INTERACTION BETWEEN ADSORBED LAYERS OF LYSOZYME STUDIED WITH THE SURFACE FORCE TECHNIQUE

The surface force technique was employed to investigate the adsorption of positively charged lysozyme onto negatively charged mica surfaces in 10(-3)M NaCl at pH 5.6 at lysozyme concentrations ranging from 0.002 to 0.2 mg/mL. At equilibrium the adsorbed lysozyme nearly neutralizes the surface charge of the mica at all bulk lysozyme concentrations investigated. Prior to charge neutralization the decay length of the long-range force is consistent with the electrostatic double-layer force predicted by the DLVO theory. At low concentration, 0.002 mg/mL, a densely packed side-on oriented layer adsorbs on the mica surface. Above 0.02 mg of lysozyme/mL, a rather thick layer is adsorbed onto the surface. It consists of an inner, strongly bound layer of both side-on and end-on adsorbed proteins and an outer layer of weakly adsorbed proteins. An adhesion force is established upon contact of the adsorbed protein layers. The force measured between one lysozyme-coated surface and one bare mica surface is attractive at short separations. It was demonstrated that, at a concentration of 0.02 mg/mL, lysozyme adsorbs ''irreversibly'' with respect to dilution with 10(-3) M NaCl.