| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 602680 | Colloids and Surfaces B: Biointerfaces | 2007 | 7 Pages |
Formation of protein-polyelectrolyte complexes (PPCs) between bovine serum albumin (BSA) and potassium poly (vinyl alcohol) sulfate (KPVS) was studied at pH 3 as a function of ionic strength. Turbidimetric titration was employed by a combination of dynamic light scattering (DLS) and electrophoretic light scattering (ELS). The formal charge (ZPPC) of the resulting PPCs at different ionic strengths were estimated from ELS data by assuming the free draining and the non-free draining model. The radius of a BSA molecule in the complex was used in the former model for calculation of ZPPC with the Henry's equation, while in the latter case the hydrodynamic radius of a PPC particle determined from DLS was employed. The results obtained were compared with the ZPPC values calculated using a relation of ZPPC=nbZBSA+αZKPVSZPPC=nbZBSA+αZKPVS, where ZBSA (≥0) and ZKPVS (≤0) denote the formal charge of BSA and KPVS, respectively. Moreover, nb is the number of bound proteins per complex composed of α polymer chains. It was suggested that the PPC between BSA and KPVS behaves as a free draining molecule during the electrophoresis, at least at a high ionic strength. Also suggested is that the PPC formation at low ionic strength follows a 1:1 stoichiometry in the charge neutralization.
