A good and bad aggregation: Effect of imidazolium- and cholinium-based ionic liquids on the thermal stability of bovine serum albumin.

• The effect of ILs on BSA was analyzed by spectral and computational methods. • The imidazolium- and cholinium-based ILs promote aggregation of BSA. • The stability of the tertiary structure of BSA is enhanced by the studied ionic liquids. • IL with octyl chain binds to BSA and does not increase its stability. The present work describes the effect of imidazolium- and cholinium-based ionic liquids (ILs) on the thermal stability, binding and aggregation of bovine serum albumin (BSA). The studied ILs include choline chloride [Ch][Cl], choline dihydrogenphosphate [Ch][DHP], choline acetate [Ch][OAc], 1-butyl-3-methylimidazolium tetrafluoroborate [BMIM][BF 4 ], 1-octyl-3-methylimidazolium tetrafluoroborate [OMIM][BF 4 ] 1-butyl-3-methylimidazolium trifluoromethanesulfonate [BMIM][TfO], 1-butyl-3-methylimidazolium acetate [BMIM][OAc], and 1-butyl-3-methylimidazolium methanesulfonate [BMIM][CH 3 SO 3 ]. The state of BSA in presence of ILs was assessed by circular dichroism (CD), temperature dependent circular dichroism, fluorescence spectroscopy, and dynamic light scattering (DLS). The thermal stability of BSA in presence of ILs increased (above 85 °C) in all studied ILs except [OMIM][BF 4 ]. Differences of binding ILs with BSA depending on alkyl chain length were estimated, the probable binding modes were identified using molecular docking. The influence of ILs on the aggregation of BSA at different temperatures was established. It was found that the ILs with short alkyl chain length (up to butyl) promote aggregation of the native form of BSA increasing its thermal stability. [ABSTRACT FROM AUTHOR]