Correction to “Thermodynamic Studies of Ionic Hydration and Interactions for Amino Acid Ionic Liquids in Aqueous Solutions at 298.15 K”

Dagade, Dilip H.; Madkar, Kavita R.; Shinde, Sandeep P.; Barge, Seema S.

doi:10.1021/jp407212s

Cited by 4 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The negative values of NB 22 *0 can be interpreted in terms of the hydrophobic association of ions; a similar effect is also reported in case of tetraphenylboron ), supporting the earlier observation for aqueous AAILs that the anion hydrophobicity of ionic liquids is directly related to the osmotic second virial coefficient, meaning that the magnitude of NB 22 *0 is a direct measurement of the anion hydrophobicity of the ionic liquids.…”

Section: Discussionsupporting

confidence: 86%

“…Thus, on going from glycine to l -leucine, that is, with increasing hydrophobicity of the amino acid anions in AAILs, ion-pair separation occurs, and the force responsible for this is the hydrophobic anion–anion interactions which may cause association of like charged species, such as anion–anion in this case. Further, if we compare data of NB 22 *0 from this work with the data reported earlier for AAILs based on the 1-ethyl-3-methylimidazolium cation, it is found that as the hydrophobicity of the cation increases, the ion-pair–ion-pair interactions become favorable as seen from the comparatively more negative magnitude of NB 22 *0 for [Bmim][Gly] than [Emim][Gly]. A similar effect is also seen for remaining studied AAILs.…”

Section: Discussionsupporting

confidence: 80%

“…Correlation of the osmotic second virial coefficient ( NB 22 *0 ) with the Pitzer interaction parameter, β (0) , for AAILs in aqueous solutions at 298.15 K: [Bmim][AA], ◊ (this work); [Emim][AA], ○ (from refs and ).…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Osmotic and Activity Coefficients for Binary Aqueous Solutions of 1-Butyl-3-methylimidazolium Based Amino Acid Ionic Liquids at 298.15 K and at 0.1 MPa

Shinde

Dagade

2015

J. Chem. Eng. Data

Self Cite

View full text Add to dashboard Cite

The osmotic coefficient data for aqueous solutions containing 1-n-butyl-3methylimidazolium ([Bmim]) based amino acid ionic liquids (AAILs) made from glycine, Lalanine, L-valine, and L-leucine are obtained in the concentration range of ∼0.01 mol•kg −1 to ∼0.6 mol•kg −1 at 298.15 K and at 0.1 MPa using vapor pressure osmometry. Activity coefficients of both components, that is, solute and solvent (water), in mixture were estimated using experimental osmotic coefficient data and have been further used to obtain the excess and mixing Gibbs free energies for the studied systems. The concentration dependence of osmotic coefficients indicates possible ion-pair formation and hence the ion-pair dissociation constant for all the studied AAILs in aqueous solutions at 298.15 K is reported. The nonelectrolyte contribution due to ion-pair formation in the aqueous AAIL solutions was discussed through estimation of osmotic second virial coefficients for AAILs using the McMillan−Mayer theory of solutions. Application of the Pitzer model to the experimental osmotic coefficient data indicated that anion−anion interactions in aqueous solutions of AAILs are favored over the cation− anion interactions with the increasing alkyl chain length on the anion signifying the hydrophobic effect responsible for attraction between the like-charged species.

show abstract

Section: Discussionsupporting

confidence: 86%

Section: Discussionsupporting

confidence: 80%

See 1 more Smart Citation

Osmotic and Activity Coefficients for Binary Aqueous Solutions of 1-Butyl-3-methylimidazolium Based Amino Acid Ionic Liquids at 298.15 K and at 0.1 MPa

Shinde

Dagade

2015

J. Chem. Eng. Data

Self Cite

View full text Add to dashboard Cite

show abstract

“…Miscibility of water and AAILs is excellent over a wide range of contents . Dagade et al reported thermodynamics of ionic hydration and discussed solvent–solute interactions of AAILs in water at room conditions. Woo and coworkers simulated certain equilibrium and transport properties of AAILs.…”

Section: Introductionmentioning

confidence: 99%

“…Amino acid‐based ionic liquids (AAILs) represent an interesting and recent implementation of RTILs . In AAILs, the anion is obtained from a molecular amino acid via deprotonation, whereas the cation can be picked up in view of prospective usage.…”

Section: Introductionmentioning

confidence: 99%

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

2015

View full text Add to dashboard Cite

Abstract. Using molecular dynamics simulations, the structure of model mini-protein was thoroughly characterized in the imidazolium-based amino acid ionic liquids and their aqueous solutions. We report that the mini-protein is more stable when AAIL is added as a cosolvent.Complete substitution of water by organic cations and anions further results in hindered conformational flexibility of the mini-protein. This observation suggests that AAILs are able to defend proteins from thermally induced denaturation. We show by means of radial distributions that the mini-protein is efficiently solvated by both solvents due to agood mutual miscibility. However, amino acid based anions prevail in the first coordination sphere of the mini-protein.

show abstract

Protein remains stable at unusually high temperatures when solvated in aqueous mixtures of amino acid based ionic liquids

2016

View full text Add to dashboard Cite

Using molecular dynamics simulations, we investigated the thermal stability and real-time denaturation of a model mini-protein in four solvents: (1) water, (2) 1-ethyl-3-methylimidazolium alaninate [EMIM][ALA] (5 mol% in water), (3) methioninate [EMIM][MET] (5 mol% in water), and (4) tryptophanate [EMIM][TRP] (5 mol% in water). Upon analyzing the radius of gyration, the solvent-accessible surface area, root-mean-squared deviations, and inter- and intramolecular hydrogen bonds, we found that the mini-protein remains stable at 30-40 K higher temperatures in aqueous amino acid based ionic liquids (AAILs) than in water. This thermal stability was correlated with the thermodynamics and shear viscosity of the AAIL-containing mixtures. These results suggest that AAILs are generally favorable for protein conservation. Graphical Abstract Conformation of the [TRP]-cage mini-protein in an aqueous amino acid based ionic liquid (AAIL).

show abstract

Correction to “Thermodynamic Studies of Ionic Hydration and Interactions for Amino Acid Ionic Liquids in Aqueous Solutions at 298.15 K”

Cited by 4 publications

References 0 publications

Osmotic and Activity Coefficients for Binary Aqueous Solutions of 1-Butyl-3-methylimidazolium Based Amino Acid Ionic Liquids at 298.15 K and at 0.1 MPa

Osmotic and Activity Coefficients for Binary Aqueous Solutions of 1-Butyl-3-methylimidazolium Based Amino Acid Ionic Liquids at 298.15 K and at 0.1 MPa

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

Protein remains stable at unusually high temperatures when solvated in aqueous mixtures of amino acid based ionic liquids

Contact Info

Product

Resources

About