Analytical Tools for Protein-Carbohydrate Interaction Studies

A wide range of assays has been used to characterize protein-carbohydrates interactions allowing access to various quantitative information including thermodynamic ones such as stoichiometry of binding, binding constant, enthalpy of binding as well as kinetics and mechanistic ones. An understanding of each technique is essential in order to propose and validate appropriate interaction models that rationalize experimental data. Due to the complexity of carbohydrate-lectins interactions as an inherent consequence of multivalent interactions, a careful control of experimental conditions is necessary in order to avoid misinterpretation. This article will briefly present the various techniques that are commonly used to characterize sugar-lectin interaction: inhibition of hemagglutination assay (HIA), enzyme-linked lectin assays (ELLA), isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR). Recently introduced, force spectroscopy by atomic force microscopy (AFM) is a new approach for measuring carbohydrate-protein interaction at the level of a single protein.

Keywords: Biomolecular interaction, biosensors, surface plasmon resonance, isothermal calorimetric titration, atomic force spectroscopy