Transfer Enthalpies of Amino Acids and Glycine Peptides from Water to Aqueous Solutions of Sugar Alcohol at 298.15 K

Qiu, Xiaomei; Lei, Qunfang; Fang, Wenjun; Lin, Ruisen

doi:10.1021/je800615s

Cited by 34 publications

(12 citation statements)

References 11 publications

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“…(3)-(5) corresponded to the standard enthalpy of Gly-Gly dissolution in pure water, its values coinciding well with the earlier determined reference values: Δ sol Н 0 (Gly-Gly) 11.56±0.07 [11], 11.67 [12], and 11.81±0.0.03 [13]. The enthalpy pair interaction parameters h xy were calculated as h xy = a 1 /2 [14].…”

Section: Mezhevoi Badelin 818supporting

confidence: 82%

Thermochemical study of glycylglycine interaction with polyhydric alcohols in aqueous solution

Mezhevoi

Badelin

2015

Russ J Gen Chem

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Integral enthalpies of glycylglycine dissolution (Δ sol H m ) in aqueous solutions of glycerol, ethylene glycol, and propylene glycol have been determined at the organic co-solvent concentration up to 32 mol %. The standard dissolution enthalpy (Δ sol Н 0 ) and standard enthalpy of transfer of the peptide from water into the binary solvent (Δ tr Н 0 ) have been calculated. The influence of various types of interactions and the structural features of the interacting molecules on the enthalpy of glycylglycine dissolution has been analyzed.Structural stability and functional activity of protein compounds is known to depend on the solvent composition, environmental temperature gradient, the presence of surfactants, pressure changes, and other physicochemical stimuli [1][2][3][4][5]. In particular, the polyhydric alcohols studied in this work participate in stabilization of native conformation of globular proteins [6]. Study of interactions involving oligopeptides (models of proteins) in aqueous-organic mixed solvents allows for deeper understanding of mechanisms of structural stability of complex biopolymers and of their chemical and biological activity. Table 1 lists the experimentally determined enthalpies of dissolution Δ sol Н 0 of glycylglycine (GlyGly) in the binary mixtures of water with glycerol, ethylene glycol, or propylene glycol. The enthalpies of transfer Δ tr Н 0 of the dipeptide from water into the binary solvents are plotted in the Figure as a function of the alcohol molar fraction (х 2 ).From the plots it is seen that the transfer enthalpy reaches a maximum at a certain molar fraction of the organic co-solvent. In general, the transfer enthalpy is determined by a number of various competing interactions including solvation processes. The obtained data were analyzed in terms of the solute-co-solvent interaction applying the approach developed earlier [7][8][9].In the dipeptide-alcohol-water three-component mixtures the hydrates solute molecules exist in a fairly densely packed solution. Therefore, the solvate shells of the molecules are overlapped, resulting in the change of the intermolecular interactions. The calculated enthalpies of transfer of Gly-Gly were combined of several terms, see Eq. (1).Δ tr Н 0 = -ΔН 1 -ΔН 2 + ΔН 3 + ΔН 4 .(1)In Eq. (1), ΔН 1 reflects the ion-bipolar interactions between the polar fragments of the dipeptide (carboxylic, carbonyl, and amino groups) and the polyhydric alcohol hydroxy groups; ΔН 2 stands for the enthalpy of donor-acceptor interactions involving peptide bonds of the dipeptide and the alcohol hydroxy groups; ΔН 3 is assigned to the hydrophobic-hydrophilic interactions between the non-polar dipeptide fragments and hydroxy groups of the co-solvent or zwitter-ion sites of Gly-Gly; and ΔН 4 reflects the hydrophobic-hydrophobic interactions between nonpolar moieties of the dipeptide and the alcohols.The first two types of interactions brought the negative contribution into the Δ tr Н 0 value, whereas the contribution of the other two interaction types was positive....

