TY - CHAP A1 - Welden, Melanie A1 - Severins, Robin A1 - Poghossian, Arshak A1 - Wege, Christina A1 - Siegert, Petra A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Studying the immobilization of acetoin reductase with Tobacco mosaic virus particles on capacitive field-effect sensors T2 - 2022 IEEE International Symposium on Olfaction and Electronic Nose (ISOEN) N2 - 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. KW - Tobacco mosaic virus KW - acetoin KW - capacitive field-effect biosensor KW - enzyme immobilization Y1 - 2022 SN - 978-1-6654-5860-3 (Online) SN - 978-1-6654-5861-0 (Print) U6 - http://dx.doi.org/10.1109/ISOEN54820.2022.9789657 N1 - IEEE International Symposium on Olfaction and Electronic Nose (ISOEN), 29 May 2022 - 01 June 2022, Aveiro, Portugal. PB - IEEE ER - TY - JOUR A1 - Molinnus, Denise A1 - Iken, Heiko A1 - Johnen, Anna Lynn A1 - Richstein, Benjamin A1 - Hellmich, Lena A1 - Poghossian, Arshak A1 - Knoch, Joachim A1 - Schöning, Michael Josef T1 - Miniaturized pH-Sensitive Field-Effect Capacitors with Ultrathin Ta₂O₅ Films Prepared by Atomic Layer Deposition JF - physica status solidi (a) applications and materials science N2 - Miniaturized electrolyte–insulator–semiconductor capacitors (EISCAPs) with ultrathin gate insulators have been studied in terms of their pH-sensitive sensor characteristics: three different EISCAP systems consisting of Al–p-Si–Ta2O5(5 nm), Al–p-Si–Si3N4(1 or 2 nm)–Ta2O5 (5 nm), and Al–p-Si–SiO2(3.6 nm)–Ta2O5(5 nm) layer structures are characterized in buffer solution with different pH values by means of capacitance–voltage and constant capacitance method. The SiO2 and Si3N4 gate insulators are deposited by rapid thermal oxidation and rapid thermal nitridation, respectively, whereas the Ta2O5 film is prepared by atomic layer deposition. All EISCAP systems have a clear pH response, favoring the stacked gate insulators SiO2–Ta2O5 when considering the overall sensor characteristics, while the Si3N4(1 nm)–Ta2O5 stack delivers the largest accumulation capacitance (due to the lower equivalent oxide thickness) and a higher steepness in the slope of the capacitance–voltage curve among the studied stacked gate insulator systems. KW - atomic layer deposition KW - capacitive field-effect sensors KW - pH sensors KW - ultrathin gate insulators Y1 - 2022 U6 - http://dx.doi.org/10.1002/pssa.202100660 SN - 1862-6319 VL - 219 IS - 8 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Wendlandt, Tim A1 - Koch, Claudia A1 - Britz, Beate A1 - Liedek, Anke A1 - Schmidt, Nora A1 - Werner, Stefan A1 - Gleba, Yuri A1 - Vahidpour, Farnoosh A1 - Welden, Melanie A1 - Poghossian, Arshak A1 - Schöning, Michael Josef T1 - Facile Purification and Use of Tobamoviral Nanocarriers for Antibody-Mediated Display of a Two-Enzyme System JF - Viruses N2 - 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. KW - biosensor KW - horseradish peroxidase (HRP) KW - glucose oxidase (GOx) KW - enzyme cascade KW - turnip vein clearing virus (TVCV) KW - tobacco mosaic virus (TMV) Y1 - 2023 U6 - http://dx.doi.org/doi.org/10.3390/v15091951 SN - 1999-4915 N1 - This article belongs to the Special Issue "Tobamoviruses 2023" VL - 9 IS - 15 PB - MDPI CY - Basel ER - TY - JOUR A1 - Karschuck, Tobias A1 - Schmidt, Stefan A1 - Achtsnicht, Stefan A1 - Poghossian, Arshak A1 - Wagner, Patrick A1 - Schöning, Michael Josef T1 - Multiplexing system for automated characterization of a capacitive field-effect sensor array JF - Physica Status Solidi A N2 - In comparison to single-analyte devices, multiplexed systems for a multianalyte detection offer a reduced assay time and sample volume, low cost, and high throughput. Herein, a multiplexing platform for an automated quasi-simultaneous characterization of multiple (up to 16) capacitive field-effect sensors by the capacitive–voltage (C–V) and the constant-capacitance (ConCap) mode is presented. The sensors are mounted in a newly designed multicell arrangement with one common reference electrode and are electrically connected to the impedance analyzer via the base station. A Python script for the automated characterization of the sensors executes the user-defined measurement protocol. The developed multiplexing system is tested for pH measurements and the label-free detection of ligand-stabilized, charged gold nanoparticles. KW - Capacitive field-effect sensor KW - Gold nanoparticles KW - Label-free detection KW - Multicell KW - Multiplexing Y1 - 2023 U6 - http://dx.doi.org/10.1002/pssa.202300265 SN - 1862-6300 (Print) SN - 1862-6319 (Online) N1 - Corresponding author: Michael Josef Schöning VL - 220 IS - 22 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Karschuck, Tobias A1 - Poghossian, Arshak A1 - Ser, Joey A1 - Tsokolakyan, Astghik A1 - Achtsnicht, Stefan A1 - Wagner, Patrick A1 - Schöning, Michael Josef T1 - Capacitive model of enzyme-modified field-effect biosensors: Impact of enzyme coverage JF - Sensors and Actuators B: Chemical N2 - 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. KW - Field-effect biosensor KW - Capacitive model KW - Enzyme coverage KW - Multianalyte detection KW - Penicillin Y1 - 2024 U6 - http://dx.doi.org/10.1016/j.snb.2024.135530 SN - 0925-4005 (Print) SN - 1873-3077 (Online) N1 - Corresponding Author: Michael J. Schöning VL - 408 PB - Elsevier CY - Amsterdam ER -