TY - JOUR A1 - Zhao, Shuang A1 - Caruso, Frank A1 - Dähne, Lars A1 - Decher, Gero A1 - De Geest, Bruno G. A1 - Fan, Jinchen A1 - Feliu, Neus A1 - Gogotsi, Yury A1 - Hammond, Paula T. A1 - Hersam, Mark C. A1 - Khademhosseini, Ali A1 - Kotov, Nicholas A1 - Leporatti, Stefano A1 - Li, Yan A1 - Lisdat, Fred A1 - Liz-Marzán, Luis M. A1 - Moya, Sergio A1 - Mulvaney, Paul A1 - Rogach, Andrey L. A1 - Roy, Sathi A1 - Shchukin, Dmitry G. A1 - Skirtach, Andre G. A1 - Stevens, Molly M. A1 - Sukhorukov, Gleb B. A1 - Weiss, Paul S. A1 - Yue, Zhao A1 - Zhu, Dingcheng A1 - Parak, Wolfgang J. T1 - The Future of Layer-by-Layer Assembly: A Tribute to ACS Nano Associate Editor Helmuth Möhwald JF - ACS Nano N2 - Layer-by-layer (LbL) assembly is a widely used tool for engineering materials and coatings. In this Perspective, dedicated to the memory of ACS Nano associate editor Prof. Dr. Helmuth Möhwald, we discuss the developments and applications that are to come in LbL assembly, focusing on coatings, bulk materials, membranes, nanocomposites, and delivery vehicles. Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-12356 SN - 1936-086X VL - 13 IS - 6 SP - 6151 EP - 6169 ER - TY - JOUR A1 - Lisdat, Fred T1 - Coupling biology to electrochemistry—future trends and needs JF - Journal of Solid State Electrochemistry N2 - The coupling of biological entities with electrodes has already quite some history and has reached a status which is not only based on phenomenological descriptions. Nowadays, we are able to effectively couple redox centres within protein molecules to electrochemical transducers. This allows the transduction of a biochemical reaction into an electrode signal with applications mainly in sensing and bioenergetics [1,2,3,4,5,6,7,8]. However, in most cases, this coupling is not direct, and shuttle molecules or side products of the reaction are used. But also for the direct coupling, significant progress has been made, and several enzymes and redox proteins can be addressed directly by electrodes [8,9,10,11,12,13]. The understanding of the functioning of developed systems is, however, in its infancy. Charge and electrostatic interactions have been mostly studied, and for small dipole molecules such as cytochrome c, the situation can be well described [14]. There is a lack of understanding for more complex enzyme molecules which brings a lot of trial and error into research. Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-13639 SN - 1433-0768 VL - 24 SP - 2125 EP - 2127 PB - Springer Nature ER - TY - JOUR A1 - Göbel, Gero A1 - Talke, Anja A1 - Ahnert, Uwe A1 - Lisdat, Fred T1 - Electrochemical Activity Determination of Catechol-O-methyl Transferase by Selective Dopamine Detection JF - ChemElectroChem N2 - For the treatment of Parkinson's disease, as one of the most frequent diseases of the central nervous system, several key enzymes for dopamine metabolism [e. g. catechol-O-methyl transferase (COMT)] are drug targets. For an efficient and long-lasting treatment, the activity of this enzyme should be monitored. In this study, an electrochemical approach using differential pulse voltammetry (DPV) is introduced for the activity determination. The applied electrode material, fluorine-doped tin oxide (FTO), is characterized by a clear discrimination between substrate and product of COMT, a high stability of the dopamine signal during consecutive measurements, and a linear dependency on the dopamine concentration in the range of the maximum reaction rate of COMT. Despite these advantageous results, dopamine detection in the complete activity assay is influenced by each of the added essential assay components, even though none of the added components reveal a current signal at the FTO electrode itself. After adjusting the potential range and the assay composition, these effects can be circumvented. By following the dopamine concentrations during COMT action, it can be shown that the activity of COMT can be detected by using differential pulse voltammetry (DPV) at an FTO electrode and, by