
http://dx.doi.org/10.3390/molecules24122262
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