Long-time and short-time investigation of the electrode interface through electrochemical impedance measurements. Application to adsorption of human serum albumin onto glassy carbon rotating disc electrode

Changes in biphasic electrode impedance with protein adsorption and cell growth

“…There was little change in V a , indicating that protein cover had an insignificant effect on R a . The effect of protein on the polarisation and capacitive elements of the waveform was consistent with previous electrochemical studies (Wegener et al 1996; de Ficquelmont-Loizos et al 1997; Franks et al 2005). Franks et al (2005) showed coatings of laminin and poly-L-lysine on platinum electrodes resulted in a reduction of the capacitance measure, thereby increasing overall electrode impedance.…”

“…Franks et al (2005) showed coatings of laminin and poly-L-lysine on platinum electrodes resulted in a reduction of the capacitance measure, thereby increasing overall electrode impedance. Human serum albumin was also shown to increase impedance on glassy carbon electrodes, with capacitance increasing to a plateau approximately 20 minutes after the addition of protein (de Ficquelmont-Loizos et al 1997). Importantly, the biphasic impedance changes brought about by protein adsorption on the gold electrodes behaved similarly to that seen using other electrochemical impedance measurement techniques.…”

Electrochemical behavior of human serum albumin–TiO2 nanocrystalline electrodes studied as a function of pH. Part 2: Presence of redox couple in solution

“…Considering the FeðCNÞ 3À=4À 6 redox couple D value informed by Ficquelmont-Loízos and colleagues [9] and using a s D of 17.2 ms obtained from the experimental data fitting, a value of d = 3.9 lm was obtained. This value corresponds to the diffusion layer thickness of the FeðCNÞ 3À=4À 6 redox couple species, which is expected to be thinner than that corresponding to the HSA protein molecule.…”

“…Adsorption studies of macromolecules of biological interest on different solid surfaces were carried out using EIS experiments [2][3][4][5][6][7][8][9][10][11][12][13][14][15]. Several studies were performed using the external redox couple FeðCNÞ 3À=4À 6 to monitor the modifications in the electron charge transfer induced by the macromolecule adsorption [5,[9][10][11][12][13][14].…”

“…Several studies were performed using the external redox couple FeðCNÞ 3À=4À 6 to monitor the modifications in the electron charge transfer induced by the macromolecule adsorption [5,[9][10][11][12][13][14]. These studies have shown a strong dependence of the charge transfer process with the adsorption on the surface of different protein layers.…”