Hydrogen Bonding in Liquid Water and in the Hydration Shell of Salts.

A near-IR spectral study on pure water and aqueous salt solutions is used to investigate stoichiometric concentrations of different types of hydrogen-bonded water species in liquid water and in water comprising the hydration shell of salts. Analysis of the thermodynamics of hydrogen-bond formation signifies that hydrogen-bond making and breaking processes are dominated by enthalpy with non-negligible heat capacity effects, as revealed by the temperature dependence of standard molar enthalpies of hydrogen-bond formation and from analysis of the linear enthalpy-entropy compensation effects. A generalized method is proposed for the simultaneous calculation of the spectrum of water in the hydration shell and hydration number of solutes. Resolved spectra of water in the hydration shell of different salts clearly differentiate hydrogen bonding of water in the hydration shell around cations and anions. A comparison of resolved liquid water spectra and resolved hydration-shell spectra of ions highlights that the ordering of absorption frequencies of different kinds of hydrogen-bonded water species is also preserved in the bound state with significant changes in band position, band width, and band intensity because of the polarization of water molecules in the vicinity of ions.

Influence of protic ionic liquids on hydration of glycine based peptides.

The structure of water, especially around the solute is thought to play an important role in many biological and chemical processes. Water-peptide and cosolvent-peptide interactions are crucial in determining the structure and function of protein molecules. In this work, we present the H-bonding analysis for model peptides like glycyl-glycine (gly-gly), glycine-ւ-valine (gly-val), glycyl-ւ-leucine (gly-leu) and triglycine (trigly) and triethylammonium based carboxylate protic ionic liquids (PILs) in aqueous solutions as well as for peptides in ∼0.2 mol·L-1 of aqueous PIL solutions in the spectral range of 7800-5500 cm-1 using Fourier transform near-infrared (FT-NIR) spectroscopy at 298.15 K. The hydration numbers for peptides and PILs were obtained using NIR method of simultaneous estimation of hydration spectrum and hydration number of a solute dissolved in water. The H-bond of water molecules around peptides and PILs are found to be stronger and shorter than those in pure liquid water. We observe that the hydration shell around zwitterions is a clathrate-like cluster of water in which ions entrap. Watery network analysis confirms that singly H-bonded species or NHBs changes to partial or distorted ice-like structures of water in the hydration shell of PILs. The overall water H-bonding in the hydration sphere of PILs increases in the order TEAF < TEAA < TEAG < TEAPy ≈ TEAP < TEAB. The influence of PILs on hydration behavior of peptides is explored in terms of H-bonding, cooperativity, hydrophobicity, water structural changes, ionic interactions etc.

Dielectric Relaxation and Hydration Interactions for Protic and Aprotic Ionic Liquids using Time Domain Reflectometry.

H-Bonding abilities of ionic liquids (ILs) along with hydrophobicity and cooperativity effects increases their hydration numbers making them capable for dissolving sparingly soluble organic molecules in aqueous or polar nonaqueous media, and hence ILs are potential candidates in pharmaceutical and medicinal sciences besides the different technological and academic interests. In this work, dielectric spectra were measured and analyzed for diethylammonium-based protic ionic liquids (PILs), imidazolium-based aprotic ionic liquids (APILs), and their aqueous solutions (∼0.02 to ∼0.8 mol·dm-3) over a frequency range from 0.01 to 50 GHz using time domain reflectometry at 298.15 K. The Cole-Cole (CC) model for neat ILs and a combination of the Debye and Cole-Cole (D+CC) models for their aqueous solutions best describes the experimental dielectric relaxation spectra. Higher values of static permittivity and relaxation time were observed for less viscous PILs compared to more viscous APILs due to the existence of hydrogen bonding in PILs, ionic translational motion, and the existence of transient, short-lived proton transfer responsible for solvent polarization. For aqueous solutions of ionic liquids, the fast collective relaxation of solvent (bulk water) observed at higher frequencies (∼20 GHz) and slow relaxation is detected at lower frequency (∼5 to ∼10 GHz) due to hydrophobic hydration with or without cooperative H-bonding effect. The apparent concentrations of bulk water, cbwap, and slow water, cswap, were used to obtain effective hydration numbers to understand the ion solvation. Hydration numbers revealed that imidazolium-based APILs are weakly hydrated than the diethylammonium-based PILs. Static permittivity and relaxation time of pure ILs and of aqueous solutions of studied ILs are discussed in terms of effect on alkyl chain length of cation/anion, H-bonding abilities of ions, dipole moments of ions, viscosity, hydrophobic effects, etc.

