Interaction between Pyrrolidinium Based Ionic Liquid and Bovine Serum Albumin: A Spectroscopic and Molecular Docking Insight
- Corresponding Author:
- Rajan Patel
Biophysical Chemistry Laboratory
Centre for Interdisciplinary Research in Basic Sciences
Jamia Millia Islamia (A Central University), New Delhi, India
E-mail: [email protected]
Received date: February 08, 2016; Accepted date: April 18, 2016; Published date: April 21, 2016
Citation: Patel R, Kumari M, Dohare N, Khan AB, Singh P, et al. (2016) Interaction between Pyrrolidinium Based Ionic Liquid and Bovine Serum Albumin: A Spectroscopic and Molecular Docking Insight. Biochem Anal Biochem 5:265. doi:10.4172/2161- 1009.1000265
Copyright: © 2016 Patel R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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.