Electrostatic complexation of a double hydrophilic block polyelectrolyte and proteins of different molecular shape

The electrostatic complexation between the polyelectrolyte block of the novel double hydrophilic copolymer quaternized poly(3,5-bis(dimethylaminomethylene) hydroxystyrene)-b-poly(ethylene oxide) (QNPHOS-PEO) and proteins of different molecular shape, that is globular bovine serum albumin (BSA) or rod-like bovine fibrinogen (FBG), is investigated by means of dynamic, static, and electrophoretic light scattering, as well as analytical ultracentrifugation measurements. The solution behavior, structure, and properties of the formed complexes at pH 7 and 0.01 M ionic strength, as a function of the protein concentration in the solution (or equivalently the charge ratio of the two components), depend on the protein concentration and molecular characteristics. Moreover, the structure of the complexes is greatly influenced by the intrinsic structure of the block polyelectrolyte, which forms rather loose multichain aggregates, due to hydrophobic interactions. A direct correlation between the stability of the preformed complexes against the increase of the solution ionic strength and their structure is established. Finally, the spectroscopic structural investigation of both complexed proteins reveals no signs of protein denaturation upon complexation. © 2016 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2016, 54, 1515–1529