Influence of surface charge on adsorption of fibrinogen and/or albumin on a rotating disc electrode of platinum and carbon.

The adsorption of fibrinogen on to platinum and carbon and of albumin on to carbon was investigated for various changes of the surface by recording the variations of the double-layer capacitance of the electrochemical interface during adsorption, as a function of time. The rate of the second step of the adsorption decreased with increasing negative charge on to platinum but was charge-independent on to carbon. In contrast, on both surfaces, the rate of the first step and the area of the electrode surface in close contact with adsorbed proteins were both found to increase with increasing negative charge of the surface, although at pH 7.4 albumin and fibrinogen are negatively charged. The hypothesis of ion coadsorption inside the proteic layer has been proposed to account for this result.