In addition, the reorganization of water molecules surrounding the ligands as well as the ligand-binding cavities has been proposed to mediate the enthalpy entropy compensation effect in the overall binding processes.
As a technique that directly measures the heat released or absorbed during a biomolecular binding event, isothermal titration calorimetry (ITC) can simultaneously determine several binding parameters (binding stoichiometry, binding constant, binding enthalpy, and entropy) in one experiment and has been used to study arsenic protein binding.
Aside from equilibrium binding, the enthalpy entropy compensation has been reported in various kinetic processes, including the transient kinetics for the binding of SAHA and TSA to HDAC8 reported previously from our laboratory.
The enthalpy of hydration of No2+ has been calculated as 1486 kJ·mol−1.
Likewise, the therapeutic efficacy of the HMG CoA inhibitors (statins) has been positively correlated with their enthalpies of binding to the enzyme.
The enthalpy entropy compensation effect has been widely observed in the binding of structurally similar ligands to their common target, and this feature is known to hinder the affinity optimization of lead molecules toward finding a tight-binding drug molecule.
In protein chemistry, the enthalpy entropy compensation effect has been frequently observed in the temperature-dependent binding of ligands to their cognate proteins.
The physical origin of enthalpy entropy compensation has been a matter of significant controversy.
In recent years, the molecular explanation for the origin of enthalpy entropy compensation effect has been revised.
The binding free energies have been determined from biosensor surface plasmon resonance (SPR), while binding enthalpies and heat capacities are from isothermal calorimetric titration (ITC).
