异嗪皮啶与人血清白蛋白的相互作用。
Interaction of isofraxidin with human serum albumin.
作者信息
Liu Jiaqin, Tian Jianniao, Tian Xuan, Hu Zhide, Chen Xingguo
机构信息
Department of Chemistry, Lanzhou University, Lanzhou 730000, China.
出版信息
Bioorg Med Chem. 2004 Jan 15;12(2):469-74. doi: 10.1016/j.bmc.2003.10.030.
This study was designed to examine the interaction of isofraxidin with human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 3.3 x 10(-6) mol L(-1)-3.0x10(-5) mol L(-1) and HSA concentration at 1.5 x 10(-6) mol L(-1). Fluorescence quenching methods in combination with Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy were used to determine the drug-binding mode, the binding constant and the protein structure changes in the presence of isofraxidin in aqueous solution. Spectroscopic evidence showed that the interaction results in one type of isofraxidin-HSA complex with binding constants of 4.1266 x 10(5) L mol(-1), 3.8612 x 10(5) L mol(-1), 3.5063 x 10(5) L mol(-1), 3.1241 x 10(5) L mol(-1) at 296 K, 303 K, 310 K, 318 K, respectively. The thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be -10.08 kJ mol(-1) and 73.57 J mol(-1) K(-1) according to van't Hoff equation, which indicated that hydrophobic interaction played a main role in the binding of isofraxidin to HSA. The experiment results are nearly in accordance with the calculation results obtained by Silicon Graphics Ocatane2 workstation.
本研究旨在考察在生理条件下，异秦皮啶与人类血清白蛋白（HSA）在药物浓度范围为3.3×10⁻⁶ mol L⁻¹ - 3.0×10⁻⁵ mol L⁻¹且HSA浓度为1.5×10⁻⁶ mol L⁻¹时的相互作用。采用荧光猝灭法结合傅里叶变换红外（FT - IR）光谱和圆二色（CD）光谱来确定药物结合模式、结合常数以及在水溶液中存在异秦皮啶时蛋白质结构的变化。光谱证据表明，这种相互作用产生了一种异秦皮啶 - HSA复合物，在296 K、303 K、310 K、318 K时的结合常数分别为4.1266×10⁵ L mol⁻¹、3.8612×10⁵ L mol⁻¹、3.5063×10⁵ L mol⁻¹、3.1241×10⁵ L mol⁻¹。根据范特霍夫方程计算得到的热力学参数，焓变（ΔH）和熵变（ΔS）分别为 - 10.08 kJ mol⁻¹和73.57 J mol⁻¹ K⁻¹，这表明疏水相互作用在异秦皮啶与HSA的结合中起主要作用。实验结果与Silicon Graphics Ocatane2工作站获得的计算结果几乎一致。
Zotero 插件