Dual mechanism of ionic liquid-induced protein unfolding

Singh, Onkar; Lee, Pei-Yin; Matysiak, Silvina; Bermudez, Harry

doi:10.1039/d0cp03138k

Cited by 20 publications

(19 citation statements)

References 52 publications

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“…Several studies revealed the contribution of both IL cation and anion in the thermal destabilization of proteins (Figueiredo et al 2013;Bui-Le et al 2020;Hebal et al 2020;Singh et al 2020). This destabilization is a result of the direct interaction of ions to the protein, but regarding protein stability, there is a dominating effect of anion over cation (Figueiredo et al 2013;Okur et al 2013;Bui-Le et al 2020).…”

Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

“…In a study of the thermal destabilization of lysozyme in the presence of two imidazolium-based ILs, [EMIM]EtSO 4 and [EMIM]Et 2 PO 4 , Singh et al (2020) observed that in both IL systems, positive protein residues attract anion and negative protein residues attract cation. In addition, some hydrophobic residues on the protein surface also attract hydrophobic parts of both cation and anion.…”

Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

“…The anion Et2PO4 -, with lower charge delocalization and greater hydrophobicity, has a greater driving force for interactions with both the protein surface charges and the hydrophobic interior, exerting therefore a stronger destabilizing effect than EtSO4anion. The [EMIM] þ cation exerts its effect locally by binding to a tryptophan side chain via favorable p-p and cation-p interactions and such bindings likely compete with the interaction of this tryptophan to two nearby arginines thus disturbing an Arg-Trp-Arg bridge in the protein that is critical to lysozyme stability (Singh et al 2020). Bui-Le et al (2020) observed interaction of both cation and anion of ILs with a green fluorescent protein via electrostatic, hydrophobic and aromatic interactions.…”

Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

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Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hebal

Boucherba

Bi̇nay

et al. 2021

Biocatalysis and Biotransformation

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The biochemical conversion route in the utilization of biomass has required intensive development of processing methods for reducing recalcitrance of cellulose to enzymatic hydrolysis. Since discovering hydrophilic ionic liquids (ILs) are efficient lignocellulose solvents, considerable efforts have been made to demonstrate their potential applications in cellulose hydrolysis. However, most of the commercial lignocellulose hydrolyzing enzymes are largely deactivated or inhibited in the presence of even low concentrations of ILs. The link found between enzyme thermostability and IL tolerance leads to the consideration that hyperthermostable enzymes are good candidates to be used together with ILs. Hyperthermostable cellulases and xylanases that are highly tolerant to aqueous solutions of ILs show resistance to competitive inhibition by IL cations and have lower amounts of structural motifs (loop and helix structures) that are prone to denaturation by IL anions. In addition, they have a net negative protein surface charge that contributes to repulsion of anions. This review provides recent developments in understanding the behaviour of hyperthermostable cellulases and xylanases in ILs by elucidating protein-IL interactions. It also outlines the current research demonstrating the potential of rational enzyme engineering to improve enzyme tolerance to ILs based on comprehension of IL-induced deactivation mechanisms.

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Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

Section: Effect Of Ils On Stability Of Thermostable Glycoside Hydrolasesmentioning

confidence: 99%

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Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hebal

Boucherba

Bi̇nay

et al. 2021

Biocatalysis and Biotransformation

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“…), ionic liquids (ILs) have rapidly established themselves in the field of bioanalytical protein chemistry during the last two decades. 30 − 33 Using these new green solvents to perform protein detection has received much attention, in particular for identifying the low-abundance analytes in biological samples. 34 , 35 Previous works have mainly focused on using ILs as surface modifiers (i.e., ILs-functionalized or modified substrates) to improve the sensitivity and the limit of detection, 36 , 37 in which the modification process is usually complex.…”

