title: Spectroscopic and docking studies on the interaction between pyrrolidinium based ionic liquid and bovine serum albumin.
abstract: The interaction of synthesized ionic liquid, 1-butyl-1-methyl-2-oxopyrrolidinium bromide (BMOP) and bovine serum albumin (BSA) was investigated using UV-Vis, FT-IR, steady state and time resolved fluorescence measurements and docking studies. Steady state spectra revealed that BMOP strongly quenched the intrinsic fluorescence of BSA through dynamic quenching mechanism. The corresponding thermodynamic parameters; Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) showed that the binding process was spontaneous and entropy driven. It is also indicated that hydrophobic forces play a key role in the binding of BMOP to BSA. The synchronous fluorescence spectroscopy reveals that the conformation of BSA changed in the presence of BMOP. The shift in amide I band of FT-IR spectrum of BSA suggested unfolding of the protein secondary structure upon the addition of BMOP. In addition, the molecular modeling study of BSA-BMOP system shows that BMOP binds with BSA at the interface between two sub domains IIA and IIIA, which is located just above the entrance of the binding pocket of IIA through hydrophobic and hydrogen bond interactions in which hydrophobic interaction are dominated.
authors: Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India.
authors: Meena
authors: M
authors: Kumari
authors: Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India.
authors: Jitendra Kumar
authors: JK
authors: Maurya
authors: Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India.
authors: Upendra Kumar
authors: UK
authors: Singh
authors: Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India.
authors: Abbul Bashar
authors: AB
authors: Khan
authors: Department of Chemistry, Jamia Millia Islamia (A Central University), New Delhi, India.
authors: Maroof
authors: M
authors: Ali
authors: Department of Chemistry, A. R. S. D. College, University of Delhi, Delhi, India.
authors: Prashant
authors: P
authors: Singh
authors: Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India. Electronic address: rpatel@jmi.ac.in.
authors: Rajan
authors: R
authors: Patel
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D052578:Ionic Liquids / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011759:Pyrrolidines / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D013997:Time Factors
chemical_list: D052578:Ionic Liquids; D011759:Pyrrolidines; D012710:Serum Albumin, Bovine
keywords: Bovine serum albumin; Fluorescence quenching; Hydrophobic interaction; Ionic liquid; Molecular docking