Thermodynamic studies of ionic interactions in aqueous solutions of imidazolium-based ionic liquids [Emim][Br] and [Bmim][Cl].

Experimental measurements of density at different temperatures ranging from 293.15 to 313.15 K, the speed of sound and osmotic coefficients at 298.15 K for aqueous solution of 1-ethyl-3-methylimidazolium bromide ([Emim][Br]), and osmotic coefficients at 298.15 K for aqueous solutions of 1-butyl-3-methylimidazolium chloride ([Bmim][Cl]) in the dilute concentration region are taken. The data are used to obtain compressibilities, expansivity, apparent and limiting molar properties, internal pressure, activity, and activity coefficients for [Emim][Br] in aqueous solutions. Experimental activity coefficient data are compared with that obtained from Debye-Hückel and Pitzer models. The activity data are further used to obtain the hydration number and the osmotic second virial coefficients of ionic liquids. Partial molar entropies of [Bmim][Cl] are also obtained using the free-energy and enthalpy data. The distance of the closest approach of ions is estimated using the activity data for ILs in aqueous solutions and is compared with that of X-ray data analysis in the solid phase. The measured data show that the concentration dependence for aqueous solutions of [Emim][Br] can be accounted for in terms of the hydrophobic hydration of ions and that this IL exhibits Coulombic interactions as well as hydrophobic hydration for both the cations and anions. The small hydration numbers for the studied ILs indicate that the low charge density of cations and their hydrophobic nature is responsible for the formation of the water-structure-enforced ion pairs.

Thermodynamic studies of drug-alpha-cyclodextrin interactions in water at 298.15 K: promazine hydrochloride/chlorpromazine hydrochloride + alpha-cyclodextrin + H(2)O systems.

Data on osmotic coefficients have been obtained for a binary aqueous solution of two drugs, namely, promazine hydrochloride (PZ) and chlorpromazine hydrochloride (CPZ) using a vapor pressure osmometer at 298.15 K. The observed critical micelle concentration (cmc) agrees excellently with the available literature data. The measurements are extended to aqueous ternary solutions containing fixed a concentration of alpha-cyclodextrin (alpha-CD) of 0.1 mol kg(-1) and varied concentrations (approximately 0.005-0.2 mol kg(-1)) of drugs at 298.15 K. It has been found that the cmc values increase by the addition of alpha-CD. The mean molal activity coefficients of the ions and the activity coefficient of alpha-CD in binary as well as ternary solutions were obtained, which have been further used to calculate the excess Gibbs free energies and transfer Gibbs free energies. The lowering of the activity coefficients of ions and of alpha-CD is attributed to the existence of host-guest (inclusion)-type complex equilibria. It is suggested that CPZ forms 2:1 and 1:1 complexed species with alpha-CD, while PZ forms only 1:1 complexed species. The salting constant (ks) values are determined at 298.15 K for promazine-alpha-CD and chlorpromazine-alpha-CD complexes, respectively, by following the method based on the application of the McMillan-Mayer theory of virial coefficients to transfer free energy data. It is noted that the presence of chlorine in the drug molecule imparts better complexing capacity, the effect of which gets attenuated as a result of hydrophobic interaction. The results are discussed from the point of view of associative equilibria before the cmc and complexed equilibria for binary and ternary solutions, respectively.

Thermodynamic studies of aqueous and CCl4 solutions of 15-crown-5 at 298.15 K: an application of McMillan-Mayer and Kirkwood-Buff theories of solutions.

