TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Scheller, Frieder W. T1 - Development of a biomimetic alkane sensor f Y1 - 1998 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Scheller, Frieder W. T1 - Enzyme and microbial sensors for environmental Monitoring Y1 - 1993 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Riedel, K. A1 - Scheller, Frieder W. T1 - Enzyme and microbial sensors for phosphate, phenols, pesticides and peroxides Y1 - 1994 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Enzymatic substrade recycling electrodes Y1 - 1997 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Hintsche, R. A1 - Scheller, Frieder W. T1 - Biosensors for analytical microsystems Y1 - 1995 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Drungiliene, A. A1 - Stöcklein, Walter F. M. A1 - Kulys, J. A1 - Scheller, Frieder W. T1 - Direct electrocatalytic determination of dissolved peroxidases Y1 - 1996 ER - TY - JOUR A1 - Welzel, H.-P. A1 - Kossmehl, G. A1 - Engelmann, G. A1 - Neumann, B. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Schröder, W. T1 - Reactive groups on polymer covered electrodes, 4. Lactate-oxidase-biosensor based on electrodes modifies by polyphiophene Y1 - 1996 ER - TY - JOUR A1 - Welzel, H.-P. A1 - Kossmehl, G. A1 - Engelmann, G. A1 - Neumann, B. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins Y1 - 1997 ER - TY - JOUR A1 - Warsinke, Axel A1 - Stancik, L. A1 - Macholán, L. A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. T1 - Biosensors for food analysis : application of biosensors to food requirements Y1 - 1998 SN - 0-85404-750-6 ER - TY - JOUR A1 - Warsinke, Axel A1 - Benkert, Alexander A1 - Scheller, Frieder W. T1 - Biomolecular modules for creatinine determination Y1 - 1996 ER - TY - JOUR A1 - Warsinke, Axel A1 - Benkert, Alexander A1 - Scheller, Frieder W. T1 - Electrochemical immunoassays Y1 - 2000 ER - TY - JOUR A1 - Vijgenboom, E. A1 - Vijgenboom, E. A1 - Teppner, A. W. J. W. A1 - Makower, Alexander A1 - Scheller, Frieder W. A1 - Canters, Gerard W. A1 - Wollenberger, Ursula T1 - Determination of phenolic compounds using recombinant tyrosinanse from Streptomyces antibioticus Y1 - 2001 ER - TY - JOUR A1 - Teller, C. A1 - Halamek, Jan A1 - Makower, Alexander A1 - Fournier, Didier A1 - Schulze, H. A1 - Scheller, Frieder W. T1 - A piezoelectric sensor with propidium as a recognition element for cholinesterases N2 - A piezoelectric biosensor has been developed on the basis of the reversible acetylcholinesterase (AChE) inhibitor propidium. The propidium cation was bound to a 11-mercaptoundecanoic acid monolayer on gold-coated quartz crystals. The immobilization was done via activation of carboxyl groups by 1,3-dicyclohexylcarbodiimide (DCC). Different types of cholinesterases (acetyl- and butyryl-ChE) from different origins were tested for their binding ability towards the immobilized propidium. Binding Studies were performed in a flow system, Furthermore, catalytically active and organophosphate-inhibited enzyme were compared re-aiding their binding capability. The binding constants were derived by using an one to one binding model and a refined model also including rebinding effects. It was shown that organophosphorylation of the active site hardly influences the affinity of AChE towards propidium. Furthermore the propidium-based biosensor provides equal sensitivity as compared with piezolelectric sensors with immobilized paraoxon- an active site ligand of AChE. (c) 2005 Elsevier B.V. All rights reserved Y1 - 2006 U6 - https://doi.org/10.1016/j.snb.2005.02.053 ER - TY - JOUR A1 - Tanne, Johannes A1 - Jeoung, Jae-Hun A1 - Peng, Lei A1 - Yarman, Aysu A1 - Dietzel, Birgit A1 - Schulz, Burkhard A1 - Schad, Daniel A1 - Dobbek, Holger A1 - Wollenberger, Ursula A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH. KW - HTHP KW - Nanohybrid KW - Poylaniline KW - Multiwalled carbon nanotube Y1 - 2015 U6 - https://doi.org/10.1002/elan.201500231 SN - 1040-0397 SN - 1521-4109 VL - 27 IS - 10 SP - 2262 EP - 2267 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Tadjoung Waffo, Armel Franklin A1 - Yesildag, Cigdem A1 - Caserta, Giorgio A1 - Katz, Sagie A1 - Zebger, Ingo A1 - Lensen, Marga C. A1 - Wollenberger, Ulla A1 - Scheller, Frieder W. A1 - Altintas, Zeynep T1 - Fully electrochemical MIP sensor for artemisinin JF - Sensors and actuators : B, Chemical N2 - This study aims to develop a rapid, sensitive and cost-effective biomimetic electrochemical sensor for artemisinin determination in plant extracts and for pharmacokinetic studies. A novel molecularly imprinted polymer (MIP)based electrochemical sensor was developed by electropolymerization of o-phenylenediamine (o-PD) in the presence of artemisinin on gold wire surface for sensitive detection of artemisinin. The experimental parameters, including selection of functional monomer, polymerization conditions, template extraction after polymerization, influence of pH and buffer were all optimized. Every step of imprinted film synthesis were evaluated by employing voltammetry techniques, surface-enhanced infrared absorption spectroscopy (SEIRAS) and atomic force microscopy (AFM). The specificity was further evaluated by investigating non-specific artemisinin binding on non-imprinted polymer (NIP) surfaces and an imprinting factor of 6.8 was achieved. The artemisinin imprinted polymers using o-PD as functional monomer have provided highly stable and effective binding cavities for artemisinin. Cross-reactivity studies with drug molecules showed that the MIPs are highly specific for artemisinin. The influence of matrix effect was further investigated both in artificial plant matrix and diluted human serum. The results revealed a high affinity of artemisinin-MIP with dissociation constant of 7.3 x 10(-9) M and with a detection limit of 0.01 mu M