The thermochemical characteristics of solution of L-cysteine and L-asparagine in aqueous 1,4-dioxane and acetone

The integral heats of solution Δ_sol H ^m of L-cysteine and L-asparagine in mixtures of water with 1,4-dioxane and acetone were measured by solution calorimetry at organic solvent concentrations of up to 0.30 mole fractions. The standard enthalpies of solution (Δ_sol H ^o) and transfer (Δ_tr H ^o) of amino acids from water to mixed solvents were calculated. The calculated enthalpy coefficients of pair interactions of L-cysteine and L-asparagine with cosolvent molecules were positive. The results were interpreted from the point of view of the predominance of interactions of various types in solutions and the influence of the nature of cosolvents and amino acid side substituents on the thermochemical characteristics of solution.     

The thermochemical characteristics of solution of DL-α-alanylglycine and DL-α-alanyl-DL-α-alanine in water-organic solvent mixtures at 298.15 K

The integral enthalpies of solution of DL-α-alanylglycine and DL-α-alanyl-DL-α-alanine in water-organic solvent (acetonitrile, 1,4-dioxane, acetone, N,N-dimethylformamide, and N,N-dimethylsulfoxide) mixtures were measured at organic component concentrations x ₂ = 0–0.4 mole fractions and T = 298.15 K. The standard enthalpies of solution (Δ_sol H°) and transfer (Δ_tr H°) of the peptides from water into mixed solvents were calculated. The influence of the structure and properties of solutes and mixture composition on the thermochemical characteristics of the peptides was considered. The enthalpy coefficients of pair interactions (h _xy ) of DL-α-alanylglycine and DL-α-alanyl-DL-α-alanine with organic solvent molecules were calculated. The h _xy values were correlated with the properties of organic solvents using the Kamlet-Taft equation.     

Enthalpy characteristics of the dissolution of L-valine in water/formamide mixtures at 298.15 K

The thermochemical dissolution of L-valine in solvent mixtures H₂O + (formamide, N-methylformamide, and N,N-dimethylformamide) is studied at an organic component concentration of x₂ = 0–0.35 molar fractions and a temperature of 298.15 K. The experimental data are used to calculate standard enthalpies of dissolution, the transferring of L-valine from water to a mixed solvent, and the enthalpy coefficients of pairwise interactions (h_xy) with organic solvent molecules. The correlation between the enthalpy characteristics of the dissolution of L-valine with the composition of aqueous organic mixtures and the nature of the organic solvent (its physicochemical properties) is determined. A comparative analysis of the values of h_xy of a number of aliphatic L-amino acids in similar solvent mixtures with the hydrophobicity parameters of their side chains is performed.     

Measuring the enthalpies of interaction between glycine,L-cysteine,glycylglycine, and sodium dodecyl sulfate in aqueous solutions

Calorimetric measurements of enthalpies of solution Δ_sol H ^m for glycine, L-cysteine, and glycylglycine in aqueous solutions of sodium dodecyl sulfate (SDS) with concentrations of up to 0.05 mol kg^–1 are made. Standard enthalpy of solution Δ_sol H ⁰ and enthalpy of transfer Δ_tr H ⁰ of the dipeptide from water into mixed solvent are calculated. The calculated enthalpy coefficients of paired interactions of amino acids and dipeptide with SDS prove to be positive. Hydrophobic interactions between the biomolecules and SDS are found to have a major impact on the enthalpies of interaction in the three-component systems under study, within the indicated range of concentrations.     

The enthalpies of solution of L-α-alanyl-L-α-alanine in water-organic solvent mixtures at 298.15 K

The integral enthalpies of solution (T = 298.15 K) of L-α-alanyl-L-α-alanine in aqueous-organic solvents (acetonitrile, 1,4-dioxane, acetone, formamide, N-methylformamide, N,N-dimethylformamide, N,N-diethylformamide, and N,N-dimethylsulfoxide) were measured at organic component concentrations x ₂ = 0–0.3 mole fractions. The standard enthalpies of solution (Δ_sol H ^o) and transfer (Δ_tr H ^o) of the peptide from water into mixed solvents were calculated. The influence of the structure and properties of solutes and mixture composition on solute thermochemical characteristics is considered. The enthalpy pair interaction coefficients h _xy between L-α-alanyl-L-α-alanine and organic solvent molecules were calculated. The linear Kamlet-Taft four-parameter equation was used to reveal correlation between the h _xy values and the properties of organic solvents.     

