Ma Jun-yan, Chen Ke-hai, Zheng Xue-fang, Guo Ming, Ma Jing, Tang Qian, Wang Yu-lian, Hu Jie-han
College of Bioengineering, Dalian University, Dalian 116622, China.
Guang Pu Xue Yu Guang Pu Fen Xi. 2007 Dec;27(12):2485-9.
The binding reaction of colchicine with human serum albumin (HSA) was studied by UV-Vis absorption, fluorescence and circular dichroism spectrometry. The results indicated that colchicine led to the increase in UV absorption and the quenching of intrinsic fluorescence of HSA. As the temperature increased, the quenching constant Ksv decreased. The binding constants and the numbers of the binding sites of the interaction between colchicine and HSA at different temperatures were obtained. The thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS), were calculated to be -11.66 kJ x mol(-1) and 51.507 J(mol x K)(-1) respectively according to Van't Hoff equation, which suggested that the main binding force between colchicine and HSA was static interaction. The protein conformation was altered (CD date) with decreasing of alpha-helices in the presence of colchicine. The results showed that the quenching mechanism of the combination of colchicine with human serum albumin was a static quenching procedure.
采用紫外可见吸收光谱、荧光光谱和圆二色光谱研究了秋水仙碱与人血清白蛋白（HSA）的结合反应。结果表明，秋水仙碱导致HSA的紫外吸收增加和内源荧光猝灭。随着温度升高，猝灭常数Ksv降低。获得了不同温度下秋水仙碱与HSA相互作用的结合常数和结合位点数目。根据范特霍夫方程计算得到热力学参数焓变（ΔH）和熵变（ΔS）分别为-11.66 kJ·mol⁻¹和51.507 J/(mol·K)，这表明秋水仙碱与HSA之间的主要结合力是静电相互作用。在秋水仙碱存在下，蛋白质构象发生改变（圆二色数据），α-螺旋减少。结果表明，秋水仙碱与人血清白蛋白结合的猝灭机制为静态猝灭过程。
