Abstract
A simple and sensitive biosensor was developed for the determination of human immunoglobulin G (IgG). Protein A was employed as molecular receptor and electrochemical impedance spectroscopy (EIS) was used as detection technique. The biosensor was obtained by self-assembling protein A on a gold electrode. The surface morphology of the self-assembled layer before and after interaction with IgG was studied by atomic force microscopy. Protein A bound specifically to the Fc portion of IgG, and this caused a change in the resistance of the interfacial electron transfer when using a ferrocyanide redox couple as a probe. The increase of the resistance of the electron transfer was linearly related to the concentration of IgG in the range from 10 ng.mL−1 to 1.0 μg.mL−1, with a detection limit of 5 ng.mL−1. The work demonstrates that protein A is a versatile matrix for the immobilization of antibodies.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
