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While monovalent sugar/lectin interactions are typically in the millimolar range, higher affinity can be achieved between multivalent ligands and lectins through complex binding mechanisms. Isothermal titration calorimetry (ITC) is generally the physicochemical technique of choice in this field. However, the formation of aggregates often observed with multivalent ligands, synthetized by our colleague of "Multiglyco" group (more info), may lead to uninterpretable data, thus precluding access to key binding parameters. Complementary technics as Surface Plasmon Resonance (SPR) (Org. Biomol. Chem. 2008) or Bio-Layer Interferometry (BLI) (Org. Biomol. Chem. 2018) were used.
 
Recent collaboration:
A. Imberty (CERMAV)