analyzing different COMT amounts, quantification can be demonstrated. KW - catechol-O-methyl transferase KW - dopamine KW - flow system KW - fluorine-doped tin oxide KW - sensing Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-13900 VL - 6 IS - 17 SP - 4533 EP - 4540 PB - Wiley ER - TY - GEN A1 - Balkenhohl, Thomas A1 - Beutler, Falko A1 - Schäfer, Daniel A1 - Lisdat, Fred T1 - Entwicklung eines impedimetrischen Biosensors für den Nachweis von Antigliadin Autoantikörpern T2 - Wissenschaftliche Beiträge 2007 N2 - In der vorliegenden Arbeit wurde ein Biosensor für den Nachweis von Antikörpern gegen Gliadin entwickelt. Gliadine sind Bestandteile der Getreideglutene und verantwortlich für die Manifestation der Zöliakie (Gluten-Unverträglichkeit). Der Biosensor basiert auf der Immobilisierung von Gliadin auf Goldelektroden, die zuvor mit Polystyrensulfonsäure beschichtet worden waren. Die erfolgreiche Immobilisierung wurde mit Hilfe der Quarzmikrowaage dokumentiert. Die Antigen-Antikörper-Bindung konnte durch die Inkubation mit einem Peroxidase-markierten Zweitantikörper und der enzymatischen Oxidation von 3-Amino-9- Ethylcarbazol (AEC) verstärkt werden. Die Zunahme in der Elektrodenisolierung durch die Bindungs- und Ablagerungsreaktion konnte durch elektrochemische Impedanzspektroskopie (EIS) in Anwesenheit des Hexacyanoferrat- Redoxsystems gemessen werden. Die Spektren wurden mit Hilfe eines Randles-Ersatzschaltbildes ausgewertet. Hierbei konnte eine Zunahme im Ladungstransferwiderstand festgestellt werden, die pro portional zur Antigliadin-Antikörperkonzentration, im Bereich von 10-8 M bis 10-6 M, war. Mit Hilfe dieses Sensors wurden schließlich humane Seren hinsichtlich ihrer Konzentration an Gliadinantikörpern, sowohl für Immunglobuline vom Typ IgG als auch IgA, untersucht. N2 - In this study an immunosensor was developed for the analysis of anti-gliadin antibodies. These antibodies can serve as an early diagnostic marker for celiac disease. The sensor is based on polystyrenesulfonic acid modifi ed gold electrodes on which gliadin was immobilized. The anti-gliadin antibody recognition was amplifi ed by a second binding step with a peroxidase- labeled antibody and subsequent peroxidase-catalyzed oxidation of 3-amino-9-ethylcarbazole (AEC) resulting in a precipitate formation on the electrode. The change of the electrode surface properties was followed by impedance spectroscopy in the presence of ferri-/ferrocyanide. By evaluating the impedance spectra the charge transfer resistance was found to be a suitable sensor parameter. A calibration curve for the detection of anti-gliadin antibodies was established for antibody concentrations between 10-8 M and 10-6 M and the sensor was also applied for the analysis of serum samples. Y1 - 2007 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus-522 SN - 0949-8214 VL - 12 SP - 48 EP - 57 ER - TY - JOUR A1 - Khalid, Waqas A1 - Göbel, Gero A1 - Hühn, Dominik A1 - Montenegro, Jose-Maria A1 - Rivera-Gil, Pilar A1 - Lisdat, Fred A1 - Parak, Wolfgang J. T1 - Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode JF - Journal of Nanobiotechnology N2 - An electrochemical sensor for p-aminophenyl phosphate (p APP) is reported. It is based on the electrochemical conversion of 4-aminophenol (4AP) at a quantum dot (QD) modified electrode under illumination. Without illumination no electron transfer and thus no oxidation of 4AP can occur. p APP as substrate is converted by the enzyme alkaline phosphatase (ALP) to generate 4AP as a product. The QDs are coupled via 1,4-benzenedithiol (BDT) linkage to the surface of a gold electrode and thus allow potential-controlled photocurrent generation. The photocurrent is modified by the enzyme reaction providing access to the substrate detection. In order to develop a photobioelectrochemical sensor the enzyme is immobilized on top of the photo-switchable layer of the QDs. Immobilization of ALP is required for the potential possibility of spatially resolved measurements. Geometries with immobilized