Section: Introductionmentioning

confidence: 99%

Hydrated Ionic Liquids Boost the Trace Detection Capacity of Proteins on TiO₂ Support

et al. 2021

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Trace detection based on surface-enhanced Raman scattering (SERS) has attracted considerable attention, and exploiting efficient strategies to stretch the limit of detection and understanding the mechanisms on molecular level are of utmost importance. In this work, we use ionic liquids (ILs) as trace additives in a protein-TiO 2 system, allowing us to obtain an exceptionally low limit of detection down to 10 –9 M. The enhancement factors (EFs) were determined to 2.30 × 10 4 , 6.17 × 10 4 , and 1.19 × 10 5 , for the three systems: one without ILs, one with ILs in solutions, and one with ILs immobilized on the TiO 2 substrate, respectively, corresponding to the molecular forces of 1.65, 1.32, and 1.16 nN quantified by the atomic force microscopy. The dissociation and following hydration of ILs, occurring in the SERS system, weakened the molecular forces but instead improved the electron transfer ability of ILs, which is the major contribution for the observed excellent detection. The weaker diffusion of the hydrated IL ions immobilized on the TiO 2 substrate did provide a considerably greater EF value, compared to the ILs in the solution. This work clearly demonstrates the importance of the hydration of ions, causing an improved electron transfer ability of ILs and leading to an exceptional SERS performance in the field of trace detection. Our results should stimulate further development to use ILs in SERS and related applications in bioanalysis, medical diagnosis, and environmental science.

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“…Singh et al, 2020). The destabilizing power of [emim][EtSO 4 ] and [emim][Et 2 PO 4 ] was higher than that of a strong denaturant as observed from lowering in the T…”

mentioning

confidence: 99%

Use of Ionic Liquids in Protein and DNA Chemistry

Shukla

Mikkola

2020

Front. Chem.

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Ionic liquids (ILs) have been receiving much attention as solvents in various areas of biochemistry because of their various beneficial properties over the volatile solvents and ILs availability in myriad variants (perhaps as many as 108) owing to the possibility of paring one cation with several anions and vice-versa as well as formulations as zwitterions. Their potential as solvents lies in their tendency to offer both directional and non-directional forces toward a solute molecule. Because of these forces, ionic liquids easily undergo intermolecular interactions with a range of polar/non-polar solutes, including biomolecules such as proteins and DNA. The interaction of genomic species in aqueous/non-aqueous states assists in unraveling their structure and functioning, which have implications in various biomedical applications. The charge density of ionic liquids renders them hydrophilic and hydrophobic, which retain intact over long-range of temperatures. Their ability in stabilizing or destabilizing the 3D-structure of a protein or the double-helical structure of DNA has been assessed superior to the water and volatile organic solvents. The aptitude of an ion in influencing the structure and stability of a native protein depends on their ranking in the Hofmeister series. However, at several instances, a reverse Hofmeister ordering of ions and specific ion-solute interaction has been observed. The capability of an ionic liquid in terms of the tendency to promote the coiling/uncoiling of DNA structure is noted to rely on the basicity, electrostatic interaction, and hydrophobicity of the ionic liquid in question. Any change in the DNA's double-helical structure reflects a change in its melting temperature (Tm), compared to a standard buffer solution. These changes in DNA structure have implications in biosensor design and targeted drug-delivery in biomedical applications. In the current review, we have attempted to highlight various aspects of ionic liquids that influence the structure and properties of proteins and DNA. In short, the review will address the issues related to the origin and strength of intermolecular interactions, the effect of structural components, their nature, and the influence of temperature, pH, and additives on them.

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Dual mechanism of ionic liquid-induced protein unfolding

Abstract: Ionic liquids (ILs) are gaining attention as protein stabilizers and refolding additives. However, varying degrees of success with this approach motivates the need to better understand fundamental IL-protein interactions. A...

Cited by 20 publications

References 52 publications

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hydrated Ionic Liquids Boost the Trace Detection Capacity of Proteins on TiO₂ Support

Use of Ionic Liquids in Protein and DNA Chemistry

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Dual mechanism of ionic liquid-induced protein unfolding

Abstract: Ionic liquids (ILs) are gaining attention as protein stabilizers and refolding additives. However, varying degrees of success with this approach motivates the need to better understand fundamental IL-protein interactions. A...

Cited by 20 publications

References 52 publications

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hydrated Ionic Liquids Boost the Trace Detection Capacity of Proteins on TiO2 Support

Use of Ionic Liquids in Protein and DNA Chemistry

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Product

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Hydrated Ionic Liquids Boost the Trace Detection Capacity of Proteins on TiO₂ Support