TY  - JOUR
A1  - Bogdanovskaya, V. A.
A1  - Fridman, Vadim
A1  - Tarasevich, M. R.
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by immobilized peroxidase : the reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Kirstein, Dieter
A1  - Kirstein, Lincoln
A1  - Scheller, Frieder W.
A1  - Dieckmann, St.
A1  - Ronnenberg, J.
A1  - Beckmann, Dieter
A1  - Weckenbrock, E.
T1  - Elektroenzymatische Reduktion von Nitrat
Y1  - 1994
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  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - Coupling biocatalysis with molecular imprinting in a biomimetic sensor
JF  - Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
KW  - biomimetic sensors
KW  - electropolymers
KW  - enzymes
KW  - hierarchical structures
KW  - molecularly imprinted polymers
Y1  - 2013
U6  - https://doi.org/10.1002/anie.201305368
SN  - 1433-7851
SN  - 1521-3773
VL  - 52
IS  - 44
SP  - 11521
EP  - 11525
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Pfeiffer, Dorothea
T1  - Commercial devices based on amperometric biosensors
Y1  - 1997
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  - Warsinke, Axel
A1  - Benkert, Alexander
A1  - Scheller, Frieder W.
T1  - Biomolecular modules for creatinine determination
Y1  - 1996
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  - Halámek, Jan
A1  - Wollenberger, Ursula
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
T1  - Development of a biosensor for glycated hemoglobin
N2  - The development of an electrochemical piezoelectric sensor for the detection of glycated hemoglobin is presented. The total hemoglobin (Hb) content is monitored with a mass-sensitive quartz crystal modified with surfactants, and the glycated fraction of the immobilized Hb is determined by subsequent voltarnmetric measurement of the coupled ferroceneboronic acid. Different modifications of the sensor were tested for their hemoglobin binding ability. Deoxycholate (DOCA) was found to be the most suitable among the examined modifiers. Piezoelectric quartz crystals with gold electrodes were modified with DOCA by covalent binding to a pre-formatted 4-aminothiophenol monolayer. The properties of the Hb binding to DOCA and the pH effect on this interaction were studied. In the proposed assay for glycated hemoglobin at first an Hb sample is incubated with ferroceneboronic acid (FcBA), which binds to the fructosyl residue of the glycated Hb. Then this preincubated Hb sample is allowed to interact with the DOCA-modified piezoelectric quartz crystal. The binding is monitored by quartz crystal nanobalance QCN). The amount of FcBA present on the sensor surface is determined by square wave voltammetry. The binding of FcBA results in well-defined peaks with an EO' of +200 mV versus Ag/AgC1 (1 M KC1). The peak height depends on the degree of glycated Hb in the sample ranging from 0% to 20% of total Hb. The regeneration of the sensing surface is achieved by pepsin digestion of the deposited Hb. Thus the sensor can be re-used more than 30 times.
Y1  - 2007
UR  - http://www.sciencedirect.com/science/journal/00134686
U6  - https://doi.org/10.1016/j.electacta.2007.03.059
SN  - 0013-4686
ER  - 
TY  - JOUR
A1  - Halámek, Jan
A1  - Wollenberger, Ursula
A1  - Stöcklein, Walter F. M.
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
T1  - Signal amplification in immunoassays using labeling via boronic acid binding to the sugar moiety of immunoglobulin G : proof of concept for glycated hemoglobin
N2  - A novel electrochemical immunoassay based on the multiple affinity labeling of the indicator antibody with an electro-active tag is presented. The concept is illustrated for the determination of the glycated hemoglobin HbA1c in hemoglobin samples. Hemoglobin is adsorbed to the surfactant-modified surface of a piezoelectric quartz crystal. Whereas the quartz crystal nanobalance is used to validate the total Hb binding, the HbA1c on the sensor surface is recognized by an antibody and quantified electrochemically after the sugar moieties of the antibody have been labeled in-situ with ferroceneboronic acid. The sensitivity of this sensor is about threefold higher than the sensitivity of a hemoglobin sensor, where the ferroceneboronic acid is bound directly to HbA1c.
