人绒毛膜促性腺激素（hCG）与单克隆抗体相互作用的热力学：对使用放射性标记hCG探针获得的实时动力学数据的分析

Thermodynamics of hCG--monoclonal antibody interaction: an analysis of real time kinetics data obtained using radiolabeled hCG probe.

作者信息

Ashish Banerjee, Tamil Selvi P, Murthy Gundlupet Satyanarayana

机构信息

Primate Research Laboratory, Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, India.

出版信息

Biochim Biophys Acta. 2002 Aug 15;1572(1):31-6. doi: 10.1016/s0304-4165(02)00274-x.

DOI:10.1016/s0304-4165(02)00274-x

PMID:12204330

Abstract

A thermodynamic analysis of the interaction of 125I-labeled human chorionic gonadotropin (IhCG) with two of its monoclonal antibodies (MAbs) was carried out. The dissociation profile of IhCG-MAb complex conforms to a two-step model. vant Hoff enthalpies were calculated with the K(A) (equilibrium constant) values obtained from dissociation at different temperatures. Free energy and entropy changes were calculated using the standard equations. DeltaH values for one of the MAbs, viz. VM7 were favorable at temperatures beyond 30 degrees C. Interestingly, the DeltaS values were also favorable at all temperatures. In the case of MAb VM4a, however, the interaction throughout the temperature range was driven by large favorable entropic contributions, indicating the importance of hydrophobic interaction in the binding of this MAb to hCG. The energetics of the interaction of these two monoclonals with hCG is discussed.

摘要

对125I标记的人绒毛膜促性腺激素（IhCG）与其两种单克隆抗体（MAb）之间的相互作用进行了热力学分析。IhCG-MAb复合物的解离曲线符合两步模型。利用在不同温度下解离得到的K(A)（平衡常数）值计算范特霍夫焓。使用标准方程计算自由能和熵变。其中一种单克隆抗体VM7的ΔH值在30摄氏度以上的温度下是有利的。有趣的是，ΔS值在所有温度下也都是有利的。然而，对于单克隆抗体VM4a，整个温度范围内的相互作用是由大量有利的熵贡献驱动的，这表明疏水相互作用在该单克隆抗体与hCG结合中的重要性。讨论了这两种单克隆抗体与hCG相互作用的能量学。