Enthalpy characteristics of L-proline dissolution in certain water–organic mixtures at 298.15 K

A thermochemical study of the processes of L-proline dissolution in aqueous solutions of acetonitrile, 1,4-dioxane, acetone, dimethyl sulfoxide, nitromethane and tetrahydrofuran at Т = 298.15 K in the range of organic solvent concentrations x₂ = 0–0.25 mole fractions is performed. Standard values of the enthalpies of solution and transfer of L-proline from water to mixed solvent, and the enthalpy coefficients of pairwise interactions between L-proline and molecules of organic solvents, are calculated. The effect the composition of a water–organic mixture and the structure of organic solvents have on the enthalpy characteristics of L-proline dissolution and transfer is examined. The effect the energy properties of intermolecular interactions between components of a mixed solvent has on the intermolecular interactions between L-proline and molecules of cosolvent is estimated. The correlation between the enthalpy characteristics of L-proline dissolution and electron-donor properties of organic cosolvent in aqueous solutions is determined.     

The enthalpy of solution of DL-α-alanyl-DL-α-valine depending on the composition of water-alcohol binary solvents at 298.15 K

The integral enthalpies of solution of DL-α-alanyl-DL-α-valine in water-ethanol, water-n-propanol, and water-isopropanol mixtures at alcohol concentrations x ₂ = 0–0.4 mole fractions were measured calorimetrically. The enthalpies of solution of the peptide Δ_sol H° and transfer from water to a mixed solvent Δ_tr H° were calculated. The effect of the structure and properties of the peptide and mixture composition on the enthalpy characteristics of the peptide are discussed. The enthalpy coefficients of pair interactions h _xy of DL-α-alanyl-DL-α-valine with alcohol molecules were calculated. It was found that they were positive and increased in the series ethanol, n-propanol, isopropanol. An analysis of the results allows the general features of changes in the thermodynamic parameters of solution of peptides of the DL-α-alanine series with different amino acid residues in water-alcohol mixtures to be established.     

Thermochemical analysis of intermolecular interactions between <Emphasis Type="Italic">N</Emphasis>-acetylglycine and polyols in aqueous solutions

The integral enthalpies of dissolution Δ_sol H _m for N-acetylglycine in aqueous solutions of glycerol, ethylene glycol and 1,2-propylene glycol are measured via solution calorimetry. The standard enthalpies of dissolution (Δ_sol Н ⁰) and transfer (Δ_tr Н ⁰) for N-acetylglycine from water to aqueous solutions of polyhydric alcohols are calculated from experimental data. Positive values of enthalpy coefficients of pair interactions h _xy for amino acids and polyol molecules are calculated using the McMillan–Mayer theory. The results are discussed using an approach for evaluating different types of interactions in ternary systems and the effect the structural features of interacting biomolecules have on the thermochemical characteristics of N-acetylglycine dissolution.     

Thermochemistry of glycyl-<Emphasis Type="Italic">DL</Emphasis>-α-alanine dissolution in water-alcohol solutions at 298.15 K

Integral enthalpies of glycyl-DL-α-alanine dissolution in aqueous solutions of ethanol, 1-propanol, and 2-propanol at concentrations of alcohols up to 0.4 mol fraction were measured by the calorimetry method. Standard values of the enthalpies of the peptide dissolution Δ_sol H ⁰ and transfer Δ_tr H ⁰ from water in mixed solvents were calculated. Dependences of the thermochemical characteristics of glycyl-DL-α-alanine dissolution on the concentration of cosolvents are of an extreme character. Within the limits of McMillan-Mayer’s theory enthalpy coefficients of pairwise interactions (h _xy ) of the studied compound with molecules of alcohols were calculated. They have positive values increasing in the series ethanol, 1-propanol, 2-propanol. The effect of the structure of dipeptides and composition of water-alcohol solvents on the dissolution enthalpy characteristics was considered on the basis of the obtained experimental and calculated data.     

The thermochemical characteristics of solution of DL-α-alanylglycine and DL-α-alanylalanine in water-alcohol mixtures at 298.15 K

The integral enthalpies of solution of DL-α-alanylglycine and DL-α-alanylalanine in water-ethanol, water-n-propanol, and water-isopropanol mixtures were measured calorimetrically at alcohol concentrations x ₂ = 0?0.4 mole fractions. The standard enthalpies of solution (Δ_sol H°) of the peptides and their transfer (Δ_tr H°) from water into the mixed solvents were calculated. The influence of the structure and properties of the solutes and mixture composition on the enthalpy characteristics were considered. The Δ_sol H° = f(x ₂) and Δ_tr H° = f(x ₂) dependences were found to have extrema. The enthalpy coefficients of pair interactions (h _xy ) between the peptide and alcohol molecules were calculated. The coefficients were positive and increased in the series ethanol, n-propanol, isopropanol.     

