Role of preferential hydration on diffusiophoresis of globular proteins

•Diffusiophoresis is the migration of a macromolecule caused by a cosolute gradient.•Preferential hydration is the thermodynamic excess of water molecules near protein surface.•A hydrodynamic model describing how preferential hydration drives diffusiophoresis of globular particles is developed.•Experimental data on lysozyme diffusiophoresis indicate that mean-force potential describing preferential hydration is weak compared to thermal energy and interaction range is an appreciable fraction of protein size. Diffusiophoresis is the migration of a colloidal particle through a fluid, caused by a cosolute concentration gradient. Preferential hydration is a thermodynamic phenomenon responsible for particle diffusiophoresis from high to low cosolute concentration in water. Here, steady-state Navier-Stokes equation for incompressible fluids, with particle modeled as an inpenetrable rigid sphere, is employed for deriving a mathematical expression of the diffusiophoresis coefficient. Mean-force potentials with arbitrary interaction range but with interaction energies small or comparable with thermal energy are employed to describe water-mediated particle-cosolute interactions. This choice of potential is movitated by previous work showing that only fluid particles weakly interacting with the colloildal particle can cause diffusiophoresis. Preferential hydration has been extensively investigated for proteins. Thus, the proposed model is applied to available experimental diffusiophoresis coefficients of lysozyme in aqueous NaCl and KCl at pH 4.5 and 25 °C. This analysis also includes data on salt osmotic diffusion, describing salt diffusion caused by protein concentration gradients. The preferential-hydration contribution of experimental lysozyme diffusiophoresis is obtained after removing electrophoretic diffusiophoresis. Examination of these experimental data shows that the mean-force potential describing preferential hydration is indeed weak, with an interaction range that is an appreciable fraction of particle size. [Display omitted]