Aggregation of non-polar solutes in water at different pressures and temperatures: The role of hydrophobic interaction

Abstract

Due to the importance of the hydrophobic interaction in protein folding, we decided to study the effect of pressure and temperature on the phase transitions of non-polar solutes in water, and thereby their solubility, using molecular dynamics simulations. The main results are: (1) within a certain range, temperature induces the aggregation of Lennard-Jones particles in water; and (2) pressure induces disaggregation of the formed clusters. From the simulated data, a non-monotonic coexistence curve for the binary system was obtained, from which a critical point of Tc = 383 ± 9 K and pc = 937 ± 11 bar was determined. The results are in accordance with previous experimental evidence involving transitions of hydrocarbons in water mixtures, and protein unfolding.