and 0.02 mu M in buffer and plant matrix, respectively. KW - Electro-synthesized molecularly imprinted polymer KW - o-Phenylenediamine KW - Artemisinin KW - Antimalarial drug detection KW - Electrochemical sensor Y1 - 2018 U6 - https://doi.org/10.1016/j.snb.2018.08.018 SN - 0925-4005 VL - 275 SP - 163 EP - 173 PB - Elsevier CY - Lausanne ER - TY - JOUR A1 - Szeponik, Jan A1 - Möller, B. A1 - Pfeiffer, Dorothea A1 - Lisdat, Fred A1 - Wollenberger, Ursula A1 - Makower, Alexander A1 - Scheller, Frieder W. T1 - Ultrasensitive bienzyme sensor for adrenaline Y1 - 1997 ER - TY - JOUR A1 - Stöllner, Daniela A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Warsinke, Axel T1 - Membrane-immobilized haptoglobin as affinity matrix for a hemoglobin-A1c-immunosensor Y1 - 2002 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides Y1 - 1997 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Kempter, Gerhard A1 - Höhne, Wolfgang A1 - Scheller, Frieder W. T1 - Diphenylurea hapten sensing with a monoclonal antibody and its Fab fragment : kinetic and thermodynamic investigations Y1 - 1998 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Höhne, Wolfgang A1 - Woller, Jochen A1 - Kempter, Gerhard A1 - Scheller, Frieder W. T1 - Characterization of a monoclonal antibody and its Fab fragment against diphenylurea hapten with BIA Y1 - 1998 SN - 3-8154-3540-4 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Höhne, Wolfgang A1 - Woller, Jochen A1 - Kempter, Gerhard A1 - Scheller, Frieder W. T1 - Detection of diphenylurea derivatives with biospecific interaction analysis (BIA) : Kinetic investigations Y1 - 1997 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Abuknesha, Rhamadan T1 - Effects of organic solvents on semicontinuous immunochemical detection of coumarin derivatives Y1 - 1995 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Enzymes and antibodies in organic media : analytical applications Y1 - 1997 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Laccase : a marker enzyme for solvent modified immunoassays Y1 - 1996 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Rohde, M. A1 - Scharte, Gudrun A1 - Behrsing, Olaf A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Scheller, Frieder W. T1 - Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives Y1 - 2000 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Makower, Alexander A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Enzyme sensors and enzyme amplifification systems Y1 - 1997 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Behrsing, Olaf A1 - Scharte, Gudrun A1 - Micheel, Burkhard A1 - Benkert, Alexander A1 - Schössler, W. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Enzyme kinetic assays with surface plasmon resonance (BIAcore) based on competition between enzyme and creatinine antibody Y1 - 2000 ER - TY - JOUR A1 - Streffer, Katrin A1 - Kaatz, Helvi A1 - Bauer, Christian G. A1 - Makower, Alexander A1 - Schulmeister, Thomas A1 - Scheller, Frieder W. A1 - Peter, Martin G. A1 - Wollenberger, Ursula T1 - Application of a sensitive catechol detector for determination of tyrosinase inhibitors Y1 - 1998 ER - TY - JOUR A1 - Stojanovic, Zorica A1 - Erdossy, Julia A1 - Keltai, Katalin A1 - Scheller, Frieder W. A1 - Gyurcsanyi, Robert E. T1 - Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection JF - Analytica chimica acta : an international journal devoted to all branches of analytical chemistry N2 - Molecularly imprinted polymers (MIPs) rendered selective solely by the imprinting with protein templates lacking of distinctive properties to facilitate strong target-MIP interaction are likely to exhibit medium to low template binding affinities. While this prohibits the use of such MIPs for applications requiring the assessment of very low template concentrations, their implementation for the quantification of high-abundance proteins seems to have a clear niche in the analytical practice. We investigated this opportunity by developing a polyscopoletin-based MIP nanofilm for the electrochemical determination of elevated human serum albumin (HSA) in urine. As reference for a low abundance protein ferritin-MIPs were also prepared by the same procedure. Under optimal conditions, the imprinted sensors gave a linear response to HSA in the concentration range of 20-100 mg/dm(3), and to ferritin in the range of 120-360 mg/dm(3). While as expected the obtained limit of detection was not sufficient to determine endogenous ferritin in plasma, the HSA-sensor was successfully employed to analyse urine samples of patients with albuminuria. The results suggest that MIP-based sensors may be applicable for quantifying high abundance proteins in a clinical setting. (c) 2017 Elsevier B.V. All rights reserved. KW - Human serum albumin KW - Ferritin KW - Molecularly imprinted polymer KW - Scopoletin KW - Urine Y1 - 2017 U6 - https://doi.org/10.1016/j.aca.2017.04.043 SN - 0003-2670 SN - 1873-4324 VL - 977 SP - 1 EP - 9 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Stoellner, Daniela A1 - Scheller, Frieder W. A1 - Warsinke, Axel T1 - Activation of cellulose membranes with 1,1ï-carbonyldiimidazole or 1-cyano-4-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors Y1 - 2002 ER - TY - JOUR A1 - Stancík, L. A1 - Macholán, L. A1 - Pluhacek, I. A1 - Scheller, Frieder W. T1 - Biosensing of rapeseed glucosinolates using amperometric enzyme electrodes based on membrane-bound glucose oxidase or tyrosinase Y1 - 1995 ER - TY - JOUR A1 - Stancik, L. A1 - Macholán, L. A1 - Scheller, Frieder W. T1 - Biosensing of tyrosinase inhibitors in nonaqueous solvents Y1 - 1995 ER - TY - JOUR A1 - Spricigo, Roberto A1 - Richter, Claudia A1 - Leimkühler, Silke A1 - Gorton, Lo A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Sulfite biosensor based on osmium redox polymer wired sulfite oxidase