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Article Dans Une Revue Bioconjugate Chemistry Année : 2018

Multivalent Glycomimetics with Affinity and Selectivity toward Fucose-Binding Receptors from Emerging Pathogens

Résumé

Bacterial and fungal pathogens involved in lung infection in cystic fibrosis patients utilize a particular family of glycan-binding proteins, characterized by the presentation of six fucose-binding sites on a ring shape scaffold. These lectins are attractive targets for anti-infectious compounds that could interfere in the recognition of host tissues by pathogens. The design of a cyclopeptide-based hexavalent structure allowed for the presentation of six fucose residues. The synthetic hexavalent compound displays appropriate geometry resulting in high avidity binding by lectins from Aspergillus fumigatus and Burkholderia ambifaria. Replacing the fucose residue with a conformationally constrained fucomimetic does not alter the affinity and provide fine specificity, with no binding to other fucose-specific lectins.
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Dates et versions

hal-02356130 , version 1 (18-01-2021)

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David Goyard, Veronica Baldoneschi, Annabelle Varrot, Michele Fiore, Anne Imberty, et al.. Multivalent Glycomimetics with Affinity and Selectivity toward Fucose-Binding Receptors from Emerging Pathogens. Bioconjugate Chemistry, 2018, 29 (1), pp.83-88. ⟨10.1021/acs.bioconjchem.7b00616⟩. ⟨hal-02356130⟩
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