Thermodynamic characteristics of solution and viscous flow of amino acids in water at 298.15 K

Thermodynamic and transport properties of aqueous solutions of 13 amino acids at 298.15 K are analyzed in relation to the structure of the side chains of the biomolecules on the basis of the newly obtained and published data. The standard enthalpies of solution (Δ_sol H ⁰), partial molar volumes (V _2,φ ⁰ ), and partial molar contributions to the molar Gibbs free energy of activation of the viscous flow (Δμ ₂ ^0≠ ) were determined for the amino acids in water. Correlation equations were suggested to describe the relationship between the enthalpy characteristics of hydration of amino acids, viscous flow parameters, and bulk properties of their aqueous solutions.     

The thermodynamic characteristics of solution of L-α-histidine and L-α-phenylalanine in water at 273–373 K

The solubility of L-phenylalanine and L-histidine in water at 298.15 and 318.15 K and the heat effects of solution of the amino acids at 328.15 K were determined. These results and the data obtained earlier were used to calculate all the standard thermodynamic functions of solution of the amino acids and the solubilities of L-phenylalanine and L-histidine over the temperature range 273–373 K. The selection of the form of the Δ_sol H ^o = f(T) dependence had a negligible effect on the free energies of solution and solubilities of the amino acids. This selection primarily influenced the entropy and heat capacity characteristics of the process.     

The chemical stability of L-isoleucine,L-threonine,and L-serine in aqueous solutions of KCl at 298.15 K

The experimental saturated solubilities of L-isoleucine, L-threonine, and L-serine in aqueous mixtures of a KCl solution at 298.15 K are presented in this article. The solubilities are measured by gravimetric method. In the present study the theoretical calculation of the standard transfer Gibbs free energy, cavity forming enthalpy of transfer, cavity forming transfer Gibbs free energy, dipole-dipole interaction effect have been computed. The chemical effects of the transfer Gibbs energies for the present amino acids have been obtained by subtracting the cavity effects and dipole-dipole interaction effects from the ΔG_t⁰(i). The stability of the experimental amino acids in aqueous KCl in terms of thermodynamic parameters is explained.     

The thermodynamic parameters of the step dissociation of L-phenylalanyl in aqueous solution

The heats of interaction of L-phenylalanine with solutions of nitric acid and potassium and lithium hydroxides were determined calorimetrically at 288.15, 298.15, and 308.15 K and solution ionic strengths of 0.5, 0.75, and 1.0 in the presence of LiNO₃ and KNO₃. The standard thermodynamic characteristics (Δ_r H°, Δ_r G°, Δ_r S°, and ΔC _p ^° of acid-base interactions in aqueous solutions of L-phenylalanine were calculated. The influence of the concentration of background electrolytes and temperature on the heats of dissociation of L-phenylalanine was considered. A comparative analysis of the standard thermodynamic characteristics of step dissociation of L-phenylalanine and alanine was performed in terms of the modern concepts of the structure and physicochemical properties of these compounds and their solutions.     

Thermodynamic characteristics of the dissolution of glycine,glycylglycine, and glycylglycylglycine in aqueous solutions of sodium dodecyl sulfate at <Emphasis Type="Italic">Т</Emphasis> = 298.15 K

the enthalpies of dissolution of glycine (Gly), glycylglycine (GlyGly), and glycylglycylglycine (GlyGlyGly) are measured in aqueous solutions of sodium dodecyl sulfate (SDS) at SDS concentrations m = 0–0.7 mol kg^?1 and Т = 298.15 K by means of calorimetry. The obtained data are used to calculate the standard values of enthalpies of dissolution (Δ_sol H ^m ) and enthalpies of transfer (Δ_tr H ^m ) of glycine and its oligomers from water to SDS aqueous solutions. The dependences of Δ_sol H ^m and Δ_tr H ^m on SDS concentration in an aqueous solution at a constant concentration of glycine and its oligomers are determined. A comparative analysis of the thermodynamic characteristics of Gly, GlyGly, and GlyGlyGly transfer within the studied range of SDS concentrations is performed. The results are interpreted in terms of ion–ion, ion–polar, and hydrophobic interactions between SDS and molecules of glycine and its oligomers.     

