Effects of salt or cosolvent addition on solubility of a hydrophobic solute in water: Relevance to those on thermal stability of a protein.
The solubility of a nonpolar solute in water is changed upon addition of a salt or cosolvent. Hereafter, "solvent" is formed by water molecules for pure water, by water molecules, cations, and anions for water-salt solution, and by water and cosolvent molecules for water-cosolvent solution. Decrease and increase in the solubility, respectively, are ascribed to enhancement and reduction of the hydrophobic effect. Plenty of experimental data are available for the change in solubility of argon or methane arising from the addition. We show that the integral equation theory combined with a rigid-body model, in which the solute and solvent particles are modeled as hard spheres with different diameters, can reproduce the data for the following items: salting out by an alkali halide and salting in by tetramethylammonium bromide, increase in solubility by a monohydric alcohol, and decrease in solubility by sucrose or urea. The orders of cation or anion species in terms of the power of decreasing the solubility can also be reproduced for alkali halides. With the rigid-body model, the analyses are focused on the roles of entropy originating from the translational displacement of solvent particles. It is argued by decomposing the solvation entropy of a nonpolar solute into physically insightful constituents that the solvent crowding in the bulk is a pivotal factor of the hydrophobic effect: When the solvent crowding in the bulk becomes more serious, the effect is strengthened, and when it becomes less serious, the effect is weakened. It is experimentally known that the thermal stability of a protein is also influenced by the salt or cosolvent addition. The additions which decrease and increase the solubility of a nonpolar solute, respectively, usually enhance and lower the thermal stability. This suggests that the enhanced or reduced hydrophobic effect is also a principal factor governing the stability change. However, urea decreases the solubility but lowers the stability. Bromide and iodide ions decrease the solubility but lower the stability of a protein with a large, positive total charge. In these cases, the urea- or ion-protein van der Waals interaction energy as well as the hydrophobic effect needs to be taken into account in arguing the stability change. We also present a new view on the so-called Hofmeister series: We show how it is expressed when the change in hydrophobic effect dominates and how it is modified when other factors are also influential.
Graduate School of Energy Science, Kyoto University, Uji, Kyoto 611-0011, Japan.
Shota
0000000288940050
S
Murakami
Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan.
Tomohiko
T
Hayashi
Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan.
Masahiro
000000018060045X
M
Kinoshita
D001128:Argon / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008697:Methane / Q000737:chemistry; D008956:Models, Chemical; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*; D000644:Quaternary Ammonium Compounds / Q000737:chemistry; D012492:Salts / Q000737:chemistry*; D012995:Solubility; D012997:Solvents / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics; D014508:Urea / Q000737:chemistry; D014867:Water / Q000737:chemistry*
D011506:Proteins; D000644:Quaternary Ammonium Compounds; D012492:Salts; D012997:Solvents; D014867:Water; D001128:Argon; D014508:Urea; C027917:tetramethylammonium; D008697:Methane