Isothermal titration calorimetry (ITC) allows direct, label-free in solution measurement of binding affinity and thermodynamics in a single experiment, enabling the accurate determination of binding constants (KD), reaction stoichiometry (n), enthalpy (∆H) and entropy (∆S). ITC measures the binding affinity and thermodynamics of biomolecular interactions, helping to understand why interactions occur. The technique is based on the measurement of heat evolved or absorbed when complexes are formed between molecules. It has the advantage of measuring all binding parameters in a single label-free, in-solution experiment. ITC reveals fundamental thermodynamic data, the forces that drive complex formation, enabling function and mechanism to be described at a molecular level. Isothermal titration microcalorimeters measure the heat change that occurs when molecules interact. Heat is released or absorbed as a result of the redistribution and formation of non-covalent bonds when the interacting molecules go from the free to the bound state. ITC can provide thermodynamic data of the interaction of nanomaterials with biomolecules, and on the formation and stability of protein corona