Isothermal Titration Calorimetry (ITC)

Isothermal Titration Calorimetry (ITC) is a biophysical technique used to directly measure molecular interactions by detecting heat changes during binding events. It provides complete thermodynamic profiles including binding affinity, enthalpy, entropy, and stoichiometry in a single experiment. Unlike indirect methods, ITC does not require labelling or immobilisation, preserving native molecular behaviour.

ITC is widely used to study protein-ligand, protein-protein, and nucleic acid interactions. In drug discovery, ITC determines how strongly a lead compound binds to its target protein and whether the interaction is energetically favourable, supporting rational drug design and candidate selection. ITC also supports antibody development, formulation studies, and structural biology. Its quantitative precision makes it a gold standard in molecular interaction analysis. As biopharmaceutical molecules become more complex, ITC continues providing essential label-free evaluation of molecular binding.