N2 - A biosensor, based on a redoxactive osmium polymer and sulfite oxidase on screen-printed electrodes, is presented here as a promising method for the detection of sulfite. A catalytic oxidative current was generated when a sample containing sulfite was pumped over the carbon screen-printed electrode modified with osmium redox polymer wired sulfite oxidase. A stationary value was reached after approximately 50 s and a complete measurement lasted no more than 3 min. The electrode polarized at -0.1 V (vs. Ag vertical bar AgCl 1M KCl) permits minimizing the influence of interfering substances, since these compounds can be unspecific oxidized at higher potentials. Because of the good stability of the protein film on the electrode surface, a well functioning biosensor-flow system was possible to construct. The working stability and reproducibility were further enhanced by the addition of bovine serum albumin generating a more long-term stable and biocompatible protein environment. The optimized biosensor showed a stable signal for more than a week of operation and a coefficient of variation of 4.8% for 12 successive measurements. The lower limit of detection of the sensor was 0.5 mu M sulfite and the response was linear until 100 mu M. The high sensitivity permitted a 1:500 dilution of wine samples. The immobilization procedure and the operational conditions granted minimized interferences. Additionally, repeating the immobilization procedure to form several layers of wired SO further increased the sensitivity of such a sensor. Finally. the applicability of the developed sulfite biosensor was tested on real samples, such as white and red wines. Y1 - 2010 UR - http://www.sciencedirect.com/science/journal/09277757 U6 - https://doi.org/10.1016/j.colsurfa.2009.09.001 SN - 0927-7757 ER - TY - JOUR A1 - Spricigo, Roberto A1 - Leimkühler, Silke A1 - Gorton, Lo A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active JF - European journal of inorganic chemistry : a journal of ChemPubSoc Europe N2 - We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices. KW - Metalloenzymes KW - Enzyme catalysis KW - Immobilization KW - Osmium Y1 - 2015 U6 - https://doi.org/10.1002/ejic.201500034 SN - 1434-1948 SN - 1099-0682 IS - 21 SP - 3526 EP - 3531 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Spricigo, Roberto A1 - Dronov, Roman A1 - Lisdat, Fred A1 - Leimkühler, Silke A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer N2 - An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8% and lost 20% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample. Y1 - 2009 UR - http://www.springerlink.com/content/100417 U6 - https://doi.org/10.1007/s00216-008-2432-y SN - 1618-2642 ER - TY - JOUR A1 - Song, Min Ik A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - A method to detect superoxide radicals using teflon membrane and superoxide dismutase Y1 - 1995 ER - TY - JOUR A1 - Sigolaeva, L. V. A1 - Markower, Alexander A1 - Eremenko, A. V. A1 - Makhaeva, G. F. A1 - Malygin, V. V. A1 - Kurochkin, I. N. A1 - Scheller, Frieder W. T1 - Bioelectrochemical anaysis of neuropathy targes esterase activity in blood Y1 - 2001 ER - TY - JOUR A1 - Shumyantseva, V. V. A1 - Ivanov, Y. D. A1 - Bistolas, Nikitas A1 - Scheller, Frieder W. A1 - Archakov, Alexander I. A1 - Wollenberger, Ursula T1 - Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles N2 - A method for construction of biosensors with membranous cytochrome P450 isoenzymes was developed based on clay/ detergent/protein mixed films. Thin films of sodium montmorillonite colloid with incorporated cytochrome P450 2134 (CYP2B4) with nonionic detergent were prepared on glassy carbon electrodes. The modified electrodes were electrochemically characterized, and bio-electrocatalytic reactions were followed. CYP2B4 can be reduced fast on clay- modified glassy carbon electrodes in the presence of the nonionic detergent Tween 80. In anaerobic solutions, reversible oxidation and reduction is obtained with a formal potential between -0.292 and - 0.305 V vs Ag/AgCl 1 M KCl depending on the preparation of the biosensor. In air-saturated solution, bio-electrocatalytic reduction currents can be obtained with the CYP2B4-modified electrode on addition of typical substrates such as aminopyrine and benzphetamine. This reaction was suppressed when methyrapone, an inhibitor of P450 reactions, was present. Measurement of product formation also indicates the bioelectrocatialysis by CYP2B4 Y1 - 2004 ER - TY - JOUR A1 - Schulmeister, Thomas A1 - Scheller, Frieder W. T1 - The mathematics of exponential signal amplification in amperometric three enzyme electrodes Y1 - 1996 ER - TY - JOUR A1 - Schulmeister, Thomas A1 - Rose, Jürgen A1 - Scheller, Frieder W. T1 - Mathematical modelling of exponential amplification in membrane-based enzyme sensors Y1 - 1997 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Zhang, Xiaorong A1 - Yarman, Aysu A1 - Wollenberger, Ulla A1 - Gyurcsányi, Róbert E. T1 - Molecularly imprinted polymer-based electrochemical sensors for biopolymers JF - Current opinion in electrochemistry N2 - Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one ‘separation plate’; thus, the selectivity does not reach the values of ‘bulk’ measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an ‘overall apparent’ signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively. KW - Electropolymerization KW - Direct electron transfer KW - Redox marker KW - Epitope imprinting KW - Biomarker Y1 - 2018 U6 - https://doi.org/10.1016/j.coelec.2018.12.005 SN - 2451-9103 VL - 14 SP - 53 EP - 59 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Yarman, Aysu A1 - Bachmann, Till A1 - Hirsch, Thomas A1 - Kubick, Stefan A1 - Renneberg, Reinhard A1 - Schumacher, Soeren A1 - Wollenberger, Ursula A1 - Teller, Carsten A1 - Bier, Frank