Comparative analysis of sulfated and ...
Document type :
Article dans une revue scientifique: Article original
DOI :
Permalink :
Title :
Comparative analysis of sulfated and sulfonated disaccharide analogs as TLR4 modulators and heparanase inhibitors
Author(s) :
El-Abid, Jamal [Auteur]
Koffi Teki, Dindet Steve-Evanes K. L. C. [Auteur]
Bil, Abed [Auteur]
Denys, Agnes [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Vallin, Aurélie [Auteur]
Lefebvre, Corentin [Auteur]
Allain, Fabrice [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Chagnault, Vincent [Auteur]
Kovensky, José [Auteur]
Koffi Teki, Dindet Steve-Evanes K. L. C. [Auteur]
Bil, Abed [Auteur]
Denys, Agnes [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Vallin, Aurélie [Auteur]
Lefebvre, Corentin [Auteur]
Allain, Fabrice [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Chagnault, Vincent [Auteur]
Kovensky, José [Auteur]
Journal title :
New Journal of Chemistry
Abbreviated title :
New J. Chem.
Volume number :
48
Pages :
9559-9566
Publisher :
Royal Society of Chemistry
Publication date :
2024-04-26
ISSN :
1144-0546
English keyword(s) :
Toll-like receptors
III Binding domain
Endogenous ligands
Drosophila
Immunity
Heparin
III Binding domain
Endogenous ligands
Drosophila
Immunity
Heparin
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
English abstract : [en]
This article delves into the synthesis and biological evaluation of sulfated and sulfonated disaccharide analogs, exploring their interactions with toll-like receptor 4 (TLR4) and their potential as drug candidates for ...
Show more >This article delves into the synthesis and biological evaluation of sulfated and sulfonated disaccharide analogs, exploring their interactions with toll-like receptor 4 (TLR4) and their potential as drug candidates for inflammatory diseases. A significant aspect of the study is the examination of these analogs as inhibitors of heparanase, an enzyme that cleaves glycosidic linkages in heparan sulfate, producing proinflammatory fragments that activate TLR4. The research presents a comparative analysis of sulfate and sulfonate groups in these compounds, evaluating their synthesis, biological activity, and specific roles in TLR4-mediated immune responses, with a particular focus on their ability to modulate heparanase activity. Compound 9 (6,6′-disulfonated disaccharide from methyl cellobioside) emerged as a potent TLR4 activator and a promising candidate for inflammatory drug development, exhibiting notable specificity and efficacy. The IC50 values for heparanase inhibition varied, highlighting distinct efficacy profiles for sulfonated and sulfated analogs, with cellobiose derivatives showing notable differences in inhibition capabilities.Show less >
Show more >This article delves into the synthesis and biological evaluation of sulfated and sulfonated disaccharide analogs, exploring their interactions with toll-like receptor 4 (TLR4) and their potential as drug candidates for inflammatory diseases. A significant aspect of the study is the examination of these analogs as inhibitors of heparanase, an enzyme that cleaves glycosidic linkages in heparan sulfate, producing proinflammatory fragments that activate TLR4. The research presents a comparative analysis of sulfate and sulfonate groups in these compounds, evaluating their synthesis, biological activity, and specific roles in TLR4-mediated immune responses, with a particular focus on their ability to modulate heparanase activity. Compound 9 (6,6′-disulfonated disaccharide from methyl cellobioside) emerged as a potent TLR4 activator and a promising candidate for inflammatory drug development, exhibiting notable specificity and efficacy. The IC50 values for heparanase inhibition varied, highlighting distinct efficacy profiles for sulfonated and sulfated analogs, with cellobiose derivatives showing notable differences in inhibition capabilities.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Diversité structurale des héparanes sulfates et régulation de la réponse inflammatoire
Submission date :
2025-01-20T12:52:58Z
2025-01-23T14:28:50Z
2025-01-23T14:28:50Z
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