Daniela Buzatu

Protein Diffusiophoresis and Salt Osmotic Diffusion in Aqueous Solutions

Diffusion of a solute can be induced by the concentration gradient of another solute in solution. This transport mechanism is known as cross-diffusion. We have investigated cross-diffusion in a ternary protein-salt-water system. Specifically, we measured the two cross-diffusion coefficients for the lysozyme-NaCl-water system at 25 °C and pH 4.5 as a function of protein and salt concentrations by Rayleigh interferometry. One cross-diffusion coefficient characterizes salt osmotic diffusion induced by a protein concentration gradient, and is related to protein-salt thermodynamic interactions as described by the theories of Donnan membrane equilibrium and protein preferential hydration. The other cross-diffusion coefficient characterizes protein diffusiophoresis induced by a salt concentration gradient, and is described as the difference between a preferential-interaction coefficient and a transport parameter. We first relate our experimental results to the protein net charge and the thermodynamic excess of water near the protein surface. We then extract the Stefan-Maxwell diffusion coefficient describing protein-salt interactions in water. We find that the value of this coefficient is negative, contrary to the friction interpretation of Stefan-Maxwell equations. This result is explained by considering protein hydration. Finally, protein diffusiophoresis is quantitatively examined by considering electrophoretic and hydration effects on protein migration and utilized to accurately estimate lysozyme electrophoretic mobility. To our knowledge, this is the first time that protein diffusiophoresis has been experimentally characterized and a protein-salt Stefan-Maxwell diffusion coefficient reported. This work represents a significant contribution for understanding and modeling the effect of concentration gradients in protein-salt aqueous systems relevant to diffusion-based mass-transfer technologies and transport in living systems.

Spinodal Curve of a Model Ternary Solution

We consider a lattice model for ternary solutions in which the lattice bonds are covered by molecules of types AA, BB, and AB, and the only interactions are between the molecular ends of a common lattice site. Using its equivalence with the standard Ising model for magnets, we derive the spinodal curve of the three-component model on the honeycomb lattice in the mean-field and Bethe-lattice approximations. The spinodal and the coexistence curves of the ternary solution are drawn at different values of the reduced temperature, the only parameter of the model. The particular case of a binary solution is also illustrated.

Amphiphile-rich phase in a model ternary solution on the honeycomb lattice

A model three-component system is considered in which the bonds of a honeycomb lattice are covered by bifunctional molecules of types AA, BB, and AB. The AB type molecule represents an amphiphile. An accurate approximation to the boundary in temperature-composition space of an ordered amphiphile-rich phase is calculated by transforming an accurate closed-form approximation of the critical frontier of an antiferromagnetic phase in an equivalent Ising model. This Ising model has coupling constants and a magnetic field that are temperature dependent.