Fabian ED - Gu, MB ED - Kim, HS T1 - Future of biosensors: a personal view JF - Advances in biochemical engineering, biotechnology JF - Advances in Biochemical Engineering-Biotechnology N2 - Biosensors representing the technological counterpart of living senses have found routine application in amperometric enzyme electrodes for decentralized blood glucose measurement, interaction analysis by surface plasmon resonance in drug development, and to some extent DNA chips for expression analysis and enzyme polymorphisms. These technologies have already reached a highly advanced level and need minor improvement at most. The dream of the "100-dollar' personal genome may come true in the next few years provided that the technological hurdles of nanopore technology or of polymerase-based single molecule sequencing can be overcome. Tailor-made recognition elements for biosensors including membrane-bound enzymes and receptors will be prepared by cell-free protein synthesis. As alternatives for biological recognition elements, molecularly imprinted polymers (MIPs) have been created. They have the potential to substitute antibodies in biosensors and biochips for the measurement of low-molecular-weight substances, proteins, viruses, and living cells. They are more stable than proteins and can be produced in large amounts by chemical synthesis. Integration of nanomaterials, especially of graphene, could lead to new miniaturized biosensors with high sensitivity and ultrafast response. In the future individual therapy will include genetic profiling of isoenzymes and polymorphic forms of drug-metabolizing enzymes especially of the cytochrome P450 family. For defining the pharmacokinetics including the clearance of a given genotype enzyme electrodes will be a useful tool. For decentralized online patient control or the integration into everyday "consumables' such as drinking water, foods, hygienic articles, clothing, or for control of air conditioners in buildings and cars and swimming pools, a new generation of "autonomous' biosensors will emerge. KW - Biosensors KW - Molecularly imprinted polymers KW - Personalized medicine Y1 - 2014 SN - 978-3-642-54143-8; 978-3-642-54142-1 U6 - https://doi.org/10.1007/10_2013_251 SN - 0724-6145 VL - 140 SP - 1 EP - 28 PB - Springer CY - Berlin ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Lisdat, Fred T1 - Research and development in biosensors Y1 - 2001 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Schubert, Florian A1 - Pfeiffer, Dorothea A1 - Markower, Alexander A1 - McNeil, C. J. T1 - Multienzyme biosensors : coupled enzyme reactions and enzyme activation Y1 - 1993 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Pfeiffer, Dorothea A1 - Schubert, Florian T1 - Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology Y1 - 1996 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Lei, Chenghong A1 - Jin, Wen A1 - Ge, Bixia A1 - Lehmann, Claudia A1 - Lisdat, Fred A1 - Fridman, Vadim T1 - Bioelectrocatalysis by redox enzymes at modified electrodes Y1 - 2002 UR - www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Enzyme Electrodes Y1 - 2003 SN - 3-527-30401-0 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wagener, C. T1 - From gene to life Y1 - 2004 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Schubert, Frank A1 - Federowitz, J. T1 - Present state and frontiers in biosensorics Y1 - 1997 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Schmid, Rolf T1 - A tribute to Isao Karube (1942-2020) and his influence on sensor science JF - Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica KW - Karube KW - Japan KW - biosensors KW - lifetime achievements Y1 - 2020 U6 - https://doi.org/10.1007/s00216-020-02946-5 SN - 1618-2642 SN - 1618-2650 VL - 412 IS - 28 SP - 7709 EP - 7711 PB - Springer CY - Berlin ER - TY - GEN A1 - Scheller, Frieder W. A1 - Sakar Dasdan, Dolunay T1 - Selected papers presented on the 2nd International Conference on the New Trends in Chemistry, Zagreb, Croatia, April 19-22, 2016 Preface T2 - Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija Y1 - 2016 SN - 0324-1130 VL - 48 SP - 4 EP - 4 PB - Bulgarian Academy of Sciences CY - Sofia ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea A1 - Schubert, Florian A1 - Wollenberger, Ursula T1 - Enzyme - based electrodes Y1 - 1995 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea A1 - Lisdat, Fred A1 - Bauer, Christian G. A1 - Gajovic, Nenad T1 - Enzyme biosensors based on oxygen detection Y1 - 1998 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea T1 - Commercial devices based on amperometric biosensors Y1 - 1997 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Makower, Alexander A1 - Ghindilis, A. L. A1 - Bier, Frank Fabian A1 - Ehrentreich-Förster, Eva A1 - Wollenberger, Ursula A1 - Bauer, Christian G. A1 - Micheel, Burkhard A1 - Pfeiffer, Dorothea A1 - Szeponik, Jan A1 - Michael, N. A1 - Kaden, H. T1 - Enzyme sensors for subnanomolar concentrations Y1 - 1995 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Lisdat, Fred A1 - Wollenberger, Ursula T1 - Application of electrically contacted enzymes for biosensors Y1 - 2005 SN - 3-527- 30690-0 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Kleinjung, Frank A1 - Bier, Frank Fabian A1 - Markower, Alexander A1 - Neumann, Barbara A1 - Wollenberger, Ursula A1 - Kurochkin, Iliya N. A1 - Eremenko, Arkadi V. A1 - Barmin, Anatoli V. A1 - Klußmann, Sven A1 - Fürste, Jens-Peter A1 - Erdmann, Volker A. A1 - Mansuy, D. T1 - New recognition elements in biosensing Y1 - 1998 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Kirstein, Dieter A1 - Schubert, Florian A1 - Pfeiffer, Dorothea A1 - McNeil, C. J. T1 - Enzymes in electrochemical biosensors Y1 - 1993 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Jin, Wen A1 - Ehrentreich-Förster, Eva A1 - Ge, Bixia