A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions: Applications to bovine serum albumin (BSA), lysozyme, α-chymotrypsin, and immuno-gamma-globulins (IgG) solutions

To investigate globular protein–protein and protein–salt interactions in electrolyte solutions, a potential of mean force including hard-core repulsion, van der Waals attraction and electric double layer repulsion is proposed in this work. Both van der Waals attraction and double-layer repulsion are represented using hard spheres with two-Yukawa tails. The explicit analytical solution of osmotic pressure is derived from the first-order mean spherical approximation. From the comparison between the calculated and experimental values of osmotic pressures for aqueous bovine serum albumin (BSA), lysozyme, α-chymotrypsin, and immuno-gamma-globulins (IgG) solutions, we found that the proposed model is adequate for the description of the interactions between proteins at low ionic strength and small self-association of protein molecules. At high ionic strength, the charge inversions of protein molecules should be taken into account.

The hard-core two-Yukawa model is able to accurately describe the osmotic pressure of aqueous globular protein solutions as functions of protein concentration, pH, and ionic strength in the case of no self-association.Figure optionsDownload as PowerPoint slide