Mr. Gero Göbel Profile

Gero Göbel

at Technische Hochschule Wildau

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Proceedings Article | 24 March 2014 Paper

Light-addressable amperometric electrodes for enzyme sensors based on direct quantum dot-electrode contacts

M. Riedel, G. Göbel, W. Parak, F. Lisdat

Proceedings Volume 8955, 89551M (2014) https://doi.org/10.1117/12.2044601

KEYWORDS: Electrodes, Sensors, Nanoparticles, Quantum dots, Glucose, Multilayers, Proteins, Biomedical optics, Current controlled current source, Particles

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Quantum dots allow the generation of charge carriers upon illumination. When these particles are attached to an electrode a photocurrent can be generated. This allows their use as a light-switchable layer on the surface. The QDs can not only exchange electronics with the electrode, but can also interact with donor or acceptor compounds in solution providing access to the construction of signal chains starting from an analytic molecule. The magnitude and the direction of the photocurrent depend on several factors such as electrode polarization, solution pH and composition. These defined dependencies have been evaluated with respect to the combination of QD-electrodes with enzyme reactions for sensorial purpose. CdSe/ZnS-QD-modified electrodes can be used to follow enzymatic reactions in solution based on the oxygen sensitivity. In order to develop a photoelectrochemical biosensor, e.g. glucose oxidase is immobilized on the CdSe/ZnS-electrode. One immobilization strategy applies the layer-by-layer-technique of GOD and a polyelectrolyte. Photocurrent measurements of such a sensor show a clear concentration dependent behavior. The principle of combing QD oxidase. The sensitivity of quantum dot electrodes can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be demonstrated that direct electron transfer from excited quantum dots can be achieved with the redox protein cytochrome c. This allows the detection of the protein, but also interaction partners such as a enzymes or superoxide.

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