Does the stability of proteins in ionic liquids obey the Hofmeister series?

Kumar, Awanish; Venkatesu, Pannuru

doi:10.1016/j.ijbiomac.2013.10.031

Cited by 103 publications

(109 citation statements)

References 179 publications

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“…3,4 Small ions are termed kosmotropes and cause strong electrostatic ordering of nearby water molecules because of their high charge densities. In contrast, large ions are chaotropes and have low 40 charge densities; they do not necessarily influence the structure of the hydrogen-bonded water molecules. 5 Besides the role of the ions to effect the water structure, it has been demonstrated that the direct interactions between the ions and the biomolecules is the key to understand the Hofmeister series.…”

Section: Introductionmentioning

confidence: 96%

“…[37][38][39] Moreover, the protein stability in ILs remain to be poorly understood because of the difficulties in obtaining the structural information of proteins in the presence of the anions of the Hofmeister 10 series. 40,41 The structural dissimilarity between ILs and Isis basically responsible for the large differences in their physical properties. However, up to now no reliable scientific source exists to compare the stabilization properties of any novel IL and 15 Is for biomolecules.…”

Section: Introductionmentioning

confidence: 99%

“…Crystal structure of CT (monomeric form) representing the location of the Trp residues in the peptide chain, downloaded from protein data bank (ID code 2CHA) and processed with PyMOL viewer software. 40 ILs combined with imidazoliumcations are highly stable and have deserved special attention in the field of protein stabilities. [45][46][47] These ILs offers new possibilities for the application of solvent engineering to enzymatic reactions and it has been revealed in some cases that the activity of the enzyme in 45 ILs obeys Hofmeister series.…”

Section: Introductionmentioning

confidence: 99%

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A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

2015

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In this article, we have compared the anions of sodium salts (Is) and ionic liquids (ILs) with the stability and structure of αchymotrypsin (CT), through fluorescence, thermal fluorescence 10 analysis and circular dichroism (CD) spectroscopy. The experimental results revealed that the Hofmeister series of anions such as SCN‾, SO 4 2¯, Cl‾, Br‾, CH 3 COO‾ and I‾ of Is destabilized the native structure of the CT. On the contrary, the anions such as CH 3 COO‾, Cl‾ and Br‾ of imidazolium-based IL with fixed cation 15 such as 1-butyl-3-methylimidazolium, [Bmim] + stabilized the native structure of the CT. The remaining anions of ILs such as SCN‾, HSO 4 ‾, and I‾ acted as denaturing agents for the native structure of CT. Furthermore, molecular docking results show that the imidazolium-cation of the IL enters the sub-domains of 20 the CT and interacts with the ionic residues of the CT, that is Ser217 close to Trp215. This interaction is in well agreement with the fluorescence quenching observed for CT in the presence of [Bmim] + . On the other hand, the destabilizing anion such as SO 4 2¯w as observed to be directly interacting with Ser195 in the 25 active site of the CT. We have observed that the Hofmeister series effects of anions of either Is or ILs are entirely based on the interaction of the anions with its counterion, that is the cation, with solvent molecules, as well as with the protein surface. Evidently, these interactions vary with co-solvent system and the 30 type of the protein. Hence, the stability of a biomolecule in the presence of the anions may or may not obey Hofmeister series. 65 80

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Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

2015

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“…Further, hydrophobicity of ILs which is expressed in terms of log P scale is another important feature of solvent property affecting the enzyme performance in ILs. The kosmotropicity of ions based on well known Hofmeister series is another important aspect affecting the solvent property of ILs41,89 .It is noteworthy to shed some light on the effects of ions on solvation on general basis. ILs are made up of ions with the fact that in aqueous solution hydrophillic ILs dissociate into individual ions 89.…”

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confidence: 99%

Endeavour to simplify the frustrated concept of protein-ammonium family ionic liquid interactions

Jha

Venkatesu

2015

Phys. Chem. Chem. Phys.

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The large amount of attention earned by ionic liquids (ILs) in the various physical and chemical sciences has been attributed to their unique, designer nature. In the past few years, the role of ILs in protein folding/unfolding has been rapidly growing. In light of the increasing importance of ILs, it is desirable to systematize the ion effects on protein properties such as structure stability, activity and enantioselectivity. Various studies available in the literature show ILs as a potential solvent medium for many enzymatic reactions, as well as in various protein folding/unfolding studies. Various reviews by many researchers focus on the synthesis, application and general properties of the ILs, however a review focussing on the effect of various ILs on the activity, structure and stability of proteins is still missing. Also, according to the best of our knowledge there is no single review available throughout the literature that focuses on the effect of the same family of ILs on different proteins. Therefore, it is a priority to obtain complete knowledge of the biomolecules, particularly amino acids (AAs) and proteins in a particular IL family. The focus of the present perspective is to investigate the performance of a list of proteins and protein model compounds in the presence of ammonium-based ILs. This perspective presents a survey of all the key developments from the available reports and also our past and present experience related to proteins and ammonium-based ILs. Additionally, we have tried to put the available information in chronological order in most of the cases. The use of ammonium family ILs as a co-solvent for various proteins model compounds and proteins has been outlined. This perspective can act as a barometer for reckoning the various advancements made in this field and can also galvanize further investigation of various untouched aspects of this research area.

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“…However, it was also shown that certain proteins, for example the redox active form of cytochrome c , could be denatured by imidazolium-based ionic liquids [18], [19], yet choline-based ionic liquids were recently shown to improve the redox activity of cytochrome c [20]. While stability and enzymatic activity of a few proteins in ionic liquid-containing aqueous media correlate with the Hofmeister's series [21], [22] others do not [23], [24]. Using simulations, it was also suggested that ionic liquids could influence xylanase activity by disturbing the dynamic motion of the protein in addition to affecting protein structure [25].…”

Section: Introductionmentioning

confidence: 99%

The effects of high concentrations of ionic liquid on GB1 protein structure and dynamics probed by high-resolution magic-angle-spinning NMR spectroscopy

Warner

Gjersing

Follett

et al. 2016

Biochemistry and Biophysics Reports

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Ionic liquids have great potential in biological applications and biocatalysis, as some ionic liquids can stabilize proteins and enhance enzyme activity, while others have the opposite effect. However, on the molecular level, probing ionic liquid interactions with proteins, especially in solutions containing high concentrations of ionic liquids, has been challenging. In the present work the 13C, 15N-enriched GB1 model protein was used to demonstrate applicability of high-resolution magic-angle-spinning (HR-MAS) NMR spectroscopy to investigate ionic liquid–protein interactions. Effect of an ionic liquid (1-butyl-3-methylimidazolium bromide, [C4-mim]Br) on GB1was studied over a wide range of the ionic liquid concentrations (0.6–3.5 M, which corresponds to 10–60% v/v). Interactions between GB1 and [C4-mim]Br were observed from changes in the chemical shifts of the protein backbone as well as the changes in 15N ps-ns dynamics and rotational correlation times. Site-specific interactions between the protein and [C4-mim]Br were assigned using 3D methods under HR-MAS conditions. Thus, HR-MAS NMR is a viable tool that could aid in elucidation of molecular mechanisms of ionic liquid–protein interactions.

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Does the stability of proteins in ionic liquids obey the Hofmeister series?

Cited by 103 publications

References 179 publications

A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

Endeavour to simplify the frustrated concept of protein-ammonium family ionic liquid interactions

The effects of high concentrations of ionic liquid on GB1 protein structure and dynamics probed by high-resolution magic-angle-spinning NMR spectroscopy

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