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Ethanol is a common protein crystallization agent, precipitant, anddenaturant, but also alters the dielectric properties of solutions. Whileethanol-induced unfolding is largely ascribed to its hydrophobic parts, itseffect on protein phase separation and inter-protein interactions remainspoorly understood. Here, the effects of ethanol and NaCl on the phase behaviorand interactions of protein solutions are studied in terms of the metastableliquid-liquid phase separation (LLPS) and the second virial coefficient $B_2$using lysozyme solutions. Determination of the phase diagrams shows that thecloud-point temperatures are reduced and raised by the addition of ethanol andsalt, respectively. The observed trends can be explained using the extended lawof corresponding states as changes of $B_2$. The results for $B_2$ agreequantitatively with those of static light scattering and small-angle X-rayscattering experiments. Furthermore, $B_2$ values calculated based oninter-protein interactions described by the Derjaguin--Landau--Verwey--Overbeek(DLVO) potential and considering the dielectric solution properties andelectrostatic screening due to the ethanol and salt content quantitativelyagree with the experimentally observed $B_2$ values.

physical chemistry chemical physics/pccp. physical chemistry chemical physics

Interactions in protein solutions close to liquid-liquid phase  separation: Ethanol reduces attractions via changes of the dielectric  solution properties