A1 - Lisdat, Fred A1 - Büttemeyer, R. A1 - Wollenberger, Ursula T1 - Cytochrome c based superoxide sensor for in vivo application Y1 - 1999 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Heiduschka, P. T1 - Preparation of an electrode surface with a high density of binding sites by an electrochemical reduction of a poly (nitrophenol) film Y1 - 1994 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bistolas, Nikitas A1 - Liu, Songqin A1 - Jänchen, Michael A1 - Katterle, Martin A1 - Wollenberger, Ursula T1 - Thirty years of haemoglobin electrochemistry N2 - Electrochemical investigations of the blood oxygen carrier protein include both mediated and direct electron transfer. The reaction of haemoglobin (Hb) with typical mediators, e.g., ferricyanide, can be quantified by measuring the produced ferrocyanide which is equivalent to the Hb concentration. Immobilization of the mediator within the electrode body allows reagentless electrochemical measuring of Hb. On the other hand, entrapment of the protein within layers of polyclectrolytes, lipids, nanoparticles of clay or gold leads to a fast heterogeneous electron exchange of the partially denatured Hb. (c) 2005 Elsevier B.V. All rights reserved Y1 - 2005 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bier, Frank Fabian T1 - Analytical Biochemistry (Editorial) Y1 - 2004 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bauer, Christian G. A1 - Markower, Alexander A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Bier, Frank Fabian T1 - Coupling of immunoassays with enzymatic recycling electrodes Y1 - 2001 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bauer, Christian G. A1 - Makower, Alexander A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Bier, Frank Fabian T1 - Immunoassays using enzymatic amplification electrodes Y1 - 2002 SN - 0-7484-0791-X ER - TY - JOUR A1 - Scheller, Frieder W. T1 - Tribute to Guenter Gauglitz (Editorial) Y1 - 2009 UR - http://www.springerlink.com/content/100417 U6 - https://doi.org/10.1007/s00216-008-2548-0 SN - 1618-2642 ER - TY - JOUR A1 - Scheller, Frieder W. T1 - New recognition elements for bioanalytics Y1 - 1996 ER - TY - JOUR A1 - Rose, Andreas A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis Y1 - 2001 ER - TY - JOUR A1 - Riedel, M. A1 - Sabir, N. A1 - Scheller, Frieder W. A1 - Parak, Wolfgang J. A1 - Lisdat, Fred T1 - Connecting quantum dots with enzymes BT - mediator-based approaches for the light-directed read-out of glucose and fructose oxidation JF - Nanoscale N2 - The combination of the biocatalytic features of enzymes with the unique physical properties of nanoparticles in a biohybrid system provides a promising approach for the development of advanced bioelectrocatalytic devices. This study describes the construction of photoelectrochemical signal chains based on CdSe/ZnS quantum dot (QD) modified gold electrodes as light switchable elements, and low molecular weight redox molecules for the combination with different biocatalysts. Photoelectrochemical and photoluminescence experiments verify that electron transfer can be achieved between the redox molecules hexacyanoferrate and ferrocene, and the QDs under illumination. Since for both redox mediators a concentration dependent photocurrent change has been found, light switchable enzymatic signal chains are built up with fructose dehydrogenase (FDH) and pyrroloquinoline quinone-dependent glucose dehydrogenase ((PQQ) GDH) for the detection of sugars. After immobilization of the enzymes at the QD electrode the biocatalytic oxidation of the substrates can be followed by conversion of the redox mediator in solution and subsequent detection at the QD electrode. Furthermore, (PQQ) GDH has been assembled together with ferrocenecarboxylic acid on top of the QD electrode for the construction of a funtional biohybrid architecture, showing that electron transfer can be realized from the enzyme over the redox mediator to the QDs and subsequently to the electrode in a completely immobilized fashion. The results obtained here do not only provide the basis for light-switchable biosensing and bioelectrocatalytic applications, but may also open the way for self-driven point-of-care systems by combination with solar cell approaches (power generation at the QD electrode by enzymatic substrate consumption). Y1 - 2017 U6 - https://doi.org/10.1039/c7nr00091j SN - 2040-3364 SN - 2040-3372 VL - 9 SP - 2814 EP - 2823 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Riedel, K. A1 - Beyersdorf-Radeck, Baerbel A1 - Neumann, B. A1 - Scheller, Frieder W. A1 - Schmid, Rolf D. T1 - Microbial sensors for determination of aromatics and their chloro derivatives. Part III: Determination of chlorinated phenols using a biosensor containing Trichosporon beigelii (cutaneum) Y1 - 1995 ER - TY - JOUR A1 - Pieper-Fürst, U. A1 - Kleuser, U. A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor N2 - We describe in this paper the development of a one-step sandwich assay for the highly sensitive and fast detection of human matrix metalloproteinase (MMP)-2 (EC 3.4.24.24), using surface plasmon resonance (SPR). For the assay, two ligands were selected: monoclonal anti-MMP-2 antibody Ab-2 and the tissue inhibitor of metalloproteinases (TIMP)-2. They were chosen on the basis of (1) their affinities to MMP-2, (2) the efficiency of immobilization to the sensor chip, (3) the efficiency of adsorption to colloidal gold, and (4) the stability of these protein-coated gold particles. The assay included mixing of MMP-2 with antibody Ab-2 adsorbed to colloidal gold with a diameter of about 20 rim and injection into the flowcell of the SPR instrument containing immobilized TIMP-2. By using colloidal gold particles an amplification factor of 114 and a detection limit of 0.5 pM for MMP-2 were obtained. The precision of