Impact of Ammonium Based Ionic Liquids on the Conformation of Bovine serum albumin (BSA)

In this study, impact of different ammonium based ionic liquids on the structure of Bovine serum albumin (BSA) was investigated by different spectroscopic methods like, UV-vis, fluorescence and CD spectroscopy. Fluorescence results reveal that the ILs has no significant impact on the environment of tryptophan residues. From the Far-UV CD results, it was observed that these ILs increase the α-helicity of the protein, BSA. Near-UV CD study confirms the fluorescence results whereas it shows the alteration of tertiary structure of BSA especially around disulphide bonds