Journal of Colloid and Interface Science, Vol.304, No.1, 77-83, 2006
A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions: Applications to bovine serum albumin (BSA), lysozyme, alpha-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, alpha-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. (c) 2006 Elsevier Inc. All rights reserved.
Keywords:osmotic pressure;globular proteins;Yukawa potential;bovine serum albumin;lysozyme;alpha-chymotrypsin;IgG;equation of state