We present a study of the interaction of the positively charged model protein lysozyme with the negatively charged amphiphilic diblock polyelectrolyte micelles of poly(tert-butylstyrene)-bsodium (sulfamate/carboxylate)isoprene) (PtBS-b-SCPI) on the surface of silver. The adsorption kinetics are monitored by surface plasmon resonance and the surface morphology by atomic force microscopy. The micellar adsorption kinetics is dictated by two processes and the micellar layer morphology shows that the micelles do not lose their integrity upon adsorption. The complexation of lysozyme with the adsorbed micellar layers depends on the micelles arrangement and density in the underlying layer and lysozyme follows the local morphology of the underlying roughness. When the micellar adsorbed amount is small, the layers show low capacity in protein binding and low resistance in loading. When the micellar adsorbed amount is high the situation is inversed. The adsorbed layers both with or without added protein are found to be irreversibly adsorbed on the Ag surface.
