Abstract
The adsorption behavior of serum albumin onto the surface of platinum, gold, and glassy carbon electrodes was studied in relation to the electrode potential, by using cyclic volutammetry and a quartz-crystal microbalance. The kinetics of adsorption was significantly dependent on the electrode potential. The adsorption was highly accelerated by the application of positive potential to the electrode, suggesting an electrostatic interaction between the negatively charged alumin molecules and the positively polarized electrode as the origin of the accelerated adsorption. The adsorption of albumin on the electrodes was irreversible with respect to dilution of the albumin solution, while the albumin molecules were desorbed in part upon shifting the electrode potential in the negative direction. The quartz-crystal microbalance data showed that alumin forms a monomolecular layer on the electrode surface. Protein adsorption on electrode surface in serum was also examined.
