Ionic Liquids and Proteins: Academic and Some Practical Interactions

Yang, Zhen

doi:10.1002/9781118158753.ch2

Cited by 8 publications

(3 citation statements)

References 183 publications

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“…ILs have been found to strongly affect protein structure and function by depleting the protein surface of water molecules, which are otherwise crucial in preserving the functional environment and polarity of the biomolecule. Especially, the IL anions having high Hbond basicity often significantly interfere with the native protein structure by tempering the existing H-bond networks (Yang 2012). With the help of a nucleophilic anion, an IL molecule can break through the strong H-bonding networks of hydrophobic biomolecules, subsequently dissolving them (Zhao et al 2006;Zhao 2016).…”

Section: Introductionmentioning

confidence: 99%

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Sajeevan

Roy

2018

Biophys Rev

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The appearance of several disulfide bond isoforms in multiple cysteine containing venom peptides poses a significant challenge in their synthesis and purification under laboratory conditions. Recent experiments suggest that careful tuning of solvent and temperature conditions can propel the disulfide bond isoform equilibrium in favor of the most potent, native form. Certain aqueous ionic liquids (ILs) have proven significantly useful as solvents for this purpose, while exceptions have also been noted. To elucidate the molecular level origin behind such a preference, we report a detailed explicit solvent replica exchange molecular dynamics study of a conotoxin, AuIB, in pure water and four different aqueous IL solutions (~45-60% v/v). The ILs studied here are comprised of cations like 1-ethyl-3-methyl-imidazolium (Im) or 1-butyl-3-methyl-imidazolium (Im) coupled with either acetate (OAc) or chloride (Cl) as the counter anion. Our simulations unfold interesting features of the conformational spaces sampled by the peptide and its solvation in pure water and aqueous IL solutions. Detailed investigation into populations of the globular disulfide bond isoform of AuIB in aqueous IL solutions reveal distinct trends which might be related to the Hofmeister effect of the cation and anion of the IL and of specific interactions of the aqueous IL solutions with the peptide. In accordance with experimental observations, the aqueous [Im][OAc] solution is found to promote the highest globular isoform population in AuIB.

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Section: Introductionmentioning

confidence: 99%

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Sajeevan

Roy

2018

Biophys Rev

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“…ILs, being highly charged alter the polarity of the protein environment leading to major structural alterations in some cases. Especially, the IL anions having high H‐bond basicity often significantly interfere with the native protein structure, by tempering the existing H‐bond networks . In a recent report, Benedetto et al comprehensively reviewed the current status of bio‐molecular solvation by ILs .…”

Section: Introductionmentioning

confidence: 99%

“…Especially, the IL anions having high H-bond basicity often significantly interfere with the native protein structure, by tempering the existing H-bond networks. [32] In a recent report, Benedetto et al comprehensively reviewed the current status of bio-molecular solvation by ILs. [13] The consequence of solvating a given protein in a specific IL is quite difficult to envisage, owing to the innumerable possible combinations of IL cations and anions and their specific/general interactions with the protein molecule.…”

Section: Introductionmentioning

confidence: 99%

Temperature‐dependent molecular dynamics study reveals an ionic liquid induced 3₁₀‐ to α‐helical switch in a neurotoxin

Sajeevan

Roy

2017

Biopolymers

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Thermal melting and recooling of AuIB, a neurotoxic conopeptide and a highly potent nonaddictive pain reliever is investigated thoroughly in water and an ionic liquid (IL) 1-butyl-3-methylimidazolium Chloride, [Im ][Cl] by classical molecular dynamics simulations. Structural evolution of AuIB in water and the IL is observed at different temperatures between 305 and 400 K, to explore how highly viscous ionic solvents affect the peptide structure as compared to conventional solvent water. At 305 K, unlike water, the coercive effect of IL frustrates AuIB secondary structural motifs significantly. As the temperature is raised, a very interesting IL induced conformational transition from 3 - to α-helix is noticed in the peptide, presumably triggered by a significant restructuring of the peptide H-bond network. The backbone length distributions of the peptide indicate that the IL induced conformational switching is accompanied by a reduction of the axial rise of the helical region, encompassing the residues Pro-6 to Ala-10. Further, we estimated the void space available to the peptide for its structural relaxation within the first solvation shell of ∼5 Å in water as well as in IL. A temperature increase by 100 K, opens up an estimated void volume of ∼70 Å , equivalent to the volume of approximately six water molecules, around the peptide in IL. Cooling simulations of AuIB point to the crucial interplay between thermodynamically favored AuIB conformers and their kinetic control. This study provides a comprehensive understanding of the ionic solvation of biomolecules reinforcing previous experimental findings.

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Effect of Ionic Liquids on Catalytic Properties and Structure of Biocatalysts

Katsoura

Papadopoulou

Polydera

et al. 2015

Ionic Liquid‐Based Surfactant Science

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Ionic Liquids and Proteins: Academic and Some Practical Interactions

Cited by 8 publications

References 183 publications

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Temperature‐dependent molecular dynamics study reveals an ionic liquid induced 3₁₀‐ to α‐helical switch in a neurotoxin

Effect of Ionic Liquids on Catalytic Properties and Structure of Biocatalysts

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Ionic Liquids and Proteins: Academic and Some Practical Interactions

Cited by 8 publications

References 183 publications

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Aqueous ionic liquids influence the disulfide bond isoform equilibrium in conotoxin AuIB: a consequence of the Hofmeister effect?

Temperature‐dependent molecular dynamics study reveals an ionic liquid induced 310‐ to α‐helical switch in a neurotoxin

Effect of Ionic Liquids on Catalytic Properties and Structure of Biocatalysts

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Temperature‐dependent molecular dynamics study reveals an ionic liquid induced 3₁₀‐ to α‐helical switch in a neurotoxin