@inproceedings{WeldenSeverinsPoghossianetal.2022,
  author    = {Welden, Melanie and Severins, Robin and Poghossian, Arshak and Wege, Christina and Siegert, Petra and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Studying the immobilization of acetoin reductase with Tobacco mosaic virus particles on capacitive field-effect sensors},
  series = {2022 IEEE International Symposium on Olfaction and Electronic Nose (ISOEN)},
  booktitle = {2022 IEEE International Symposium on Olfaction and Electronic Nose (ISOEN)},
  publisher = {IEEE},
  isbn      = {978-1-6654-5860-3 (Online)},
  doi       = {10.1109/ISOEN54820.2022.9789657},
  pages     = {4 Seiten},
  year      = {2022},
  abstract  = {A capacitive electrolyte-insulator-semiconductor (EISCAP) biosensor modified with Tobacco mosaic virus (TMV) particles for the detection of acetoin is presented. The enzyme acetoin reductase (AR) was immobilized on the surface of the EISCAP using TMV particles as nanoscaffolds. The study focused on the optimization of the TMV-assisted AR immobilization on the Ta 2 O 5 -gate EISCAP surface. The TMV-assisted acetoin EISCAPs were electrochemically characterized by means of leakage-current, capacitance-voltage, and constant-capacitance measurements. The TMV-modified transducer surface was studied via scanning electron microscopy.},
  language  = {en}
}
@article{WeldenPoghossianVahidpouretal.2022,
  author    = {Welden, Melanie and Poghossian, Arshak and Vahidpour, Farnoosh and Wendlandt, Tim and Keusgen, Michael and Wege, Christina and Sch{\"o}ning, Michael Josef},
  title     = {Towards multi-analyte detection with field-effect capacitors modified with tobacco mosaic virus bioparticles as enzyme nanocarriers},
  series = {Biosensors},
  volume    = {12},
  journal   = {Biosensors},
  number    = {1},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios12010043},
  pages     = {Artikel 43},
  year      = {2022},
  abstract  = {Utilizing an appropriate enzyme immobilization strategy is crucial for designing enzyme-based biosensors. Plant virus-like particles represent ideal nanoscaffolds for an extremely dense and precise immobilization of enzymes, due to their regular shape, high surface-to-volume ratio and high density of surface binding sites. In the present work, tobacco mosaic virus (TMV) particles were applied for the co-immobilization of penicillinase and urease onto the gate surface of a field-effect electrolyte-insulator-semiconductor capacitor (EISCAP) with a p-Si-SiO₂-Ta₂O₅ layer structure for the sequential detection of penicillin and urea. The TMV-assisted bi-enzyme EISCAP biosensor exhibited a high urea and penicillin sensitivity of 54 and 85 mV/dec, respectively, in the concentration range of 0.1-3 mM. For comparison, the characteristics of single-enzyme EISCAP biosensors modified with TMV particles immobilized with either penicillinase or urease were also investigated. The surface morphology of the TMV-modified Ta₂O₅-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an XOR (Exclusive OR) enzyme logic gate.},
  language  = {en}
}
@article{PoghossianKarschuckWagneretal.2022,
  author    = {Poghossian, Arshak and Karschuck, Tobias and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Field-Effect Capacitors Decorated with Ligand-Stabilized Gold Nanoparticles: Modeling and Experiments},
  series = {Biosensors},
  volume    = {12},
  journal   = {Biosensors},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios12050334},
  pages     = {Artikel 334},
  year      = {2022},
  abstract  = {Nanoparticles are recognized as highly attractive tunable materials for designing field-effect biosensors with enhanced performance. In this work, we present a theoretical model for electrolyte-insulator-semiconductor capacitors (EISCAP) decorated with ligand-stabilized charged gold nanoparticles. The charged AuNPs are taken into account as additional, nanometer-sized local gates. The capacitance-voltage (C-V) curves and constant-capacitance (ConCap) signals of the AuNP-decorated EISCAPs have been simulated. The impact of the AuNP coverage on the shift of the C-V curves and the ConCap signals was also studied experimentally on Al-p-Si-SiO₂ EISCAPs decorated with positively charged aminooctanethiol-capped AuNPs. In addition, the surface of the EISCAPs, modified with AuNPs, was characterized by scanning electron microscopy for different immobilization times of the nanoparticles.},
