Version 2 2022-09-01, 14:33Version 2 2022-09-01, 14:33
Version 1 2018-05-23, 12:50Version 1 2018-05-23, 12:50
journal contribution
posted on 2022-09-01, 14:33authored byEda Celikbas, Emine Guler Celik, Dilek Odaci Demirkol, Shuhei Yamada, Takeshi Endo, Suna Timur, Yusuf Yagci
A novel catechol-bearing polypeptide (CtP) was synthesized and
used as a component of electrochemical biosensor involving both enzymatic
activity and affinity-based sensing systems. Glucose oxidase (GOx)
and anti-immunoglobulin G (Anti-IgG) were selected as model biorecognition
elements for the selective analysis of glucose and IgG. Step-by-step
surface modifications were followed using various techniques such
as cyclic voltammetry (CV) and electrochemical impedance spectrometry
(EIS) as well as X-ray photoelectron spectroscopy (XPS). Additionally,
contact angles were measured in order to observe surface properties.
Amperometric measurements using the GOx biosensor were performed at
−0.7 V by following the oxygen consumption due to the enzymatic
reaction in different glucose concentrations. Affinity-based interactions
via IgG sensor were monitored using the differential pulse voltammetry
(DPV) technique. As the “surface design with CtP” approach
employed herein is generally applicable and easily adaptable to obtain
functional matrices for biomolecule immobilization, CtP-coated surfaces
can be promising platforms for the fabrication of various biobased
sensing systems.