TY - JOUR A1 - Bauer, Christian G. A1 - Eremenko, A. V. A1 - Ehrentreich-Förster, Eva A1 - Bier, Frank Fabian A1 - Makower, Alexander A1 - Halsall, H. B. A1 - Heineman, W. R. A1 - Scheller, Frieder W. T1 - Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid Y1 - 1996 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Schubert, Florian A1 - Bier, Frank Fabian T1 - Vom Biosensor zur Nanobiotechnologie Y1 - 1995 ER - TY - JOUR A1 - Jetzschmann, Katharina J. A1 - Jagerszki, Gyula A1 - Dechtrirat, Decha A1 - Yarman, Aysu A1 - Gajovic-Eichelmann, Nenad A1 - Gilsing, Hans-Detlev A1 - Schulz, Burkhard A1 - Gyurcsanyi, Robert E. A1 - Scheller, Frieder W. T1 - Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition JF - Advanced functional materials N2 - Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid. KW - acetylcholinesterase KW - biomimetic sensors KW - molecularly imprinted electropolymers KW - peripheral anionic site KW - propidium Y1 - 2015 U6 - https://doi.org/10.1002/adfm.201501900 SN - 1616-301X SN - 1616-3028 VL - 25 IS - 32 SP - 5178 EP - 5183 PB - Wiley-VCH CY - Weinheim ER - TY - CHAP A1 - Asche, Hartmut A1 - Böckmann, Christine A1 - Laue, Steffen A1 - Löhmannsröben, Hans-Gerd A1 - Lemke, Matthias A1 - Schober, Lars A1 - Reich, Oliver A1 - Lück, Erika A1 - Schütte, Marc A1 - Domsch, Horst A1 - Makower, Alexander A1 - Scheller, Frieder W. A1 - Stöcklein, Wolfgang A1 - Wollenberger, Ursula A1 - Schultze, Rainer A1 - Hengstermann, Theo A1 - Schael, Frank T1 - Umweltforschung für das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme Y1 - 2000 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-3862 SP - 176 EP - 227 ER - TY - CHAP A1 - Lück, Erika A1 - Balderjahn, Ingo A1 - Kamm, Birgit A1 - Greil, Holle A1 - Wallschläger, Hans-Dieter A1 - Jessel, Beate A1 - Böckmann, Christine A1 - Oberhänsli, Roland A1 - Soyez, Konrad A1 - Schmeer, Ernst A1 - Blumenstein, Oswald A1 - Berndt, Klaus-Peter A1 - Edeling, Thomas A1 - Friedrich, Sabine A1 - Kaden, Klaus A1 - Scheller, Frieder W. A1 - Petersen, Hans-Georg A1 - Asche, Hartmut A1 - Bronstert, Axel A1 - Giest, Hartmut A1 - Gaedke, Ursula A1 - Löhmannsröben, Hans-Gerd A1 - Jeltsch, Florian A1 - Jänkel, Ralph A1 - Gzik, Axel A1 - Bork, Hans-Rudolf A1 - Bork, Hans-Rudolf T1 - Umweltforschung für das Land Brandenburg : Arbeitsgruppen und Professuren Y1 - 2000 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-3797 ER - TY - JOUR A1 - Bier, Frank Fabian A1 - Ehrentreich-Förster, Eva A1 - Scheller, Frieder W. A1 - Makower, Alexander A1 - Eremenko, A. V. A1 - Wollenberger, Ursula A1 - Bauer, Christian G. A1 - Pfeiffer, Dorothea A1 - Micheel, Burkhard T1 - Ultrasensitive biosensors Y1 - 1996 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 - 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 - 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. A1 - Bier, Frank Fabian T1 - Trends in der Bioanalytik Y1 - 2002 ER - TY - JOUR A1 - Nießner, Reinhard A1 - Broekaert, J. A1 - Einax, J. W. A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. T1 - Trendbericht analytische Biochemie 2000/2001 Y1 - 2002 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 - Yarman, Aysu A1 - Schulz, Christopher A1 - Sygmund, Cristoph A1 - Ludwig, Roland A1 - Gorton, Lo A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Third generation ATP sensor with enzymatic analyte recycling JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - For the first time the direct electron transfer of an enzyme - cellobiose dehydrogenase, CDH - has been coupled with the hexokinase catalyzed competition for glucose