Y1  - 2007
UR  - http://www.informaworld.com/openurl?genre=journal&issn=0003-2719
U6  - https://doi.org/10.1080/00032710701327096
SN  - 0003-2719
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  - Yarman, Aysu
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Sensors based on cytochrome P450 and CYP mimicking systems
JF  - ELECTROCHIMICA ACTA
N2  - Cytochrome P450 enzymes (CYPs) act on more than 90 percent of all drugs currently on the market. The catalytic cycle requires electron supply to the heme iron in the presence of oxygen. Electrochemistry allows to characterise the reaction mechanism of these redox enzymes by observing the electron transfer in real time. According to the number of publications on protein electrochemistry CYP has the third position after glucose oxidase and cytochrome c. CYP based enzyme electrodes for the quantification of drugs, metabolites or pesticides have been developed using different iso-enzymes. A crucial step in the sensor development is the efficiency of coupling the biocatalytic systems with the electrode is. In the 1970s the direct electron transfer of heme and heme peptides called microperoxidases (MPs) was used as model of oxidoreductases. They exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of P450 making heme and MPs to alternate recognition elements in biosensors for the detection of typical CYP substrates. In these enzyme electrodes the signal is generated by the conversion of all substrates thus representing in complex media an overall parameter. By combining the biocatalytic substrate conversion with selective binding to a molecularly imprinted polymer layer the specificity has been improved. Here we discuss different approaches of biosensors based on CYP, microperoxidases and catalytically active MIPs and discuss their potential as recognition elements in biosensors. The performance of these sensors and their further development are discussed. (C) 2013 Elsevier Ltd. All rights reserved.
KW  - Cytochrome P450
KW  - Microperoxidases
KW  - Catalytically active molecularly imprinted polymers
KW  - Biosensors
KW  - Personalised medicine
Y1  - 2013
U6  - https://doi.org/10.1016/j.electacta.2013.03.154
SN  - 0013-4686
SN  - 1873-3859
VL  - 110
SP  - 63
EP  - 72
PB  - PERGAMON-ELSEVIER SCIENCE LTD
CY  - OXFORD
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by a selenoenzyme
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Kirstein, Dieter
A1  - Kirstein, Lincoln
A1  - Scheller, Frieder W.
A1  - Borcherding, H.
T1  - Amperometric nitrate biosensors on the basis of Pseudomonas stutzeri nitrate reductase
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Neue Dimensionen der Biosensorik
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Jin, Wen
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - PQQ as redox shuttle for quinoprotein glucose dehydrogenase
Y1  - 1998
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  - 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  - 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  - 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  - 
TY  - JOUR
A1  - Bauer, Christian G.
A1  - Eremenko, A. V.
A1  - Kühn, A.
A1  - Kürzinger, K.
A1  - Markower, Alexander
A1  - Scheller, Frieder W.
T1  - Automated amplifield flow immunoassay for cocaine
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Jin, Wen
A1  - Bernhardt, Rita
A1  - Lehmann, Claudia
A1  - Stöcklein, Walter F. M.
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Funktionalisierung von Elektroden für den direkten heterogenen Elektrotransfer
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Gajovic, Nenad
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
T1  - A bienzyme electrode for L-malate based on a novel and general design
Y1  - 1998
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  - Baeumner, Antje J.
A1  - Gauglitz, Guenter
A1  - Scheller, Frieder W.
T1  - Focus on bioanalysis
N2  - Editoria
Y1  - 2010
UR  - http://www.springerlink.com/content/100417
U6  - https://doi.org/10.1007/s00216-010-4203-9
SN  - 1618-2642
ER  - 
TY  - JOUR
A1  - Bosserdt, Maria
A1  - Gajovic-Eichelman, Nenad
A1  - Scheller, Frieder W.
T1  - Modulation of direct electron transfer of cytochrome c by use of a molecularly imprinted thin film
JF  - Analytical & bioanalytical chemistry
N2  - We describe the preparation of a molecularly imprinted polymer film (MIP) on top of a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold, where the template cytochrome c (cyt c) participates in direct electron transfer (DET) with the underlying electrode. To enable DET, a non-conductive polymer film is electrodeposited from an aqueous solution of scopoletin and cyt c on to the surface of a gold electrode previously modified with MUA. The electroactive surface concentration of cyt c was 0.5 pmol cm(-2). In the absence of the MUA layer, no cyt c DET was observed and the pseudo-peroxidatic activity of the scopoletin-entrapped protein, assessed via oxidation of Ampliflu red in the presence of hydrogen peroxide, was only 30 % of that for the MIP on MUA. This result indicates that electrostatic adsorption of cyt c by the MUA-SAM substantially increases the surface concentration of cyt c during the electrodeposition step, and is a prerequisite for the productive orientation required for DET. After template removal by treatment with sulfuric acid, rebinding of cyt c to the MUA-MIP-modified electrode occurred with an affinity constant of 100,000 mol(-1) L, a value three times higher than that determined by use of fluorescence titration for the interaction between scopoletin and cyt c in solution. The DET of cyt c in the presence of myoglobin, lysozyme, and bovine serum albumin (BSA) reveals that the MIP layer suppresses the effect of competing proteins.