Interaction Between an Active Pharmaceutical Ingredient Ionic Liquid Benzalkonium Salicylate and Small Biomolecules in Aqueous Solution: UV Absorption,Conductivity, and Volumetric Study

UV absorption spectroscopy, electrical conductivity and density experiments have been used to investigate the interactions of some small biomolecules (amino acids/dipeptides) with an active pharmaceutical ingredient in ionic liquid form (API-IL), benzalkonium salicylate (BaSal), in aqueous solution. A number of useful parameters, such as critical micellar concentration (cmc), aggregation number (N_agg) and limiting molar conductivity (Λ₀) of BaSal, standard partial molar volumes (\(V_{2,\phi }^{ \circ }\)), corresponding volumes of transfer from water to aqueous BaSal solutions (Δ_trV^o), standard partial molar expansibilities (\(E_{\phi }^{ \circ }\)), hydration number (n_H) of small biomolecules, as well as the binding constants (K_b) for small biomolecule–BaSal complexes have been evaluated. The dependence of the properties on concentration, temperature and alkyl chain length of amino acids/dipeptides is examined. The results are used to identify the solute–solvent physicochemical interactions occurring in the studied systems.     

Thermodynamics of interaction of L-α-phenylalanine with urea and dimethylformamide in aqueous solution

The thermal effects of solution of L-phenylalanine in aqueous solutions of urea and dimethylformamide (DMF) at 25°C were determined. The solubility of L-phenylalanine in water and aqueous DMF solutions was measured. The standard enthalpies, free energies, and entropies of solution of the amino acid in aqueous solutions of amides were calculated. The parameters of pair and ternary amino acid-amide interactions were determined within the framework of the McMillan-Mayer theory. The amino acid-amide pair interaction is accompanied by a decrease in the Gibbs free energy, controlled by the entropy term with DMF and by the enthalpy term with urea. The interaction of L-phenylalanine with two amide molecules is repulsive, which in the case of DMF leads to an increase in the standard free energies of solution of the amino acid at the amide mole fraction X ₂ > 0.05.     

Solubility of <Emphasis Type="Italic">d</Emphasis>-elements salts in organic and aqueous-organic solvents: IV. Solubility of cadmium chloride

Solubility of cadmium chloride at 25°C in four ternary systems containing mixed water-organic solvents was measured by the isothermal saturation method. Dimethyl sulfoxide, N,N-dimethylacetamide, N,N-dimethylformamide, and 1,4-dioxane were used as organic components. In all systems the organic component addition provides a salting-out effect within the whole range of the binary solvent compositions.     

Thermal properties of <Emphasis Type="Italic">n</Emphasis>-R<Subscript>4</Subscript>NBr solutions in binary solvents containing formamide

The enthalpies of solution of tetraethyl- and tetra-n-hexylammonium bromides have been measured in mixtures of formamide with ethylene glycol at 298.15 and 313.15 K in the whole mole fraction range by the calorimetric method. The standard enthalpies of solution in binary mixtures have been calculated with Redlich–Rosenfeld–Meyer type equation. The enthalpy and heat capacity parameters of pair interaction of organic electrolytes with EG in FA and with FA in EG have been computed and discussed. The enthalpy interaction parameters of single ions with EG in FA medium have been evaluated and compared with those for ion–water and ion–MeOH interaction in FA. The standard heat capacities of solution have been evaluated. The excess enthalpies of solution, Δ_sol H ^E, of Et₄NBr, Bu₄NBr, and Hex₄NBr have been determined. The Δ_sol H ^E values are positive for Et₄NBr and negative for Bu₄NBr and Hex₄NBr and become more negative from Bu₄NBr to Hex₄NBr.     

Prediction of partition and distribution coefficients in various solvent pairs with COSMO-RS

Performance of COSMO-RS method as a tool for partition and distribution modeling in 20 solvent pairs—composed of neutral or acidic aqueous solution and organic solvents of different polarity, ranging from alcohols to toluene and hexane—was evaluated. Experimental partition/distribution data of lignin-related and drug-like compounds (neutral, acidic, moderately basic) were used as reference. Several aspects of partition modeling were addressed: accounting for mutual saturation of aqueous and organic phases, variability of systematic prediction errors across solvent pairs, taking solute ionization into account. COSMO-RS was found to predict extraction outcome for both ligneous and drug-like compounds in various solvent pairs fairly well without any additional empirical input. The solvent-specific systematic errors were found to be moderate, despite being statistically significant, and related to the solvent hydrophobicity. Accounting for mutual solubilities of the two liquids was proven crucial in cases where water was considerably soluble in the organic solvent. The root mean square error of a priori logP prediction varied, depending mainly on the solvent pair, from 0.2 to 0.7, overall value being 0.6 log units. The accuracy was higher in case of hydrophilic than hydrophobic solvents. The logD predictions were less accurate, due to pK_a prediction being an additional source of error, and also because of the complexity of modeling the behaviour of ionic species in the two-phase system. A simple correction for partitioning of free ions was found to notably improve logD prediction accuracy in case of the most hydrophilic organic phase (butanol/water).