Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation.
Moderately or highly concentrated nonideal solutions of macromolecules are very important systems e.g. in biology and in many technical processes. In this work we have used the small-angle neutron scattering technique (SANS) to study the interactions and interparticle structure in solutions of human serum albumin (HSA) up to a concentration of 0.26 g/cm3 in 1.08 M NaCl. In order to obtain a model for the interactions we have combined the SANS data with results obtained by Monte Carlo simulations where we calculate the structure factor S(Q) and the pair correlation function g(r). The advantage of using the Monte Carlo method is that completely general models for the particle shape and the interactions can be considered. It is found that the SANS data can be explained by a model where the shape of the HSA molecule is approximated by an ellipsoid of revolution with semiaxes a = 6.8 nm and b = c = 1.9 nm. The interaction potential between the HSA molecules consists of two parts: (a) the molecules are hard and impenetrable and (b) the molecules are surrounded by a spherically symmetric repulsive potential which can be expressed by an empirical formula containing the HSA concentration and the centre-centre distances as the only variables.
Sjöberg
B
B
Department of Medical Biochemistry, University of Göteborg, Sweden.
Mortensen
K
K
D006801:Humans; D009010:Monte Carlo Method; D009502:Neutrons; D011487:Protein Conformation; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000737:chemistry*; D012996:Solutions
D012709:Serum Albumin; D012996:Solutions