the assay was high even at low analyte concentrations, the standard deviation being 8.3% for five determinations of 1 pM MMP- 2. No significant binding was observed with the structurally related MMP-9. The assay is far more sensitive and faster than commonly used methods for MMP-2 detection. As TIMP-bound MMP-2 is not detected by this method, the assay can be applied for measuring free MMP-2, reflecting the imbalance of free and inhibitor-bound enzyme in various pathological situations. (C) 2004 Elsevier Inc. All rights reserved Y1 - 2004 ER - TY - JOUR A1 - Pfeiffer, Dorothea A1 - Yang, L. A1 - Scheller, Frieder W. A1 - Kissinger, P. T. T1 - Continous measurement of lactate in microdialysate Y1 - 1997 ER - TY - JOUR A1 - Pfeiffer, Dorothea A1 - Schubert, Frank A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemical sensors : enzyme electrodes and field effect transistors Y1 - 1996 ER - TY - JOUR A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. A1 - Schubert, Florian A1 - Setz, K. T1 - Amperometric enzyme electrodes for lactate and glucose determinations in highly diluted and undiluted media Y1 - 1993 ER - TY - JOUR A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. A1 - McNeil, C. J. A1 - Schulmeister, Thomas T1 - Cascade-like exponential substrate amplification in enzyme sensors Y1 - 1995 ER - TY - JOUR A1 - Peng, Lei A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Jeoung, Jae-Hun A1 - Schad, Daniel A1 - Dobbek, Holger A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis JF - SENSORS N2 - For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP). KW - hydrogen peroxide KW - bioelectrocatalysis KW - molecularly imprinted polymers KW - direct electron transfer KW - self-assembled monolayer Y1 - 2016 U6 - https://doi.org/10.3390/s16030272 SN - 1424-8220 VL - 16 SP - 1343 EP - 1364 PB - MDPI CY - Basel ER - TY - JOUR A1 - Peng, Lei A1 - Utesch, Tillmann A1 - Yarman, Aysu A1 - Jeoung, Jae-Hun A1 - Steinborn, Silke A1 - Dobbek, Holger A1 - Mroginski, Maria Andrea A1 - Tanne, Johannes A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein JF - Chemistry - a European journal N2 - Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant k(s) values between 0.93 and 2.86 s(-1) and apparent formal potentials E-app(0)' between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH. KW - electrochemistry KW - electron transfer KW - heme proteins KW - molecular modeling KW - monolayers Y1 - 2015 U6 - https://doi.org/10.1002/chem.201405932 SN - 0947-6539 SN - 1521-3765 VL - 21 IS - 20 SP - 7596 EP - 7602 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Paeschke, Manfred A1 - Hintsche, Rainer A1 - Wollenberger, Ursula A1 - Jin, Wen A1 - Scheller, Frieder W. T1 - Dynamic redox recycling of cytochrome c Y1 - 1995 SN - 0022-0728 ER - TY - JOUR A1 - Ozcelikay, Goksu A1 - Kurbanoglu, Sevinc A1 - Zhang, Xiaorong A1 - Söz, Çağla Kosak A1 - Wollenberger, Ulla A1 - Ozkan, Sibel A. A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - Electrochemical MIP Sensor for Butyrylcholinesterase JF - Polymers N2 - Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range. KW - molecularly imprinted polymers KW - biomimetic sensors KW - butyrylcholinesterase KW - o-phenylenediamine KW - rivastigmine Y1 - 2019 U6 - https://doi.org/10.3390/polym11121970 SN - 2073-4360 VL - 11 IS - 12 PB - MDPI CY - Basel ER - TY - JOUR A1 - Ozcelikay, Goksu A1 - Kurbanoglu, Sevinc A1 - Yarman, Aysu A1 - Scheller, Frieder W. A1 - Ozkan, Sibel A. T1 - Au-Pt nanoparticles based molecularly imprinted nanosensor for electrochemical detection of the lipopeptide antibiotic drug Daptomycin JF - Sensors and actuators : B, Chemical N2 - In this work, a novel electrochemical molecularly imprinted polymer (MIP) sensor for the detection of the lipopeptide antibiotic Daptomycin (DAP) is presented which integrates gold decorated platinum nanoparticles (Au-Pt NPs) into the nanocomposite film. The sensor was prepared by electropolymerization of o-phenylenediamine (o-PD) in the presence of DAP using cyclic voltammetry. Cyclic voltammetry and differential pulse voltammetry were applied to follow the changes in the MIP-layer related to rebinding and removal of the target DAP by using the redox marker [Fe(CN)(6)](3-/4-). Under optimized operational conditions, the MIP/Au-Pt NPs/ GCE nanosensor exhibits a linear response in the range of 1-20 pM towards DAP. The limit of detection and limit of quantification were determined to be 0.161pM +/- 0.012 and 0.489pM +/- 0.012, respectively. The sensitivity towards the antibiotics Vancomycin and Erythromycin and the amino acids glycine and tryptophan was below 7 percent as compared with DAP. Moreover, the nanosensor was also successfully used for the detection of DAP in deproteinated human serum samples. KW - molecularly imprinted polymer KW - Daptomycin KW - platinum nanoparticles KW - gold KW - nanoparticles KW - modified electrodes Y1 - 2020 U6 - https://doi.org/10.1016/j.snb.2020.128285 SN - 0925-4005 VL - 320 PB - Elsevier Science CY - Amsterdam ER - TY - JOUR A1 - Nitsche, Andreas A1 - Kurth, Andreas A1 - Dunkhorst, Anna A1 - Pänke, Oliver A1 - Sielaff, Hendrik A1 - Junge, Wolfgang A1 - Muth, Doreen A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. A1 - Pauli, Georg A1 - Kage, Andreas T1 - One-step selection of vaccinia virus binding DNA-aptamers by MonoLEX Y1 - 2007 UR - http://www.biomedcentral.com/1472-6750/7 U6 - https://doi.org/10.1186/1472-6750-7-48 ER - TY - JOUR A1 - Neumann, Bettina A1 - Yarman, Aysu A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Characterization of the enhanced peroxidatic activity of amyloid beta peptide-hemin complexes towards neurotransmitters JF - Analytical & bioanalytical chemistry N2 - Binding of heme to the amyloid peptides A beta 40/42 is thought to be an initial step in the development