Aryl fucosides: synthesis and evaluation of their binding affinity towards the DC-SIGN receptor

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22310%2F25%3A43931520" target="_blank" >RIV/60461373:22310/25:43931520 - isvavai.cz</a>
Result on the web
<a href="https://pubs.rsc.org/en/content/articlehtml/2025/ob/d5ob00472a" target="_blank" >https://pubs.rsc.org/en/content/articlehtml/2025/ob/d5ob00472a</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/d5ob00472a" target="_blank" >10.1039/d5ob00472a</a>

Result language
angličtina
Original language name
Aryl fucosides: synthesis and evaluation of their binding affinity towards the DC-SIGN receptor
Original language description
DC-SIGN, a C-type lectin receptor expressed on antigen presenting cells, is crucial for pathogen recognition and immune modulation. While most glycomimetic DC-SIGN ligands are mannose-based, fucose-based ligands offer enhanced selectivity, potentially reducing off-target effects. This study reports the stereoselective synthesis of aryl alpha-l-fucosides and their binding affinity for DC-SIGN. Using 1H-15N HSQC NMR and a competition assay, we identified 3-trifluoromethylphenyl alpha-l-fucoside as the best ligand, exhibiting both KD and IC50 values in a three-digit micromolar range and binding not only to the canonical site, but also to a secondary allosteric site.
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
10401 - Organic chemistry

Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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