具有表面活性的离子液体与牛血清白蛋白相互作用的研究

he interactions between a surface active imidazolium ionic liquid (IL), 1-tetradecyl-3-methylimidazolium bromide (C14mimBr) and bovine serum albumin (BSA) were investigated by surface tension, isothermal titration microcalorimetry, far-UV circular dichroism (CD) and fluorescence spectra. The surface tension measurement shows the formation of C14mimBr/BSA complex and the effect of the complex on surface tension. The enthalpy change in the whole interaction process between C14mimBr and BSA was obtained by isothermal titration microcalorimetry, and the results show alteration of the BSA structure. The contents of α-helix and random coil were obtained by far-UV CD. Changes of these contents reveal that the secondary structure of BSA changes with addition of C14mimBr. Fluorescence spectra show that tryptophan (Trp) residues, one of the intrinsic fluorophores in BSA, are exposed to a hydrophobic microenvironment with the addition of C14mimBr.