of symptoms in the early stages of Alzheimer's disease by enhancing the intrinsic peroxidatic activity of heme. We found considerably higher acceleration of the reaction for the physiologically relevant neurotransmitters dopamine and serotonin than reported earlier for the artificial substrate 3,3',5,5'-tetramethylbenzidine (TMB). Thus, the binding of hemin to A beta peptides might play an even more crucial role in the early stages of Alzheimer's disease than deduced from these earlier results. To mimic complex formation, a new surface architecture has been developed: The interaction between the truncated amyloid peptide A beta 1-16 and hemin immobilized on an aminohexanethiol spacer on a gold electrode has been analyzed by cyclic voltammetry. The resulting complex has a redox pair with a 25 mV more cathodic formal potential than hemin alone. KW - Peroxidatic activity Y1 - 2014 U6 - https://doi.org/10.1007/s00216-014-7822-8 SN - 1618-2642 SN - 1618-2650 VL - 406 IS - 14 SP - 3359 EP - 3364 PB - Springer CY - Heidelberg ER - TY - JOUR A1 - Neumann, Bettina A1 - Götz, Robert A1 - Wrzolek, Pierre A1 - Scheller, Frieder W. A1 - Weidinger, Inez M. A1 - Schwalbe, Matthias A1 - Wollenberger, Ulla T1 - Enhancement of the Electrocatalytic Activity of Thienyl-Substituted Iron Porphyrin Electropolymers by a Hangman Effect JF - ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe N2 - The thiophene-modified iron porphyrin FeT3ThP and the respective iron Hangman porphyrin FeH3ThP, incorporating a carboxylic acid hanging group in the second coordination sphere of the iron center, were electropolymerized on glassy carbon electrodes using 3,4-ethylenedioxythiophene (EDOT) as co-monomer. Scanning electron microscopy images and Resonance Raman spectra demonstrated incorporation of the porphyrin monomers into a fibrous polymer network. Porphyrin/polyEDOT films catalyzed the reduction of molecular oxygen in a four-electron reaction to water with onset potentials as high as +0.14V vs. Ag/AgCl in an aqueous solution of pH7. Further, FeT3ThP/polyEDOT films showed electrocatalytic activity towards reduction of hydrogen peroxide at highly positive potentials, which was significantly enhanced by introduction of the carboxylic acid hanging group in FeH3ThP. The second coordination sphere residue promotes formation of a highly oxidizing reaction intermediate, presumably via advantageous proton supply, as observed for peroxidases and catalases making FeH3ThP/polyEDOT films efficient mimics of heme enzymes. KW - activation of oxygen species KW - electro-polymerization KW - Hangman porphyrin KW - heterogeneous catalysis KW - immobilization Y1 - 2018 U6 - https://doi.org/10.1002/cctc.201800934 SN - 1867-3880 SN - 1867-3899 VL - 10 IS - 19 SP - 4353 EP - 4361 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Menger, Marcus A1 - Yarman, Aysu A1 - Erdössy, Júlia A1 - Yildiz, Huseyin Bekir A1 - Gyurcsányi, Róbert E. A1 - Scheller, Frieder W. T1 - MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing JF - Biosensors : open access journal N2 - Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application. KW - biomimetic recognition elements KW - aptamers KW - molecularly imprinted polymers KW - chemical sensors KW - aptasensors KW - in vitro selection KW - SELEX Y1 - 2016 U6 - https://doi.org/10.3390/bios6030035 SN - 2079-6374 VL - 6 SP - 4399 EP - 4413 PB - MDPI CY - Basel ER - TY - JOUR A1 - Markower, Alexander A1 - Wollenberger, Ursula A1 - Hörtnagel, H. A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. T1 - Catecholamine detection using enzymatic amplification Y1 - 1997 ER - TY - JOUR A1 - Makower, Alexander A1 - Halámek, Jan A1 - Skládal, Petr A1 - Kernchen, Frank A1 - Scheller, Frieder W. T1 - New principle of direct real-time monitoring of the interaction of cholinesterase and its inhibitors by piezoelectric biosensor Y1 - 2003 ER - TY - JOUR A1 - Makower, Alexander A1 - Eremenko, A. V. A1 - Streffer, Katrin A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds Y1 - 1996 ER - TY - JOUR A1 - Makower, Alexander A1 - Barmin, Anatoli V. A1 - Morzunova, T. A1 - Eremenko, Arkadi V. A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Affinity enzymomoetric assay for detection of organophosphorus compounds Y1 - 1997 ER - TY - JOUR A1 - Mak, Wing Cheung A1 - Cheung, Kwan Yee A1 - Trau, Dieter A1 - Warsinke, Axel A1 - Scheller, Frieder W. A1 - Renneberg, Reinhard T1 - Electrochemical bioassay utilizing encapsulated electrochemical active microcrystal biolabels N2 - A new approach to perform electrochemical immunoassay based on the utilization of encapsulated microcrystal was developed. The microcrystal labels create a "supernova effect" upon exposure to a desired releasing agent. The microcrystal cores dissolve, and large amounts of signal-generating molecules diffuse across the capsule wall into the outer environment. Layer-by-Layer (LbL) technology was employed for the encapsulation of electrochemical signal- generating microcrystals (ferrocene microcrystals). The encapsulated microcrystals were conjugated with antibody molecules through the adsorption process. The biofunctionalized microcrystals were utilized as a probe for immunoassays. The microcrystal-based label system provided a high-signal molecule to antibody (SIP) ratio of 10(4)-10(5). Microcrystal biolabels with different antibody surface coverage (1.60-5.05 mg m(-2)) were subjected to a solid-phase immunoassay for the detection of mouse immunoglobulin G (M-IgG) molecules. The microcrystal-based immunoassay for the detection of M-IgG performed with microcrystals having antibody surface coverage of 5.05 mg m(-2) showed a sensitivity of 3.93 nA g(- 1) L-1 with a detection limit of 2.82 g L-1 Y1 - 2005 SN - 0003-2700 ER - TY - JOUR A1 - Mak, Karen K. W. