Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Unit 1000, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Biochem Soc Trans. 2010 Aug;38(4):888-93. doi: 10.1042/BST0380888.
The binding of two biomolecules viewed from the atomic level is highly complex. It involves the formation or removal of many individual non-covalent bonds both between the interacting molecules as well as with solvent. Currently, our understanding of the thermodynamic quantification of biomolecular interactions is somewhat naïve. ITC (isothermal titration calorimetry) provides a rapid route to a full thermodynamic characterization of a biomolecular interaction. Armed with these data, what are we really able to understand about complex formation and can any of this information provide a useful tool to aid drug development? Correlations between thermodynamic data and structural detail have been investigated, allowing insight into ways in which these can be used to understand protein-ligand interactions and provide input into the decision-making process in drug development.
从原子水平上看，两种生物分子的结合非常复杂。它涉及到许多单个非共价键的形成或断裂，这些键不仅存在于相互作用的分子之间，也存在于溶剂中。目前，我们对生物分子相互作用的热力学量化的理解有些幼稚。ITC（等温滴定量热法）为全面热力学表征生物分子相互作用提供了快速途径。有了这些数据，我们真正能够理解复杂形成的是什么，并且这些信息中的任何一个都可以提供一个有用的工具来帮助药物开发？已经研究了热力学数据与结构细节之间的相关性，从而深入了解如何利用这些数据来理解蛋白质-配体相互作用，并为药物开发的决策过程提供信息。
