ABSTRACT
The thermodynamics and kinetics of binding of glycans and glycoproteins to Ganoderma lucidum lectin was studied using surface plasmon resonance. The lectin showed highest affinity for asialo triantennary N glycan (Ka = 3.52 x 10(5)) among the glycans tested. There was a several fold increase in affinity for glycoproteins compared to their corresponding glycans and coincident increase in contribution from enthalpy (DeltaH), suggesting the involvement of hydrogen bonding in the interaction as well as involvement of protein-protein interactions. Increased affinity also showed increase in unfavorable negative binding entropy (DeltaS) which was compensated with higher enthalpy. The glycoproteins showed faster association rates (k(1)) and the activation energy (E(1)) in the association process was much lower for the glycoproteins than glycans, resulting in their faster associations. These observations elaborate the role of protein matrix in lectin-glycoconjugate interaction.
