等温滴定量热法在蛋白质-配体相互作用中的应用

Applications of Isothermal Titration Calorimetry in Protein-ligand Interactions

等温滴定量热法(ITC)近年来迅速发展并广泛应用于分子生物学及其相关领域的研究分子相互作用的生物物理技术,它是在恒定温度下唯一能够直接测量复合物形成过程中的热量变化的方法。它可以简单地通过测量两个溶液相互作用时吸收或放出的热量来提供分子相互作用的重要信息,如结合常数、结合位点数、自由能、焓和熵。综述了ITC的工作原理、技术特点,以及在蛋白质-配体相互作用方面的最新应用和未来的发展方向,表明ITC数据结果的有效性及其在该领域的应用价值。

Isothermal titration calorimetry （ ITC ） is a biophysical technique widely used to study molecular interactions in molecular biology and these related fields, it is the sole direct method to measure the heat change during complex formation at constant temperature. We may obtain much important information about molecular interactions （ such as binding constant, number of binding sites, free energy, enthalpy, and entropy ） simply by measuring the heat absorbed or released during an interaction between two liquid solutions. This review concentrates on the principle and featdres of ITC, the new applications of ITC in protein-ligand interactions, and potential development direction, it has been shown that it plays an important role in the elucidation of binding mechanisms and the validity of the data.