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Section: Mezhevoi Badelin 818supporting

confidence: 82%

Thermochemical study of glycylglycine interaction with polyhydric alcohols in aqueous solution

Mezhevoi

Badelin

2015

Russ J Gen Chem

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“…Ionic liquids are assumed to be the appropriate medium for studying protein stability . Thermodynamic studies on amino acids as a function of concentration and temperature in the presence of various additives have been performed to understand solute–solvent interactions. − Ionic liquids have been utilized in aqueous biphasic systems consisting of amino acids, to study the protein stability in the presence of ionic liquids that has attracted the attention of different researchers toward their physicochemical properties. Thermodynamic variables like temperature and pressure affect proteins in aqueous medium and play a key role in establishing a complete interpretation of the physical immutability .…”

Section: Introductionmentioning

confidence: 99%

Temperature-Dependent Thermodynamic Properties of Amino Acids in Aqueous Imidazolium-Based Ionic Liquid

2020

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Molecular interactions of amino acids with ionic liquids are significant to study the molecular stability and physicochemical properties of amino acids. Mixtures of amino acids l-leucine and N-acetyl-l-leucine + (0.005, 0.010, 0.030, and 0.050 mol·kg–1) aqueous solution of ionic liquid (1-butyl-3-methylimidazolium chloride) at temperature T = (288.15, 298.15, 308.15, and 318.15 K) have been studied by density and speeds of sound measurements. Volumetric properties have been obtained by utilizing data of density. Volumetric properties include apparent molar volumes, partial molar volumes at infinite dilution, limiting partial molar volumes of transfer at infinite dilution, apparent molar expansibility, etc. Similarly, speeds of sound measurements are utilized to calculate corresponding parameters like apparent molar isentropic compression, K ϕ,s, apparent molar isentropic compression at infinite dilution, K ϕ,s 0, and transfer compressibility at infinite dilution ΔK ϕ,s 0. Results confirmed the predominance of the hydrophilic–hydrophilic interaction over the hydrophobic–hydrophobic interaction in ternary solutions.

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“…Here, by applying Pierotti's approach, we calculated thermodynamic parameters of solvation for xylitol in water and in aqueous amino acids at 298.15 K. Literature survey indicates that no work has been reported on xylitol–amino acid interactions using SPT. However, studies have been reported on xylitol–amino acid interactions using volumetric, calorimetric, solubility and tensiometric methods. These considerations led us to undertake the present study.…”

Section: Introductionmentioning

confidence: 99%

Solvation thermodynamics of xylitol in water and in aqueous amino acids at 298.15 K

Ali

Bidhuri

2012

J of Physical Organic Chem

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The scaled particle theory has been applied to calculate the free energy, ΔGsolv, enthalpy, ΔHsolv, and entropy, ΔSsolv of solvation for xylitol in water and in aqueous amino acids (glycine, alanine and valine) at 298.15 K. The solvation energy, enthalpy and entropy of xylitol are expressed in terms of their various ingredients. The results show that the interaction terms contribute favorably to the process of solvation. The results suggest that the cavity formation for accommodation of xylitol molecules in aqueous amino acids is an enthalpy‐dominated process. Furthermore, the investigated parameters indicate that xylitol–amino acid interactions follow the sequence: glycine alanine valine water. The findings of the present work may help to throw light on the role that xylitol can play to stabilize macromolecules like proteins in aqueous solutions. Copyright © 2012 John Wiley & Sons, Ltd.

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Transfer Enthalpies of Amino Acids and Glycine Peptides from Water to Aqueous Solutions of Sugar Alcohol at 298.15 K

Cited by 34 publications

References 11 publications

Thermochemical study of glycylglycine interaction with polyhydric alcohols in aqueous solution

Thermochemical study of glycylglycine interaction with polyhydric alcohols in aqueous solution

Temperature-Dependent Thermodynamic Properties of Amino Acids in Aqueous Imidazolium-Based Ionic Liquid

Solvation thermodynamics of xylitol in water and in aqueous amino acids at 298.15 K

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