Imaging Science and Photochemistry ›› 2015, Vol. 33 ›› Issue (1): 84-97.DOI: 10.7517/j.issn.1674-0475.2015.01.084

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Binding Characteristic of Imidazolium Ionic Liquid with Bovine Serum Albumin

DING Yuanhua, CUI Jian, DAI Tuosu, GUO Rong   

  1. School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, Jiangsu, P. R. China
  • Received:2014-11-05 Revised:2014-12-10 Online:2015-01-15 Published:2015-01-15

Abstract:

In the present work, UV-Vis spectroscopy, fluorescence spectroscopy, synchronous fluorescence spectroscopy, circular dichroism spectroscopy(CD), attenuated total refraction-fourier transform infrared spectroscopy(ATR-FTIR), negative staining-transmission electron microscopy, light scattering and isothermal titration calorimetry (ITC) were used to study the binding characteristics between bovine serum albumin and a typical imidazolium ionic liquid(IL), 1-butyl-3-methylimidazolium chloride ([Bmim]Cl). The results showed that the addition of [Bmim]Cl would make the UV absorption intensity of BSA increased and also lead to static fluorescence quenching. Synchronous fluorescence results suggested that [Bmim]Cl molecules mainly interact with the region which is close to the tryptophan residues of BSA, so that made the conformation and internal hydrophobic structure changed. Negative staining-transmission electron microscopy directly showed that the change of protein-IL complex structure after adding the ionic liquid. From circular dichroism and ATR-FTIR results, it was found that ionic liquid also produced a much stronger impact to α-helix, β-fold of BSA, which led to changes in protein secondary structure. Finally, ITC and surface tension methods indicated that the above interaction were driven by the electrostatic interaction and hydrophobic interaction, however, the hydrophobic interaction between the alkyl chain of IL and the internal hydrophobic microstructure of BSA was the main driving force.

Key words: ionic liquid, protein, binding characteristic, interaction mechanism