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Effects of Ionic Liquids on Aqueous Urea Solutions: Insights into the Ionic Liquid-Assisted Protein Renaturation

Cite this: J. Phys. Chem. B 2021, 125, 18, 4808–4818
Publication Date (Web):April 29, 2021
https://doi.org/10.1021/acs.jpcb.1c00586
Copyright © 2021 American Chemical Society

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    Abstract

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    Ionic liquids (ILs) are designer solvents that find wide applications in various areas. Recently, ILs have been shown to induce the refolding of certain proteins that were previously denatured under the treatment of urea. A molecular-level understanding of the counteracting mechanism of ILs on urea-induced protein denaturation remains elusive. In this study, we employ atomistic molecular dynamics simulations to investigate the ternary urea–water–IL solution in comparison to the aqueous urea solution to understand how the presence of ILs can modulate the structure, energetics, and dynamics of urea–water solutions. Our results show that the ions of the IL used, ethylammonium nitrate (EAN), interact strongly with urea and disrupt the urea aggregates that were known to stabilize the unfolded state of the proteins. Results also suggest a disruption in urea–water interaction that releases more free water molecules in solution. We subsequently strengthened these findings by simulating a model peptide in the absence and presence of EAN, which showed broken versus intact secondary structure in urea solution. Analyses show that these changes were accomplished by the added IL, which enforced a gradual displacement of urea from the peptide surface by water. We propose that the ILs facilitate protein renaturation by breaking down the urea aggregates and increasing the amount of free water molecules around the protein.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.jpcb.1c00586.

    • (Figure S1) Urea–urea rdfs with increasing EAN concentration; (Figure S2) distributions of IL ions around urea; (Figure S3) urea–urea center-of-mass rdfs for increasing EAN concentration; (Figure S4) distributions of water around the IL ions with increasing EAN concentration; (Figure S5) time-averaged secondary structures of the S-peptide; (Figure S6) time evolution of peptide–urea interaction energy; (Table S1) urea–urea, water–water, water–anion, and water–cation coordination numbers; (Table S2) water–water hydrogen bond time correlation function; (Table S3) percentage helicity of the S-peptide; (Table S4) average interaction energies between the S-peptide and other different components in the solution (PDF)

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    Cited By

    This article is cited by 4 publications.

    1. Krishna Prasad Ghanta, Sanjoy Bandyopadhyay. Counteraction Effects of Ammonium-Based Ionic Liquids on Urea-Induced Denaturation of α-Lactalbumin: A Comprehensive Molecular Simulation Study. The Journal of Physical Chemistry B 2023, 127 (33) , 7251-7265. https://doi.org/10.1021/acs.jpcb.3c03223
    2. Michael Feig. Virtual Issue on Protein Crowding and Stability. The Journal of Physical Chemistry B 2021, 125 (38) , 10649-10651. https://doi.org/10.1021/acs.jpcb.1c07093
    3. Beñat Olave. DNA nanotechnology in ionic liquids and deep eutectic solvents. Critical Reviews in Biotechnology 2023, 12 , 1-21. https://doi.org/10.1080/07388551.2023.2229950
    4. Zeyu Zhang, Guiquan Jiang, Jiuyin Pang, Ling Su. Synthesis of renewable soybean protein and acrylate copolymers via ATRP in ionic liquid. Industrial Crops and Products 2022, 180 , 114720. https://doi.org/10.1016/j.indcrop.2022.114720

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