ALP are compared versus having the ALP in solution. Data indicate that functional immobilization with layer-by-layer assembly is possible. Enzymatic activity of ALP and thus the photocurrent can be described by Michaelis- Menten kinetics. p APP is detected as proof of principle investigation within the range of 25 μM - 1 mM. Y1 - 2011 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-5808 SN - 1477-3155 VL - 9 IS - 46 ER - TY - JOUR A1 - Stern, Daniel A1 - Pauly, Diana A1 - Zydek, Martin A1 - Miller, Lilija A1 - Piesker, Janett A1 - Laue, Michael A1 - Lisdat, Fred A1 - Dorner, Martin B. A1 - Dorner, Brigitte G. A1 - Nitsche, Andreas T1 - Development of a Genus-Specific Antigen Capture ELISA for Orthopoxviruses – Target Selection and Optimized Screening JF - PLoS ONE N2 - Orthopoxvirus species like cowpox, vaccinia and monkeypox virus cause zoonotic infections in humans worldwide. Infections often occur in rural areas lacking proper diagnostic infrastructure as exemplified by monkeypox, which is endemic in Western and Central Africa. While PCR detection requires demanding equipment and is restricted to genome detection, the evidence of virus particles can complement or replace PCR. Therefore, an easily distributable and manageable antigen capture enzyme-linked immunosorbent assay (ELISA) for the detection of orthopoxviruses was developed to facilitate particle detection. By comparing the virus particle binding properties of polyclonal antibodies developed against surface-exposed attachment or fusion proteins, the surface protein A27 was found to be a well-bound, highly immunogenic and exposed target for antibodies aiming at virus particle detection. Subsequently, eight monoclonal anti-A27 antibodies were generated and characterized by peptide epitope mapping and surface plasmon resonance measurements. All antibodies were found to bind with high affinity to two epitopes at the heparin binding site of A27, toward either the N- or C-terminal of the crucial KKEP-segment of A27. Two antibodies recognizing different epitopes were implemented in an antigen capture ELISA. Validation showed robust detection of virus particles from 11 different orthopoxvirus isolates pathogenic to humans, with the exception of MVA, which is apathogenic to humans. Most orthopoxviruses could be detected reliably for viral loads above 1 × 103 PFU/mL. To our knowledge, this is the first solely monoclonal and therefore reproducible antibody-based antigen capture ELISA able to detect all human pathogenic orthopoxviruses including monkeypox virus, except variola virus which was not included. Therefore, the newly developed antibody-based assay represents important progress towards feasible particle detection of this important genus of viruses. Y1 - 2016 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-5830 SN - 1932-6203 VL - 11 IS - 3 ER - TY - GEN A1 - Vogt, Christian A1 - Lisdat, Fred T1 - BioHyTec: Biohybride Technologien in der Hauptstadtregion – Kompetenzbildung und Aufbau einer regionalen Wertschöpfungskette T2 - Wissenschaftliche Beiträge 2004 N2 - Das Bundesministerium für Bildung und Forschung (BMBF) startete 1999 mit dem InnoRegio-Wettbewerb eine neuartige Förderinitiative unter der Leitidee „Innovative Impulse in den Neuen Ländern“. In zahlreichen Regionen wurden Aktivitäten in Gang gesetzt, um neue Formen der Zusammenarbeit von Menschen aus den unterschiedlichsten Bereichen zu entwickeln und damit die Wertschöpfung und Wettbewerbsfähigkeit in den ostdeutschen Regionen zu erhöhen. An dieser Ausschreibung nahmen in der Anfangsphase 444 Bewerberregionen teil. Nach der ersten Jury-Sitzung im Oktober 1999 wurden 50 InnoRegios ausgewählt, in einer Entwicklungsphase ihre Kernkompetenzen herauszufiltern und tragfähige Innovationskonzepte zu erarbeiten. Mit der zweiten Jury-Sitzung im Herbst 2000 fiel der Startschuss zur Umsetzungsphase. Zur Zeit werden vom BMBF 23 InnoRegios in den Neuen Ländern gefördert. Y1 - 2004 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-4094 SN - 0949-8214 VL - 9 SP - 97 EP - 102 ER - TY - JOUR A1 - Zhao, Shuang A1 - Yue, Zhao A1 - Zhu, Dingcheng A1 - Harberts, Jann A1 - Blick, Robert H. A1 - Zierold, Robert A1 - Lisdat, Fred A1 - Parak, Wolfgang J. T1 - Quantum Dot/TiO2 Nanocomposite-Based Photoelectrochemical Sensor for Enhanced H2O2 Detection Applied for Cell Monitoring and Visualization JF - Small N2 - This work exploits the possibility of using CdSe/ZnS quantum dot (QD)-electrodes to monitor the metabolism of living cells based on photoelectrochemical (PEC) measurements. To realize that, the PEC setup is improved with respect to an enhanced photocurrent signal, better stability, and an increased signal-to-noise ratio, but also for a better biocompatibility of the sensor surface on which cells have been grown. To achieve this, a QD-TiO2 heterojunction is introduced with the help of atomic layer deposition (ALD). The heterojunction reduces the charge carrier recombination inside the semiconductor nanoparticles and improves the drift behavior. The PEC performance is carefully analyzed by adjusting the TiO2 thickness and combining this strategy with multilayer immobilizations of QDs. The optimal thickness of this coating is ≈5 nm; here, photocurrent generation can be enhanced significantly (e.g., for a single QD layer electrode by more than one order of magnitude at 0 V vs Ag/AgCl). The resulting optimized electrode is used for hydrogen peroxide (H2O2) sensing with a good sensitivity down to µmolar concentrations, reusability, stability, response rate, and repeatability. Finally, the sensing system is applied to monitor the activity of cells directly grown on top of the electrode surface. KW - biocompatible interface with atomic layer deposition KW - biosensor KW - detection of cellular metabolism KW - light addressable potentiometric sensor KW - photocurrent measurements Y1 - 2024 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-19642 VL - 20 IS - 45 PB - Wiley ER - TY - JOUR A1 - Göbel, Gero A1 - Dietz, T. A1 - Lisdat, Fred T1 - Biosensor based on an oxygen reducing bilirubin oxidase electrode JF - Procedia Chemistry N2 - An oxygen reducing electrode made of bilirubin oxidase and multi-walled carbon nanotubes (BOD-MWCNT-Au electrode) is coupled to enzymes catalysing oxygen-consuming reactions such as glucose oxidase (GOD) to result in a membrane-free bienzyme electrode. The feasibility of such a molecularly assembled system stabilized by covalent linkage has been demonstrated. The electrochemical characterisation of the bienzyme electrode reveals sensitivity to the enzyme substrate. The results indicate that the BOD-electrode provides a suitable platform for sensing analytes for which oxidases of high activity are available. KW - bienzyme sensor KW - bilirubin oxidase KW - carbon nanotube KW - membran-free KW - mediator-less Y1 - 2009 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-6237 SN - 1876-6196 VL - 1 IS - 1 SP - 273 EP - 276 ER - TY - JOUR A1 - Wegerich, F. A1 - Turano, Paola A1 - Allegrozzi, Marco A1 - Möhwald, H. A1 - Lisdat, Fred T1 - Superoxide Biosensing with Engineered Cytochrome c JF - Procedia Chemistry N2 - Several mutation positions have been chosen for introducing positively charged lysines in human cytochrome c (cyt c) with the aim of increasing the reaction rate with superoxide radicals (SO) and thus, the sensitivity of an electrochemical cyt c based SO biosensor. The impact of the mutations on structural and redox properties as well as on the reaction rate with SO are verified. Four mutants show a higher reaction rate with the radical compared to the wild type. These mutants are used for the construction of SO sensors based on thiol-modified gold electrodes and covalently fixed proteins. The E66K mutant electrode has a clearly higher sensitivity in comparison to the wildtype based sensor. KW - biosensor KW - cytochrome c KW - superoxide KW - protein engineering Y1 - 2009 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:526-opus4-6523 SN - 1876-6196 VL - 1 IS - 1 SP - 1287 EP - 1290 ER -