Molecular interaction on imidazolium based ionic liquids and serum albumin: A spectroscopy approach

Manoj Kumar Banjare,Ramesh Kumar Banjare,Kallol Kumar Ghosh

doi:10.14419/ijac.v8i2.30994

Abstract

Interaction between globular proteins with imidazolium based ionic liquids (ILs) is extremely significant considering that of the vast use of ILs, since protein stabilizer in the current years. The present work, the interaction of human serum albumin (HSA) and bovine serum albumin (BSA) with 1-butyl-3-methylimidazolium octylsulphate (BmimOS) and 1-decyl-3-methylimidazolium tetrafluoroborate (DmimBF4) have been examine the use of fluorescence and FTIR. Fluorescence spectra of HSA/BSA are extinguished by BmimOS /DmimBF4 ILs by way of the dynamic method. The various thermodynamic parameters were revealing that very susceptible interactions exist between HSA/BSA and BmimOS /DmimBF4. The conformational adjustments of HSA/BSA were observed by means of FTIR analysis. Fluorescence methods were completed to find out about the thermal balance of HSA/BSA at different temperature. The thermal balance of BSA in the presence of ILs follows the style BmimOS/DmimBF4 and presence of extra hydrophobic IL, decay increases swiftly as a characteristic of concentration.Â Â

Highlights

Effect of proteins on the ionic liquids (ILs) provides important information about interactions between them which can change the secondary or tertiary structure of protein or denature them, thereby modifying the function of the molecule (Venkatesu et al 2012, Venkatesu et al 2014, Weingartner et al 2012, Zhao et al 2005)
The present investigated the molecular interaction between ionic liquids i.e., 1-butyl-3-methyl imidazolium octyl sulfate (BmimOS) and 1-decyl-3-methylimidazolium tetrafluoroborate (DmimBF4) and serum albumins i.e., human serum albumin (HSA), bovine serum albumin (BSA) by fluorescence and FTIR spectroscopy
Spectroscopic revealed that 1-butyl-3-methylimidazolium octylsulphate (BmimOS) and 1-decyl-3-methylimidazolium tetrafluoroborate (DmimBF4) interact with HSA/BSA in the bulk earlier to interaction

Summary

Introduction

Effect of proteins on the ionic liquids (ILs) provides important information about interactions between them which can change the secondary or tertiary structure of protein or denature them, thereby modifying the function of the molecule (Venkatesu et al 2012, Venkatesu et al 2014, Weingartner et al 2012, Zhao et al 2005). The present study is contributed to improve considerate of function of the molecular structure of ILs in protein-ILs interactions and as a result, in the behaviour of ionic ILs since denaturants (Schroder et al 2016, Sairi et al 2014, Roy et al 2016). Patel et al 2016, studied the interaction among N, N-dimethyl-2oxopyrrolidinium iodide and BSA by fluorescence, UV-vis and FTIR in mixture among molecular docking method. The present investigated the molecular interaction between ionic liquids i.e., 1-butyl-3-methyl imidazolium octyl sulfate (BmimOS) and 1-decyl-3-methylimidazolium tetrafluoroborate (DmimBF4) and serum albumins i.e., human serum albumin (HSA), bovine serum albumin (BSA) by fluorescence and FTIR spectroscopy. Scheme 1: Molecular Structure of Ionic Liquid 1-Butyl-3-Methylimidazolium Octylsulphate and 1-Decyl-3methylimidazolium Tetrafluoroborate

Fluorescence spectrometry

FT-IR spectrometry

Results and discussion

Calculate the binding constant and binding number

Binding interaction between ionic liquids and serum albumins

Conclusion