in a sensor for ATP. To enhance the signal output for ATP, pyruvate kinase was coimmobilized to recycle ADP by the phosphoenolpyruvate driven reaction. The new sensor overcomes the limit of 1:1 stoichiometry of the sequential or competitive conversion of ATP by effective enzymatic recycling of the analyte. The anodic oxidation of the glucose converting CDH proceeds at electrode potentials below 0 mV vs. Ag vertical bar AgCl thus potentially interfering substances like ascorbic acid or catecholamines do not influence the measuring signal. The combination of direct electron transfer of CDH with the enzymatic recycling results in an interference-free and oxygen-independent measurement of ATP in the lower mu molar concentration range with a lower limit of detection of 63.3 nM (S/N=3). KW - ATP KW - Third generation sensor KW - Enzymatic recycling KW - Cellobiose dehydrogenase KW - Hexokinase KW - Pyruvate kinase Y1 - 2014 U6 - https://doi.org/10.1002/elan.201400231 SN - 1040-0397 SN - 1521-4109 VL - 26 IS - 9 SP - 2043 EP - 2048 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Krylov, Andrey V. A1 - Beissenhirtz, Moritz Karl A1 - Adamzig, Holger A1 - Scheller, Frieder W. A1 - Lisdat, Fred T1 - Thick-film electrodes for measurement of superoxide and hydrogen peroxide based on direct protein-electrode contacts N2 - Cytochrome c was immobilized on screen-printed thick-film gold electrodes by a self-assembly approach using mixed monolayers of mercaptoundecanoic acid and mercaptoundecanol. Cyclic voltammetry revealed quasi-reversible electrochemical behavior of the covalently fixed protein with a formal potential of +10 mV vs. Ag/AgCl. Polarized at +150 mV vs. Ag/AgCl the electrode was found to be sensitive to superoxide radicals in the range 300-1200 nmol L-1. Compared with metal needle electrodes sensitivity and reproducibility could be improved and combined with the easiness of preparation. This allows the fabrication of disposable sensors for nanomolar superoxide concentrations. By changing the electrode potential the sensor can be switched from response to superoxide radicals to hydrogen peroxide-another reactive oxygen species. H2O2 sensitivity can be provided in the range 10-1000 mumol L-1 which makes the electrode suitable for oxidative stress studies 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 - GEN A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - The first electrochemical MIP sensor for tamoxifen T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1046 KW - molecularly imprinted polymers KW - anticancer drug KW - tamoxifen KW - electropolymerisation Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-476173 SN - 1866-8372 IS - 1046 ER - TY - JOUR A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - The first electrochemical MIP sensor for tamoxifen JF - Sensors N2 - We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences. KW - molecularly imprinted polymers KW - anticancer drug KW - tamoxifen KW - electropolymerisation Y1 - 2014 U6 - https://doi.org/10.3390/s140507647 SN - 1424-8220 VL - 14 IS - 5 SP - 7647 EP - 7654 PB - MDPI CY - Basel 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 - Eremenko, Arkadi V. A1 - Bauer, Christian G. A1 - Makower, Alexander A1 - Kanne, Beate A1 - Baumgarten, Horst A1 - Scheller, Frieder W. T1 - The development of a non-competitive immunoenzymometric Assay (IEMA) of cocaine Y1 - 1998 ER - TY - JOUR A1 - Huang, T. A1 - Warsinke, Axel A1 - Kuwana, T. A1 - Scheller, Frieder W. T1 - The determination of L-phenylalanine based on a novel NADH-detecting biosensor Y1 - 1998 ER -