释义：

Isothermal Titration Calorimetry (ITC) is a technique used to directly measure the heat released or absorbed during the interaction between two molecules. By recording these heat changes, ITC can provide thermodynamic parameters of the binding reaction, such as the binding constant (Ka), enthalpy change (ΔH), free energy (ΔG), and entropy change (ΔS).
In the experiment, ITC gradually injects one reactant (such as a ligand) into a reaction vessel containing another reactant (such as a protein) and monitors the heat changes triggered by each injection. These heat changes reflect the degree of molecular binding, with the heat signal gradually decreasing as the unbound molecules in the reaction vessel are consumed, until binding saturation is reached.
The main advantage of ITC is that it does not require labeling or modification of the molecules, allowing the study of molecules in their native state. ITC is widely used in drug development, protein-ligand interaction studies, enzyme activity research, and the exploration of the formation mechanisms of biomolecular complexes. Through ITC, researchers can gain a comprehensive understanding of the interaction mechanisms and thermodynamic properties between molecules, providing key data support for biochemistry and pharmaceutical sciences.

等温滴定量热法 (Isothermal Titration Calorimetry, ITC) 是一种用于直接测量两种分子相互作用过程中释放或吸收热量的技术。通过记录这些热量的变化，ITC 可以提供关于结合反应的热力学参数，如结合常数 (Ka) 、结合焓 (ΔH) 、自由能 (ΔG) 以及熵变 (ΔS)。
在实验中，ITC 通过逐步将一种反应物 (如配体) 注入到含有另一种反应物 (如蛋白质) 的反应池中，监测每次注入引发的热量变化。这些热量反映了分子间的结合程度，随着反应池中未结合分子逐渐减少，热量信号逐渐减弱，直至达到结合饱和。
ITC 的主要优势在于无需标记或修饰分子，能够直接研究分子的天然状态。它广泛应用于药物开发、蛋白质-配体相互作用研究、酶活性研究以及生物分子复合物的形成机制探索中。通过 ITC，研究者可以全面了解分子间的相互作用机制及其热力学特性，为生物化学和药物科学提供关键数据支持。