@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{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}
}