KW  - Cytochrome c
KW  - Molecularly imprinted polymer film
KW  - Mercaptoundecanoic acid
KW  - Direct electron transfer
KW  - Scopoletin (7-hydroxy-6-methoxycoumarin)
Y1  - 2013
U6  - https://doi.org/10.1007/s00216-013-7009-8
SN  - 1618-2642
VL  - 405
IS  - 20
SP  - 6437
EP  - 6444
PB  - Springer
CY  - Heidelberg
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - New recognition elements for bioanalytics
Y1  - 1996
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  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Enzyme activation for activator and enzyme activity measurement
Y1  - 1993
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  - 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  - 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  - Wu, Yunhua
A1  - Wollenberger, Ursula
A1  - Hofrichter, Martin
A1  - Ullrich, Rene
A1  - Scheibner, Katrin
A1  - Scheller, Frieder W.
T1  - Direct electron transfer of Agrocybe aegerita peroxygenase at electrodes modified with chitosan-capped Au nanoparticles and its bioelectrocatalysis to aniline
JF  - Sensors and actuators : B, Chemical
N2  - Three different sizes of chitosan-capped Au nanoparticles were synthesized and were used to incorporate Agrocybe aegerita peroxygenase (AaeAPO) onto the surface of glassy carbon electrode. The direct electron transfer of AaeAPO was achieved in all films. The highest amount of electroactive enzyme and highest electron transfer rate constant k(s) of AaeAPO were obtained in the film with the smallest size of chitosan-capped Au nanoparticles.
 In anaerobic solutions, quasi-reversible oxidation and reduction are obtained with a formal potential of -0.280V vs. Ag/AgCl 1 M KCl in 100 mM (pH 7.0) PBS at scan rate of 1 V s(-1). Bioelectrocatalytic reduction currents can be obtained with the AaeAPO-modified electrode on addition of hydrogen peroxide. This reaction was suppressed when sodium azide, an inhibitor of AaeAPO, was present. Furthermore, the peroxide-dependent conversion of aniline was characterized and it was found that a polymer product via p-aminophenol is formed. And the AaeAPO biosensor was applied to determine aniline and p-aminophenol.
KW  - Agrocybe aegerita peroxygenase
KW  - Au nanoparticles
KW  - Direct electron transfer
KW  - Aniline biosensor
KW  - Bioelectrocatalysis
Y1  - 2011
U6  - https://doi.org/10.1016/j.snb.2011.09.090
SN  - 0925-4005
VL  - 160
IS  - 1
SP  - 1419
EP  - 1426
PB  - Elsevier
CY  - Lausanne
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Badalyan, Artavazd
A1  - Gajovic-Eichelmann, Nenad
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Enzyme electrode for aromatic compounds exploiting the catalytic activities of microperoxidase-11
JF  - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
N2  - Microperoxidase-11 (MR-11) which has been immobilised in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode catalyzes the conversion of aromatic substances. This peroxide-dependent catalysis of microperoxidase has been applied in an enzyme electrode for the first time to indicate aromatic compounds such as aniline. 4-fluoroaniline, catechol and p-aminophenol. The electrode signal is generated by the cathodic reduction of the quinone or quinoneimine which is formed in the presence of both MP-II and peroxide from the substrate. The same sensor principle will be extended to aromatic drugs.
KW  - Microperoxidase-11
KW  - Nanoparticles
KW  - p-Aminophenol
KW  - Aniline
KW  - Catechol
KW  - 4-Fluoroaniline
KW  - Biosensors
Y1  - 2011
U6  - https://doi.org/10.1016/j.bios.2011.09.004
SN  - 0956-5663
VL  - 30
IS  - 1
SP  - 320
EP  - 323
PB  - Elsevier
CY  - Oxford
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  - 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  - JOUR
A1  - Yarman, Aysu
A1  - Nagel, Thomas
A1  - Gajovic-Eichelmann, Nenad
A1  - Fischer, Anna
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by Microperoxidase-11 in a Multilayer Architecture of Chitosan Embedded Gold Nanoparticles
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - We report on the redox behaviour of the microperoxidase-11 (MP-11) which has been electrostatically immobilized in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode. MP-11 contains a covalently bound heme c as the redox active group that exchanges electrons with the electrode via the gold nanoparticles. Electroactive surface concentration of MP-11 at high scan rate is between 350+/-50 pmol cm(-2), which reflects a multilayer process. The formal potential (E degrees') of MP-11 in the gold nanoparticles-chitosan film was estimated to be -(267.7+/-2.9) mV at pH 7.0. The heterogeneous electron transfer rate constant (k(s)) starts at 1.21 s(-1) and levels off at 6.45 s(-1) in the scan rate range from 0.1 to 2.0 V s(-1). Oxidation and reduction of MP-11 by hydrogen peroxide and superoxide, respectively have been coupled to the direct electron transfer of MP-11.
