4.6 Article

Field-Effect Transistor with a Plasmonic Fiber Optic Gate Electrode as a Multivariable Biosensor Device

期刊

ACS SENSORS
卷 7, 期 2, 页码 504-512

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acssensors.1c02313

关键词

electrolyte-gated field-effect transistor (EG-FET); surface plasmon resonance (SPR); layer-by-layer (LBL) assemblies; surface investigation; multivariant sensing; fiber optics; sensor geometry

资金

  1. European Union [813863]
  2. Austrian Research Promotion Agency (FFG) [870025, 873541]
  3. Marie Curie Actions (MSCA) [813863] Funding Source: Marie Curie Actions (MSCA)

向作者/读者索取更多资源

A novel multivariable system that combines a transistor with fiber optic-based surface plasmon resonance spectroscopy has been developed. The system allows for discrimination of mass and charge contributions for binding assays on the same sensor surface. The sensor geometry has been optimized and the reversibility of plasmon resonance wavelength shifts has been demonstrated. The system was successfully tested with a layer-by-layer assembly of polyelectrolytes and a thrombin binding assay.
A novel multivariable system, combining a transistor with fiber optic-based surface plasmon resonance spectroscopy with the gate electrode simultaneously acting as the fiber optic sensor surface, is reported. The dual-mode sensor allows for discrimination of mass and charge contributions for binding assays on the same sensor surface. Furthermore, we optimize the sensor geometry by investigating the influence of the fiber area to transistor channel area ratio and distance. We show that larger fiber optic tip diameters are favorable for electronic and optical signals and demonstrate the reversibility of plasmon resonance wavelength shifts after electric field application. As a proof of principle, a layer-by-layer assembly of polyelectrolytes is performed to benchmark the system against multivariable sensing platforms with planar surface plasmon resonance configurations. Furthermore, the biosensing performance is assessed using a thrombin binding assay with surface-immobilized aptamers as receptors, allowing for the detection of medically relevant thrombin concentrations.

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