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Renneberg, Reinhard T1 - An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration Y1 - 2003 ER - TY - JOUR A1 - Loew, Noya A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Katterle, Martin T1 - Direct electrochemistry and spectroelectrochemistry of osmium substituted horseradish peroxidase N2 - In this contribution the substitution of the central protoporphyrin IX iron complex of horseradish peroxidase by the respective osmium porphyrin complex is described. The direct electrochemical reduction of the Os containing horseradish peroxidase (OsHRP) was achieved at ITO and modified glassy carbon electrodes and in combination with spectroscopy revealed the three redox couples (OsHRP)-H-III/(OsHRP)-H-IV, (OsHRP)-H-IV/(OsHRP)-H-V and (OsHRP)-H-V/ (OsHRP)-H-VI. The midpoint potentials differ dependent on the electrode material used with E-1/2 (Os-III/IV) of -0.4 V (ITO) and -0.25 V (GC), E-1/2 (Os-IV/V) of -0.16 V (ITO) and +0.10 V (GC), and E-1/2 (Os-V/VI)of +018 V (ITO), respectively Moreover, with immobilised OsHRP the direct electrocatalytic reduction of hydrogen peroxide and tert-butyl hydroperoxide was observed. In comparison to electrodes modified with native HRP the sensitivity of the OsHRP-electrode for tert-butyl hydroperoxide is higher. Y1 - 2009 UR - http://www.sciencedirect.com/science/journal/15675394 U6 - https://doi.org/10.1016/j.bioelechem.2009.03.015 SN - 1567-5394 ER - TY - JOUR A1 - Loew, Noya A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Characterization of self-assembling of glucose dehydrogenase in mono- and multilayers on gold electrodes N2 - Glucose dehydrogenase (GDH) was assembled electrostatically onto QCM-gold electrodes by their sequential deposition with anionic polyelectrolytes such as PSS and PASA. For the layer-by-layer arrangements both the microgravimetric and the electrochemical sensor signal were followed. Increasing amounts of GDH were deposited by stepwise formation of alternating layers of GDH and PSS or PASA. The mass increase was about 1.88 mug/cm(2) for one GDH/ PASA bilayer and 2.4 mug/cm(2) for a GDH/PSS bilayer. The addition of phenolic compounds resulted in an oxidation current, which could be catalytically increased by the GDH catalysed reaction in the presence of glucose. The system functions as glucose sensor when quinones are present in nonlimiting amount. The amperometric response was already diffusion limited when a single layer of GDH was adsorbed. The sensor sensitivity increased by a factor of 10 when MSA was used instead of MUA as initial electrode modifier Y1 - 2004 ER - TY - JOUR A1 - Loew, Noya A1 - Bogdanoff, Peter A1 - Herrmann, Iris A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Katterle, Martin T1 - Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found. KW - cobalt porphyrin KW - electron transfer KW - horseradish peroxidase KW - hydrogen peroxide KW - immobilization Y1 - 2006 U6 - https://doi.org/10.1002/elan.200603664 SN - 1040-0397 VL - 18 IS - 23 SP - 2324 EP - 2330 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Liu, Songqin A1 - Wollenberger, Ursula A1 - Katterle, Martin A1 - Scheller, Frieder W. T1 - Ferroceneboronic acid-based amperometric biosensor for glycated hemoglobin N2 - An amperometric biosensor for the determination of glycated hemoglobin in human whole blood is proposed. The principle is based on the electrochemical measurement of ferroceneboronic acid (FcBA) that has been specifically bound to the glycated N-terminus. Hemoglobin is immobilized on a zirconium dioxide nanoparticle modified pyrolytic graphite electrode (PGE) in the presence of didodecyldimethylammonium bromide (DDAB). The incubation of this sensor in FcBA solution leads to the formation of an FcBA-modified surface due to the affinity interaction between boronate and the glycated sites of the hemoglobin. The binding of FcBA results in well-defined redox peaks with an E-0' of 0.299 V versus Ag/AgCl (1 M KCl). The square wave voltammetric response of the bound FcBA reflects the amount of glycated hemoglobin at the surface. This signal increases linearily with the degree of glycated hemoglobin from 6.8 to 14.0% of total immobilized hemoglobin. The scheme was applied to the determination of the fraction of glycated hemoglobin in whole blood samples. Y1 - 2006 UR - http://www.sciencedirect.com/science/journal/09254005 U6 - https://doi.org/10.1016/j.snb.2005.07.011 SN - 0925-4005 ER - TY - JOUR A1 - Liu, Songqin A1 - Wollenberger, Ursula A1 - Halamek, Jan A1 - Leupold, Eik A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP N2 - A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945 Y1 - 2005 ER - TY - JOUR A1 - Lisdat, Fred A1 - Wollenberger, Ursula A1 - Paeschke, Manfred A1 - Scheller, Frieder W. T1 - Sensitive catecholamine measurement using a monoenzymatic recycling system Y1 - 1998 ER - TY - JOUR A1 - Lisdat, Fred A1 - Utepbergenov, D. A1 - Haseloff, R. F. A1 - Blasig, Ingolf E. A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Brigelius-Flohé, Regina T1 - An optical method for the detection of oxidative stress using protein-RNA interaction Y1 - 2001 ER - TY - JOUR A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Technical principles. Electrodes Y1 - 2000 SN - 90-5702-447-7 ER - TY - JOUR A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Principles of sensorial radical detection - a minireview Y1 - 2000 ER - TY - JOUR A1 - Lisdat, Fred A1 - Ho, Wah O. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Richter, Torsten A1 - Bilitewski, Ursula T1 - Recycling systems based on screen-printed electrodes Y1 - 1998 ER - TY - JOUR A1 - Lisdat, Fred A1 - Ge, Bixia A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Meyer, T. T1 - Electrochemical behaviour and nitric oxides interaction of immobilised cytochrome c from Rhodocyclus gelatinosus Y1 - 2000 ER -