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

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][BF4], 1-octyl-3-methylimidazolium tetrafluoroborate [OMIM][BF4] 1-butyl-3-methylimidazolium trifluoromethanesulfonate [BMIM][TfO], 1-butyl-3-methylimidazolium acetate [BMIM][OAc], and 1-butyl-3-methylimidazolium methanesulfonate [BMIM] [CH3SO3]. The state of BSA in presence of ILs was assessed by circular dichroism (CD), temperature depen-dent circular dichroism, fluorescence spectroscopy, and dynamic light scattering (DLS). The thermal sta-bility of BSA in presence of ILs increased (above 85 & DEG;C) in all studied ILs except [OMIM][BF4]. 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 tem-peratures 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.& COPY; 2023 Elsevier B.V. All rights reserved.

Automated summary

This work investigates the impact of imidazolium- and cholinium-based ionic liquids (ILs) on the thermal stability, binding, and aggregation of bovine serum albumin (BSA). The study evaluates various ILs including choline chloride [Ch][Cl], choline dihydrogenphosphate [Ch][DHP], and others. The presence of ILs enhances the thermal stability of BSA except for [OMIM][BF4]. Molecular docking is used to identify the probable binding modes of ILs with BSA. The findings suggest that ILs with short alkyl chain length promote the aggregation and thermal stability of BSA.