The density and osmotic coefficient data for solutions of 15-crown-5 (15C5) in water and in CCl4 solvent systems at 298.15 K have been reported using techniques of densitometry and vapor pressure osmometry in the concentration range of 0.01-2 mol kg-1. The data are used to obtain apparent molar and partial molar volumes, activity coefficients of the components as a function of 15C5 concentration. Using the literature heat of dilution data for aqueous system, it has become possible to calculate entropy of mixing (DeltaS(mix)), excess entropy of solution (DeltaS(E)), and partial molar entropies of the components at different concentrations. The results of all these are compared to those obtained for aqueous 18-crown-6 solutions reported earlier. It has been observed that the partial molar volume of 15C5 goes through a minimum and that of water goes through a maximum at approximately 1.2 mol kg(-1) in aqueous solutions whereas the opposite is true in CCl4 medium but at approximately 0.5 mol kg(-1). The osmotic and activity coefficients of 15C5 and excess free energy change for solution exhibit distinct differences in the two solvent systems studied. These results have been explained in terms of hydrophobic hydration and interactions in aqueous solution while weak solvophobic association of 15C5 molecules in CCl4 solutions is proposed. The data are further subjected to analysis by applying McMillan-Mayer and Kirkwood-Buff theories of solutions. The analysis shows that osmotic second virial coefficient value for 15C5 is marginally less than that of 18C6 indicating that reduction in ring flexibility does not affect the energetics of the interactions much in aqueous solution while the same gets influenced much in nonpolar solvent CCl4.

Thermodynamic studies of molecular interactions in aqueous alpha-cyclodextrin solutions: application of McMillan-Mayer and Kirkwood-Buff theories.

Osmotic vapor pressure and density measurements were made for aqueous alpha-cyclodextrin (alpha-CD) solutions in the temperature range between 293.15 and 313.15 K. The experimental osmotic coefficient data were used to determine the corresponding activity coefficients and the excess Gibbs free energy of solutions. Further, the activity data obtained at different temperatures along with the enthalpies of dissolution (reported in the literature) were processed to obtain the excess enthalpy and excess entropy values for the solution process. The partial molar entropies of water and of alpha-cyclodextrin were calculated at different temperatures and also at different concentrations of alpha-CD. Using the partial molar volume data at infinite dilution, the solute-solvent cluster integrals were evaluated which yielded information about solute-solvent interactions. The application of McMillan-Mayer theory of solutions was made to obtain osmotic second and third virial coefficients which were decomposed into attractive and repulsive contributions to solute-solute interactions. The second and third osmotic virial coefficients are positive and show minimum at 303.15 K. The Kirkwood-Buff (KB) integrals G(ij), defined by the equation G(ij) = f(infinity)0 (g(ij)- 1)4pir(2) dr, have been evaluated using the experimental osmotic coefficient (and hence activity coefficient) and partial molar volume data. The limiting values of KB integrals, G(ij)(0) are compared with molecular interaction parameters (solute-solute i.e., osmotic second virial coefficient) obtained using McMillan-Mayer theory of solutions. We found an excellent agreement between the two approaches.

Thermodynamic studies of ionic hydration and interactions for amino acid ionic liquids in aqueous solutions at 298.15 K.

Amino acid ionic liquids are a special class of ionic liquids due to their unique acid-base behavior, biological significance, and applications in different fields such as templates in synthetic chemistry, stabilizers for biological macromolecules, etc. The physicochemical properties of these ionic liquids can easily be altered by making the different combinations of amino acids as anion along with possible cation modification which makes amino acid ionic liquids more suitable to understand the different kinds of molecular and ionic interactions with sufficient depth so that they can provide fruitful information for a molecular level understanding of more complicated biological processes. In this context, volumetric and osmotic coefficient measurements for aqueous solutions containing 1-ethyl-3-methylimidazolium ([Emim]) based amino acid ionic liquids of glycine, alanine, valine, leucine, and isoleucine are reported at 298.15 K. From experimental osmotic coefficient data, mean molal activity coefficients of ionic liquids were estimated and analyzed using the Debye-Hückel and Pitzer models. The hydration numbers of ionic liquids in aqueous solutions were obtained using activity data. Pitzer ion interaction parameters are estimated and compared with other electrolytes reported in the literature. The nonelectrolyte contribution to the aqueous solutions containing ionic liquids was studied by calculating the osmotic second virial coefficient through an application of the McMillan-Mayer theory of solution. It has been found that the second osmotic virial coefficient which includes volume effects correlates linearly with the Pitzer ion interaction parameter estimated independently from osmotic data as well as the hydrophobicity of ionic liquids. The enthalpy-entropy compensation effect, explained using the Starikov-Nordén model of enthalpy-entropy compensation, and partial molar entropy analysis for aqueous [Emim][Gly] solutions are made by using experimental Gibb's free energy data and literature enthalpy data. This study highlights that the hydrophobic interaction persists even in the limit of infinite dilution where the hydration effects are usually dominant, implying importance of hydrophobic hydration. Analysis of the results further shows that the hydration of amino acid ionic liquids occurs through the cooperative H-bond formation with the kosmotropic effect in contrast to the usual inorganic salts or hydrophobic salts like tetraalkylammonium halides.

