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अमूर्त

Interaction between Pyrrolidinium Based Ionic Liquid and Bovine Serum Albumin: A Spectroscopic and Molecular Docking Insight

Rajan Patel, Meena Kumari, Neeraj Dohare, Abbul Bashar Khan, Prashant Singh, Maqsood Ahmad Malik and Amit Kumar

Herein, we report the interaction of N, N-dimethyl-2-oxopyrrolidinium iodide with bovine serum albumin by using steady-state fluorescence, time-resolved fluorescence, UV-visible and Fourier Transform-Infrared spectroscopy in combination with molecular docking method. The steady state fluorescence spectra results confirmed that N, N-dimethyl- 2-oxopyrrolidinium iodide strongly quenches the intrinsic fluorescence of bovine serum albumin by a dynamic quenching mechanism as confirmed by time resolved fluorescence spectroscopy. The thermodynamic parameters (ΔH, ΔG and ΔS) showed that the binding process was spontaneous and enthalpy driven. Moreover, the interacting forces between bovine serum albumin and N, N-dimethyl-2-oxopyrrolidinium were mainly governed through hydrogen bond and van der Waals forces. The Fourier Transform-Infrared spectroscopy results show the conformational change of bovine serum albumin on binding with N, N-dimethyl-2-oxopyrrolidinium. Additionally, molecular modeling results revealed that N, N-dimethyl-2-oxopyrrolidinium binds with the amino acid residues of the sub domain IIA of bovine serum albumin.