Electrochemical studies of the adsorption behavior of bovine serum albuminon stainless steel

Citation
S. Omanovic et Sg. Roscoe, Electrochemical studies of the adsorption behavior of bovine serum albuminon stainless steel, LANGMUIR, 15(23), 1999, pp. 8315-8321
Citations number
52
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
LANGMUIR
ISSN journal
07437463 → ACNP
Volume
15
Issue
23
Year of publication
1999
Pages
8315 - 8321
Database
ISI
SICI code
0743-7463(19991109)15:23<8315:ESOTAB>2.0.ZU;2-Q
Abstract
The adsorption behavior of bovine serum albumin (BSA) on high-purity austen itic levy-carbon stainless steel and its effect on the state of the electro de surface have been studied over the temperature range 299-343 K under ope n-circuit-potential conditions, using electrochemical impedance spectroscop y (EIS). The impedance spectra were interpreted in terms of an equivalent e lectrical circuit (EEC) based on a possible physical model with the circuit elements representing the electrochemical properties of the investigated s ystem. The adsorption of BSA onto the stainless steel surface resulted in a n increased rate of metal dissolution, i.e., corrosion. The plateau values of corrosion rate were achieved after a "threshold" BSA concentration in th e bulk solution at all the temperatures studied. The rate of the corrosion process was found to be controlled by both the surface diffusion and charge transfer process. Adsorption of BSA onto the stainless steel sur face was described with a Langmuir adsorption isotherm. The thermodynamic data were calculated to give the corrosion activation energy, Gibbs free energy, enth alpy, and entropy of adsorption. The data suggested a very strong adsorptio n of BSA molecules, accompanied by a charge transfer mechanism involving ch emisorption. An adsorption mechanism was proposed involving the interaction of the negatively charged carboxylate groups of the proteins with the stai nless steel surface. The EIS technique was shown to be a valuable tool in s tudying the interfacial behavior of proteins at metal electrode surfaces.