Zhang Jianzhong, Huang Shaoyan, Han Yongbin, Wang Chenghai, Shao Wei, Fu Zhijian
Shandong Provincial Hospital Affiliated to Shandong University, Jinan, 250021, People's Republic of China.
Yantaishan Hospital, Yantai, 264000, People's Republic of China.
J Biochem Mol Toxicol. 2016 May;30(5):258-64. doi: 10.1002/jbt.21789. Epub 2016 Jan 8.
The interaction of hydroxyethyl starch 130/0.4 (Voluven) with human serum albumin (HSA) has been investigated by fluorescence (steady state and synchronous), Fourier transforms infrared (FT-IR), and circular dichroism (CD) spectroscopies. Analysis of the fluorescence quenching data of HSA by Voluven using the Stern-Volmer method revealed the formation of 1:1 ground-state complex. Evaluation of binding parameters and binding energy indicated that the binding reaction was exothermic. On the basis of fluorescence measurements, it was concluded that electrostatic forces play a crucial role in stabilizing the complex. The binding distance was calculated by using Förster resonance energy transfer (FRET) theory. The conformational changes of HSA were obtained qualitatively as well as quantitatively using synchronous fluorescence, FT-IR, and CD. The HSA underwent partial unfolding in the presence of Voluven.
通过荧光光谱（稳态和同步荧光光谱）、傅里叶变换红外光谱（FT-IR）和圆二色光谱（CD）研究了羟乙基淀粉130/0.4（万汶）与人血清白蛋白（HSA）的相互作用。采用斯特恩-沃尔默方法分析万汶对HSA的荧光猝灭数据，结果表明形成了1:1的基态复合物。结合参数和结合能的评估表明，结合反应是放热的。基于荧光测量，得出静电力在稳定复合物中起关键作用的结论。利用福斯特共振能量转移（FRET）理论计算了结合距离。使用同步荧光光谱、FT-IR和CD对HSA的构象变化进行了定性和定量分析。在万汶存在的情况下，HSA发生了部分去折叠。
