Institute of Environmental Toxicology and Environmental Ecology, Yancheng Teachers University, Yancheng City, Jiangsu Province 224051, People's Republic of China.
Institute of Environmental Toxicology and Environmental Ecology, Yancheng Teachers University, Yancheng City, Jiangsu Province 224051, People's Republic of China; Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng Teachers University, Yancheng City, Jiangsu Province 224051, People's Republic of China.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 May 5;196:323-333. doi: 10.1016/j.saa.2018.02.040. Epub 2018 Feb 14.
The effects of six imidazolium-based ionic liquids (ILs) with different alkyl chain length ([CMim]Cl, n=2, 4, 6, 8, 10, 12) on the structure and functions of bovine serum albumin (BSA) were studied by multi-spectral methods and molecular docking. ILs with the longer alkyl chain length have the stronger binding interaction with BSA and the greater conformational damage to protein. The effects of ILs on the functional properties of BSA were further studied by the determination of non-enzyme esterase activity, β-fibrosis and other properties of BSA. The thermal stability of BSA was reduced, the rate of the formation of beta sheet structures of BSA was lowered, and the esterase-like activity of BSA were decreased with the increase of ILs concentration. Simultaneous molecular modeling technique revealed the favorable binding sites of ILs on protein. The hydrophobic force and polar interactions were the mainly binding forces of them. The calculated results are in a good agreement with the spectroscopic experiments. These studies on the impact of the alkyl chain length on binding of imidazolium-based ionic liquids to BSA are of great significance for understanding and developing the application of ionic liquid in life and physiological system.
六种不同烷基链长的咪唑类离子液体（[CMim]Cl，n=2,4,6,8,10,12）对牛血清白蛋白（BSA）结构和功能的影响，通过多光谱方法和分子对接进行了研究。具有较长烷基链长的离子液体与 BSA 的结合相互作用更强，对蛋白质的构象损伤更大。通过测定非酶酯酶活性、β-纤维化等 BSA 性质，进一步研究了 ILs 对 BSA 功能性质的影响。BSA 的热稳定性降低，BSA 中β-折叠结构的形成速度降低，BSA 的酯酶样活性随着 ILs 浓度的增加而降低。同时分子建模技术揭示了 ILs 在蛋白质上的有利结合位点。疏水力和极性相互作用是它们的主要结合力。计算结果与光谱实验吻合较好。这些关于烷基链长对咪唑类离子液体与 BSA 结合影响的研究，对于理解和开发离子液体在生命和生理系统中的应用具有重要意义。
