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The electrochemical oxidation of CA19-9 tagged with L-Histidine (CA199-His) was investigated for the first time with screen-printed electrodes (DS) modified with graphene oxide (DS/GO) or thermally reduced graphene oxide (DS/TRGO). Successive cyclic voltammograms (CV) measurements performed with bare and DS/TRGO electrodes proved that the intensity of the oxidation peak (I peak) is time-dependent. In fact, the oxidation signal increased over time, reached a maximum and then decreased due to the saturation of the surface with CA199-His molecules. The interaction of CA199-His with GO, TRGO, or graphite was additionally studied by isothermal calorimetry, a useful tool for accessing information regarding the biomolecule adsorption on graphene surface. The adsorption of CA199-His on TRGO was generating a higher heat, suggesting quantitative and efficient interactions. At the same time, in the case of TRGO, the saturation was not reached, indicating the existence of more free binding sites than in the case of GO and graphite. As such, the carbohydrate marker CA199-His showed a higher affinity for the TRGO surface than for the graphite or GO surfaces. The lack of saturation in the case of TRGO may indicate a continuous structural modification of the antigen when interacting with the graphene surface.

Sensing and Interaction of His-Tagged CA19-9 Antigen with Graphene-Modified Electrodes