Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation

Readily accessible, low-valency glycoclusters based on a triazine core bearing D-galactose and L-fucose epitopes are able to inhibit biofilm formation by Pseudomonas aeruginosa. These multivalent ligands are simple to synthesize, are highly soluble, and can be either homofunctional or heterofunction...

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Detalles Bibliográficos
Autores principales: Smadhi, Meriem, de Bentzmann, Sophie, Imberty, Anne, Gingras, Marc, Abderrahim, Raoudha, Goekjian, Peter G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2014
Materias:
Full Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4168900/
https://www.ncbi.nlm.nih.gov/pubmed/25246957
http://dx.doi.org/10.3762/bjoc.10.206
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author Smadhi, Meriem
de Bentzmann, Sophie
Imberty, Anne
Gingras, Marc
Abderrahim, Raoudha
Goekjian, Peter G
author_facet Smadhi, Meriem
de Bentzmann, Sophie
Imberty, Anne
Gingras, Marc
Abderrahim, Raoudha
Goekjian, Peter G
author_sort Smadhi, Meriem
collection PubMed
description Readily accessible, low-valency glycoclusters based on a triazine core bearing D-galactose and L-fucose epitopes are able to inhibit biofilm formation by Pseudomonas aeruginosa. These multivalent ligands are simple to synthesize, are highly soluble, and can be either homofunctional or heterofunctional. The galactose-decorated cluster shows good affinity for Pseudomonas aeruginosa lectin lecA. They are convenient biological probes for investigating the roles of lecA and lecB in biofilm formation.
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spelling pubmed-41689002014-09-22 Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation Smadhi, Meriem de Bentzmann, Sophie Imberty, Anne Gingras, Marc Abderrahim, Raoudha Goekjian, Peter G Beilstein J Org Chem Full Research Paper Readily accessible, low-valency glycoclusters based on a triazine core bearing D-galactose and L-fucose epitopes are able to inhibit biofilm formation by Pseudomonas aeruginosa. These multivalent ligands are simple to synthesize, are highly soluble, and can be either homofunctional or heterofunctional. The galactose-decorated cluster shows good affinity for Pseudomonas aeruginosa lectin lecA. They are convenient biological probes for investigating the roles of lecA and lecB in biofilm formation. Beilstein-Institut 2014-08-25 /pmc/articles/PMC4168900/ /pubmed/25246957 http://dx.doi.org/10.3762/bjoc.10.206 Text en Copyright © 2014, Smadhi et al. https://creativecommons.org/licenses/by/2.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)
spellingShingle Full Research Paper
Smadhi, Meriem
de Bentzmann, Sophie
Imberty, Anne
Gingras, Marc
Abderrahim, Raoudha
Goekjian, Peter G
Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title_full Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title_fullStr Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title_full_unstemmed Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title_short Expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of Pseudomonas aeruginosa biofilm formation
title_sort expeditive synthesis of trithiotriazine-cored glycoclusters and inhibition of pseudomonas aeruginosa biofilm formation
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4168900/
https://www.ncbi.nlm.nih.gov/pubmed/25246957
http://dx.doi.org/10.3762/bjoc.10.206
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