Molecular level insight into the effect of triethyloctylammonium bromide on the structure, thermal stability, and activity of Bovine serum albumin.

Understanding the interactions between protein and ionic liquids (IL) is vital in order to avail the ILs in biological applications. In this study, we have investigated the influence of triethyloctylammonium bromide on the structure, stability, and activity of Bovine Serum Albumin (BSA) using different spectroscopic methods Fluorescence and circular dichroism measurements revealed that BSA appears to be in a non-native compact structure in the presence of IL (up to concentration 0.02M). But beyond that limit (0.02M), the protein was found to be in an unfolded state. The results are supported by dynamic light scattering (DLS) measurements and also esterase-like activity test proves non-native or unfolded form of protein at a higher concentration of IL. In addition, molecular docking study is carried out to find the possible binding sites of IL with BSA.