Solvation behavior of some amino acids in aqueous solutions of non-steroidal anti-inflammatory drug sodium ibuprofen at different temperatures analysed by volumetric and acoustic methods

• Apparent molar properties of amino acids in aqueous solutions of sodium ibuprofen.
• Volume and compression data suggest dominance of hydrophilic–hydrophilic interactions in amino acids–drug mixtures.
• Hydration number and group contribution have been determined.
• Positive values of pair interaction coefficients predict pairwise interaction.

Apparent molar volume (V∅)(V∅), apparent molar isentropic compression (K∅,s)(K∅,s) of glycine, l-alanine and l-valine in binary aqueous solutions of (0.05, 0.15, 0.25 and 0.35) mol·kg−1 sodium ibuprofen (Na-IBP) have been determined at temperatures (288.15, 293.15, 298.15, 303.15 and 308.15) K from density and ultrasonic speed measurements. Apparent molar volume at infinite dilution V∅0, apparent molar isentropic compression at infinite dilution K∅,s0 and the experimental slopes (SV(SV and SK)SK) were obtained from Masson’s equation. These values are used for calculating the number of water molecules hydrated (nH)(nH) to the amino acids. The structure-making/breaking ability of solutes was discussed using Hepler’s Criterion. Transfer parameters (ΔV∅0) and Δ(K∅,s0) at infinite dilution from aqueous to aqueous Na-IBP solutions have been calculated and were interpreted in terms of hydrophilic–hydrophilic, hydrophilic–hydrophobic and hydrophobic–hydrophobic interactions on the basis of co-sphere overlap model. The linear correction of V∅0 for a homologous series of amino acids has been utilized to calculate to contribution of the charged end groups (NH3+,COO-), (CH2)(CH2) groups, and the other alkyl chain of the amino acids to V∅0. The pair and triplet interaction coefficients have also been calculated from both the properties. The volume and compression data suggest that hydrophilic–hydrophilic interactions are predominant in these systems. It is inferred that the effect of Na-IBP on protein stability need not be necessarily due to preferential hydration, it can also interact with the hydrophilic groups of the constituents of proteins affecting its stability.