Department of Chemistry and Biochemistry, Graduate School of Engineering, Centre for Molecular Systems (CMS), Kyushu University, 744-Moto-oka, Fukuoka-819-0395, Japan.
J Phys Chem B. 2012 Oct 4;116(39):11924-35. doi: 10.1021/jp303609h. Epub 2012 Sep 20.
Structural changes of a globular protein, bovine serum albumin (BSA), as a consequence of interaction with the surface active ionic liquids (ILs)-3-methyl-1-octylimidazolium chloride, [C(8)mim][Cl], and 1-butyl-3-methylimidazolium octylsulfate, [C(4)mim][C(8)OSO(3)]-have been investigated using various physicochemical and spectroscopic techniques such as tensiometry, conductometry, steady-state fluorescence, far-UV circular dichroism spectroscopy (CD), and dynamic light scattering (DLS). The interactional behavior of ILs (monomers and self-assembled structures) toward BSA in different IL concentration regimes at the air/solution interface as well as in the bulk is investigated and discussed depending upon the nature of ions of ILs. CD combined with the steady state fluorescence spectroscopy provided valuable insights into the unfolding of BSA as a consequence of IL binding. The complementary results obtained from the multitechnique approach proved very useful in drawing out the mechanism of interaction between ILs and BSA in different IL concentration regimes.
采用表面张力法、动态光散射（DLS）、电导法、稳态荧光法、远紫外圆二色光谱（CD）等多种物理化学和光谱技术，研究了球形蛋白质牛血清白蛋白（BSA）与表面活性离子液体（ILs）-3-甲基-1-辛基咪唑氯化物[C（8）mim][Cl]和 1-丁基-3-甲基咪唑辛基硫酸盐[C（4）mim][C（8）OSO（3）]相互作用引起的结构变化。根据 IL 离子的性质，研究并讨论了 IL（单体和自组装结构）在不同 IL 浓度区在空气/溶液界面以及在本体中与 BSA 的相互作用行为。圆二色光谱（CD）与稳态荧光光谱相结合，为 IL 结合引起的 BSA 展开提供了有价值的见解。从多技术方法获得的补充结果非常有助于得出不同 IL 浓度区 IL 和 BSA 之间相互作用的机制。
