Singh Sreelekha K, Kishore Nand
Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.
J Pharm Sci. 2008 Jun;97(6):2362-72. doi: 10.1002/jps.21140.
The potential binding interaction(s) of the anti-thyroid drug methimazole (MMZ) with the protein bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC) and UV-Visible, fluorescence and circular dichroism (CD) spectroscopic techniques. The binding of MMZ to BSA has been studied in both the presence and absence of added surfactants. Since, the ITC thermograms show the molar enthalpy of binding of MMZ and BSA to be zero within experimental error, either the enthalpy change of the binding interaction is zero or there is no binding occurring. The CD and the intrinsic fluorescence and life time spectra of BSA were unchanged by the addition of MMZ. This is also indicative of the absence of any significant interaction of MMZ with BSA.
利用等温滴定量热法（ITC）以及紫外可见、荧光和圆二色性（CD）光谱技术，研究了抗甲状腺药物甲巯咪唑（MMZ）与蛋白质牛血清白蛋白（BSA）之间潜在的结合相互作用。在添加和不添加表面活性剂的情况下，均对MMZ与BSA的结合进行了研究。由于ITC热谱图显示，在实验误差范围内，MMZ与BSA结合的摩尔焓为零，因此结合相互作用的焓变要么为零，要么不存在结合。添加MMZ后，BSA的CD光谱、固有荧光光谱和寿命光谱均未发生变化。这也表明MMZ与BSA之间不存在任何显著的相互作用。
