This work describes the results of a mechanistic investigation of antibody-antigen binding using electrochemical quartz crystal microbalance (EQCM). The aim was to verify the contribution of electrolytes to conducting polypyrrole electrodes that have been modified with proteins. The behavior of an EQCM film containing various counterions was studied (chloride, dodecylsulphate and proteins) and mass changes recorded in a series of anions, cations and proteins. Results obtained indicate that the interaction of different proteins at quartz crystal electrode surface is dependent on the applied potential, the nature of the cations and anions, and the specificity of the immobilized antibody. The resonant frequency of the anti-HSA-coated quartz abruptly decreased upon contact with the antigen and this stabilized within 5 min in the concentration range between 1 and 100 ppm. The injection of other proteins such as bovine serum albumin and chymotrypsin, yielded responses that were significantly lower in magnitude than those obtained for the corresponding HSA.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Antibody-antigen interactions
- Pulsed electrochemical detection