Phase transitions in polar binary mixtures can be drastically altered by even a small amount of salt. This is because the preferential solvation strongly depends on the ambient composition. Together with a summary of our research on this problem, we present some detailed results on the role of antagonistic salt composed of hydrophilic and hydrophobic ions. These ions tend to segregate at liquid...

We address the response of a random heteropolymer to preferential solvation of certain monomer types at the globule-solvent interface. For each set of monomers that can comprise the molecule's surface, we represent the ensemble of allowed configurations by a Gaussian distribution of energy levels, whose mean and variance depend on the set's composition. Within such a random energy model, mean s...

We develop a self-consistent field theory for salt-doped diblock copolymers, such as polyethylene oxide (PEO)–polystyrene with added lithium salts. We account for the inhomogeneous distribution of Li ions bound to the ion-dissolving block, the preferential solvation energy of anions in the different block domains, the translational entropy of anions, the ion-pair equilibrium between polymer-bou...

Imidazolium-based chloride ionic liquids (ILs) have exhibited remarkable performance in several important applications such as biomass dissolution and extraction, but their large viscosity is a non-negligible problem. Adding molecular co-solvents into chloride ILs is effective in reducing viscosity; nevertheless, understanding of the accompanied change of thermodynamic polarity is quite few. Th...

Dynamic equations are presented for polar binary mixtures containing ions in the presence of preferential solvation. In one-phase states, we calculate the dynamic structure factor of the composition accounting for ion motion. Microphase separation can take place for sufficiently large solvation asymmetry of the cations and the anions. We show two-dimensional simulation results of the mesophase ...

Although the nature of solvent-protein interactions is generally weak and non-specific, addition of cosolvents such as denaturants and osmolytes strengthens protein-protein interactions for some proteins, whereas it weakens protein-protein interactions for others. This is exemplified by the puzzling observation that addition of glycerol oppositely affects the association constants of two antibo...