KW  - Microperoxidase
KW  - Direct electron transfer
KW  - Nanoparticles
KW  - Hydrogen peroxide
KW  - Superoxide
KW  - Bioelectrocatalysis
Y1  - 2011
U6  - https://doi.org/10.1002/elan.201000535
SN  - 1040-0397
VL  - 23
IS  - 3
SP  - 611
EP  - 618
PB  - Wiley-Blackwell
CY  - Malden
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  - 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  - Yarman, Aysu
A1  - Gröbe, Glenn
A1  - Neumann, Bettina
A1  - Kinne, Mathias
A1  - Gajovic-Eichelmann, Nenad
A1  - Wollenberger, Ursula
A1  - Hofrichter, Martin
A1  - Ullrich, Rene
A1  - Scheibner, Katrin
A1  - Scheller, Frieder W.
T1  - The aromatic peroxygenase from Marasmius rutola-a new enzyme for biosensor applications
JF  - Analytical & bioanalytical chemistry
N2  - The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of -278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe(2+)/Fe(3+) redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.
KW  - Unspecific peroxygenase
KW  - Cytochrome P450
KW  - Biosensors
KW  - Phenolic substances
Y1  - 2012
U6  - https://doi.org/10.1007/s00216-011-5497-y
SN  - 1618-2642
VL  - 402
IS  - 1
SP  - 405
EP  - 412
PB  - Springer
CY  - Heidelberg
ER  - 
TY  - JOUR
A1  - Erdossy, Julia
A1  - Horvath, Viola
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Robert E.
T1  - Electrosynthesized molecularly imprinted polymers for protein recognition
JF  - Trends in Analytical Chemistry
N2  - Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.
KW  - Molecularly imprinted polymers
KW  - Proteins
KW  - Surface imprinting
KW  - Electropolymerization
KW  - Nanostructuring
KW  - Hybrid nanofilms
Y1  - 2016
U6  - https://doi.org/10.1016/j.trac.2015.12.018
SN  - 0165-9936
SN  - 1879-3142
VL  - 79
SP  - 179
EP  - 190
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.
KW  - Paracetamol
KW  - Molecularly imprinted polymers
KW  - Electropolymerization
KW  - Tyrosinase
KW  - Esterase
KW  - Phenacetin
Y1  - 2016
U6  - https://doi.org/10.1002/elan.201600042
SN  - 1040-0397
SN  - 1521-4109
VL  - 28
SP  - 2222
EP  - 2227
PB  - Wiley-VCH
CY  - Weinheim
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  - 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  - Yarman, Aysu
A1  - Dechtrirat, Decha
A1  - Bosserdt, Maria
A1  - Jetzschmann, Katharina J.
A1  - Gajovic-Eichelmann, Nenad
A1  - Scheller, Frieder W.
T1  - Cytochrome c-derived hybrid systems based on moleculary imprinted polymers
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - Hybrid architectures which combine a MIP with an immobilized affinity ligand or a biocatalyst sum up the advantages of both components. In this paper, hybrid architectures combining a layer of a molecularly imprinted electropolymer with a mini-enzyme or a self-assembled monolayer will be presented. (i) Microperoxidase-11 (MP-11) catalyzed oxidation of the drug aminopyrine on a product-imprinted sublayer: The peroxide dependent conversion of the analyte aminopyrine takes place in the MP-11 containing layer on top of a product-imprinted electropolymer on the indicator electrode. The hierarchical architecture resulted in the elimination of interfering signals for ascorbic acid and uric acid. An advantage of the new hierarchical structure is the separation of MIP formation by electropolymerization and immobilization of the catalyst. In this way it was for the first time possible to integrate an enzyme with a MIP layer in a sensor configuration. This combination has the potential to be transferred to other enzymes, e.g. P450, opening the way to clinically important analytes. (ii) