Enhanced stability of the model mini‐protein in amino acid ionic liquids and their aqueous solutions

Chevrot, Guillaume; Fileti, Eudes Eterno; Chaban, Vitaly V.

doi:10.1002/jcc.24042

Cited by 38 publications

(24 citation statements)

References 37 publications

(79 reference statements)

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“…Amino acid-based ILs are another promising class of biocompatible ILs that have received some interest in recent years (Chevrot et al 2015;Guncheva et al 2015;Sankaranarayanan et al 2012;Tarannum et al 2018). Amino acids have been mostly incorporated as anions, especially with imidazolium or choline cations to produce a biocompatible or Bgreen^IL.…”

Section: Choline-based Ilsmentioning

confidence: 99%

Ionic liquids as biocompatible stabilizers of proteins

2018

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Ionic liquids (ILs) have recently emerged as versatile solvents and additives in the field of biotechnology, particularly as stabilizers of proteins and enzymes. Of interest to the biotechnology industry is the formulation of stable biopharmaceuticals, therapeutic proteins, and vaccines which have revolutionized the treatment of many diseases including debilitating conditions such as cancers and auto-immune diseases. The stabilization of therapeutic proteins is typically achieved using additives that prevent unfolding and aggregation of these proteins during manufacture, transport, and long-term storage. To determine if ILs could be used in the formulation of stable therapeutic proteins, a thorough understanding of the effects of ILs on protein stability is needed, as well as understanding the toxicity of ILs on humans, and other considerations for formulation development such as viscosity and osmolality. In this review, we summarize recent developments on the stabilization of proteins and enzymes using ILs, with emphasis on identifying biocompatible ILs that may be suitable for the formulation of stable biopharmaceuticals in the future.

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Section: Choline-based Ilsmentioning

confidence: 99%

Ionic liquids as biocompatible stabilizers of proteins

2018

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“…RMSD is not only the function of solvent transport properties, but also, and to a larger extent, it is depended on specic chemical interactions between the solute molecule and solvent system. 42 Fig . 7D shows the difference between average RMSD of naringin-DMSO and naringin-water versus mole fraction of DMSO.…”

Section: View Article Onlinementioning

confidence: 99%

Solubility temperature and solvent dependence and preferential solvation of citrus flavonoid naringin in aqueous DMSO mixtures: an experimental and molecular dynamics simulation study

et al. 2017

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This study describes the thermodynamics of dissolution of flavonoid naringin in different aqueous solutions of dimethyl sulfoxide (DMSO) containing 0-100% (w/w) under atmospheric pressure and over a temperature range of 298.15 to 325.15 K. The temperature dependence of solubility of naringin was analyzed using the modified Apelblat equation model, ideal model, and the lH equation model. In a mean harmonic temperature, the dissolution thermodynamic parameters of naringin containing DG sol , DH sol and DS sol were also calculated. Furthermore, the effects of solvent composition on the solubility of this flavonoid were analyzed in terms of Hildebrand's solubility parameter (d H ) and Kamlet, Abboud and Taft (KAT) solvatochromic parameters (a, b, and p*). Finally, the preferential solvation parameters of the flavonoid naringin by DMSO (dx DMSO,S ) were determined from experimental solubility data using the inverse Kirkwood-Buff integrals (IKBIs). It was found that water preferentially solvates naringin in waterrich mixtures while DMSO forms local solvation shells in compositions from 50% (w/w) or x DMSO ¼ 0.19 up to pure co-solvent. Moreover, the structure of solvation shells of naringin in the under study mixtures was obtained by molecular dynamics (MD) simulations. The computational results showed that in the compositions x DMSO > 0.20, the probability of presence of the DMSO molecules in vicinity of naringin is more than water molecules. These findings are compatible with the available IKBI data.

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“…However, Chaban and co-workers (Chevrot et al 2015 ) showed that the radius of gyration does not increase in ionic liquids with amino acid-based anions during the simulation period of 10 ns which may not be long enough to monitor the unfolding process due to the high viscosity of these ionic liquids. Interestingly, Shao ( 2013 ) reported that r g y r of the B domain of protein A from Staphylococcus aureus actually decreased with increasing [C 4 mim]Cl content of the aqueous solution.…”

Section: Large Flexible Proteinsmentioning

confidence: 99%

Computational solvation analysis of biomolecules in aqueous ionic liquid mixtures

Zeindlhofer

Schröder

2018

Biophys Rev

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Based on their tunable properties, ionic liquids attracted significant interest to replace conventional, organic solvents in biomolecular applications. Following a Gartner cycle, the expectations on this new class of solvents dropped after the initial hype due to the high viscosity, hydrolysis, and toxicity problems as well as their high cost. Since not all possible combinations of cations and anions can be tested experimentally, fundamental knowledge on the interaction of the ionic liquid ions with water and with biomolecules is mandatory to optimize the solvation behavior, the biodegradability, and the costs of the ionic liquid. Here, we report on current computational approaches to characterize the impact of the ionic liquid ions on the structure and dynamics of the biomolecule and its solvation layer to explore the full potential of ionic liquids.

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Enhanced stability of the model mini‐protein in amino acid ionic liquids and their aqueous solutions

Cited by 38 publications

References 37 publications

Ionic liquids as biocompatible stabilizers of proteins

Ionic liquids as biocompatible stabilizers of proteins

Solubility temperature and solvent dependence and preferential solvation of citrus flavonoid naringin in aqueous DMSO mixtures: an experimental and molecular dynamics simulation study

Computational solvation analysis of biomolecules in aqueous ionic liquid mixtures

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