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Investigation of binding interactions between BSA and [EPMpyr][Sal] through spectroscopy studies, thermophysical and thermodynamic properties.

The intensity of research, probing the interactions between proteins and ionic liquid (IL), has been increasing and parallels the fast-growing applications of ILs in biotechnology. The specific aspects which have attracted the involvement of researchers are stabilization, separation, biochemical and enzymatic reactions of proteins. In this work the synthesis of IL, epoxypropyl and N-methyl substituted 2‑oxopyrrolidinium cation with salicylate anion, [EPMpyr][Sal], and its interaction with aqueous BSA{BSA(aq) -[EPMpyr][Sal]}. Measurements of thermophysical properties (density (ρ), and speed of sound (u)) showed that both moderately strong and weak interactions occur on treatment of BSA with that chosen IL. H-bond formation, dipole-dipole interactions and ionic interactions occurring in this system were investigated via thermophysical and thermodynamic properties as well as spectroscopic data. Thermodynamic data (excess molar volume (Vm E ), isentropic compressibility (ks ), deviation in isentropic compressibility (∆ks ) and intermolecular free length (Lf )) showed that there were stronger interaction between IL and BSA at higher temperature. The data from all the studies were correlated with Redlich Kister polynomial equation. The blue shift observed in the fluorescent spectra was interpreted to indicate that thetryptophan (Trp) residue of BSA moves to a more hydrophobic environment. It was also observed that the addition of more IL to BSA resulted in denaturation of BSA due to high hydrophobic nature of IL. Circular dichroism studies show that there were significant changes in the fine structure of BSA on interaction with IL. From the FTIR spectra the position of H-bond in the secondary structure of BSA was deduced.

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