Thermodynamic studies of aqueous solutions of 2,2,2-cryptand at 298.15 K: enthalpy-entropy compensation, partial entropies, and complexation with K+ ions.

The osmotic coefficient measurements for binary aqueous solutions of 2,2,2-cryptand (4,7,13,16,21,24-hexaoxa-1,10-diazabicyclo[8.8.8] hexacosane) in the concentration range of ~0.009 to ~0.24 mol·kg(-1) and in ternary aqueous solutions containing a fixed concentration of 2,2,2-cryptand of ~0.1 mol·kg(-1) with varying concentration of KBr (~0.06 to ~0.16 mol·kg(-1)) have been reported at 298.15 K. The diamine gets hydrolyzed in aqueous solutions and needs proper approach to obtain meaningful thermodynamic properties. The measured osmotic coefficient values are corrected for hydrolysis and are used to determine the solvent activity and mean ionic activity coefficients of solute as a function of concentration. Strong ion-pair formation is observed, and the ion-pair dissociation constant for the species [CrptH](+)[OH(-)] is reported. The excess and mixing thermodynamic properties (Gibbs free energy, enthalpy, and entropy changes) have been obtained using the activity data from this study and the heat data reported in the literature. Further, the data are utilized to compute the partial molal entropies of solvent and solute at finite as well as infinite dilution of 2,2,2-cryptand in water. The concentration dependent non-linear enthalpy-entropy compensation effect has been observed for the studied system, and the compensation temperature along with entropic parameter are reported. Using solute activity coefficient data in ternary solutions, the transfer Gibbs free energies for transfer of the cryptand from water to aqueous KBr as well as transfer of KBr from water to aqueous cryptand were obtained and utilized to obtain the salting constant (ks) and thermodynamic equilibrium constant (log K) values for the complex (2,2,2-cryptand:K(+)) at 298.15 K. The value of log K = 5.8 ± 0.1 obtained in this work is found to be in good agreement with that reported by Lehn and Sauvage. The standard molar entropy for complexation is also estimated for the 2,2,2-cryptand-KBr complex in aqueous medium.

Studies of enthalpy-entropy compensation, partial entropies, and Kirkwood-Buff integrals for aqueous solutions of glycine, L-leucine, and glycylglycine at 298.15 K.

Densities and osmotic coefficient measurements for dilute aqueous solutions of glycine, l-leucine, and glycylglycine have been reported at 298.15 K. The partial molar volumes and activity coefficients of solute as well as solvent have been estimated using the density and osmotic coefficient data, respectively. Excess and mixing thermodynamic properties, such as Gibbs free energy, enthalpy, and entropy changes, have been obtained using the activity data from this study and the heat data reported in the literature. The concentration enthalpy-entropy compensation effects have been observed for the studied systems, and the compensation temperatures are reported. It has been observed that the excess free energy change for all the studied systems is almost the same over the studied concentration range, showing that the differences in properties of such solutions are largely decided by the enthalpy-entropy effects. These results, along with partial entropy data, show the effects of the presence of hydrophobic interactions and water structure making effect in the case of aqueous solutions of l-leucine. The application of the Starikov-Norden enthalpy-entropy compensation model yielded information about a "hidden Carnot cycle" and the existence of multiple microphases. Application of the Kirkwood-Buff (KB) theory of solutions for the studied systems yields pair correlation functions between the components. The variation of Kirkwood-Buff integrals with concentration further signifies the concentration dependence of the hydrophobic hydration and interactions in the solution phase. The osmotic second virial coefficients have also been obtained using the KB theory and show good agreement with those obtained using the McMillan-Mayer theory of solutions. The mean square concentration fluctuations is estimated using the KB theory, which gives information about the microheterogeneity in the solution phase, which further reflects the presence of hydration and solute association.