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Isothermal Titration Calorimetry (ITC) is a label-free biophysical technique that directly measures the heat released or absorbed during molecular binding events by titrating a ligand into its macromolecular target until saturation, thereby preserving native molecular behaviour without the need for labelling or immobilisation. In a single experiment, ITC provides a complete thermodynamic profile encompassing binding affinity (Kd), molar free energy change (ΔG), enthalpy change (ΔH), entropy change (ΔS), and binding stoichiometry (n), enabling differentiation between enthalpy- and entropy-driven interactions. Owing to its quantitative precision, ITC is widely regarded as the gold standard for analysing protein–ligand, protein–protein, and nucleic acid interactions, and it plays a pivotal role in drug discovery by determining binding strength and energetic favourability to support rational drug design and candidate selection. Furthermore, ITC continues to provide essential label-free evaluation in antibody development, formulation studies, and structural biology, making it an indispensable tool as biopharmaceutical molecules grow increasingly complex.