  language  = {en}
}
@article{WendlandtKochBritzetal.2023,
  author    = {Wendlandt, Tim and Koch, Claudia and Britz, Beate and Liedek, Anke and Schmidt, Nora and Werner, Stefan and Gleba, Yuri and Vahidpour, Farnoosh and Welden, Melanie and Poghossian, Arshak and Sch{\"o}ning, Michael Josef},
  title     = {Facile Purification and Use of Tobamoviral Nanocarriers for Antibody-Mediated Display of a Two-Enzyme System},
  series = {Viruses},
  volume    = {9},
  journal   = {Viruses},
  number    = {15},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1999-4915},
  doi       = {doi.org/10.3390/v15091951},
  pages     = {Artikel 1951},
  year      = {2023},
  abstract  = {Immunosorbent turnip vein clearing virus (TVCV) particles displaying the IgG-binding domains D and E of Staphylococcus aureus protein A (PA) on every coat protein (CP) subunit (TVCVPA) were purified from plants via optimized and new protocols. The latter used polyethylene glycol (PEG) raw precipitates, from which virions were selectively re-solubilized in reverse PEG concentration gradients. This procedure improved the integrity of both TVCVPA and the wild-type subgroup 3 tobamovirus. TVCVPA could be loaded with more than 500 IgGs per virion, which mediated the immunocapture of fluorescent dyes, GFP, and active enzymes. Bi-enzyme ensembles of cooperating glucose oxidase and horseradish peroxidase were tethered together on the TVCVPA carriers via a single antibody type, with one enzyme conjugated chemically to its Fc region, and the other one bound as a target, yielding synthetic multi-enzyme complexes. In microtiter plates, the TVCVPA-displayed sugar-sensing system possessed a considerably increased reusability upon repeated testing, compared to the IgG-bound enzyme pair in the absence of the virus. A high coverage of the viral adapters was also achieved on Ta2O5 sensor chip surfaces coated with a polyelectrolyte interlayer, as a prerequisite for durable TVCVPA-assisted electrochemical biosensing via modularly IgG-assembled sensor enzymes.},
  language  = {en}
}
@article{KarschuckPoghossianSeretal.2024,
  author    = {Karschuck, Tobias and Poghossian, Arshak and Ser, Joey and Tsokolakyan, Astghik and Achtsnicht, Stefan and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Capacitive model of enzyme-modified field-effect biosensors: Impact of enzyme coverage},
  series = {Sensors and Actuators B: Chemical},
  volume    = {408},
  journal   = {Sensors and Actuators B: Chemical},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0925-4005 (Print)},
  doi       = {10.1016/j.snb.2024.135530},
  pages     = {12 Seiten},
  year      = {2024},
  abstract  = {Electrolyte-insulator-semiconductor capacitors (EISCAP) belong to field-effect sensors having an attractive transducer architecture for constructing various biochemical sensors. In this study, a capacitive model of enzyme-modified EISCAPs has been developed and the impact of the surface coverage of immobilized enzymes on its capacitance-voltage and constant-capacitance characteristics was studied theoretically and experimentally. The used multicell arrangement enables a multiplexed electrochemical characterization of up to sixteen EISCAPs. Different enzyme coverages have been achieved by means of parallel electrical connection of bare and enzyme-covered single EISCAPs in diverse combinations. As predicted by the model, with increasing the enzyme coverage, both the shift of capacitance-voltage curves and the amplitude of the constant-capacitance signal increase, resulting in an enhancement of analyte sensitivity of the EISCAP biosensor. In addition, the capability of the multicell arrangement with multi-enzyme covered EISCAPs for sequentially detecting multianalytes (penicillin and urea) utilizing the enzymes penicillinase and urease has been experimentally demonstrated and discussed.},
  language  = {en}
}