Protein Stability and Conformation: Impact of Ammonium based Ionic Liquids

Abstract

In view of wide scope of Ionic liquids (IL) in biochemical applications, it is essential to investigate the effect of ILs on the structure and stability of biomolecules. In this study, the thermal stability of Bovine serum albumin (BSA) has been explored in aqueous IL (triethyloctyl ammonium bromide) medium. The thermal aggregation behavior of BSA was analyzed by UV-Vis spectroscopy, Dynamic light scattering and Scanning electron microscopy techniques. Circular dichroism measurements provide the conformational changes as well as the thermal unfolding/refolding of BSA.Our results show the thermal stability/aggregation is influenced by the IL in a concentration dependent manner, which indicates the concentration of IL is very crucial in the stabilization/destablization of proteins. Here, we have observed that a high concentration of IL not only prevents the thermal aggregation but also refolds the thermally denatured BSA. Moreover, the molecular docking studies revealed the possible binding site of IL on BSA.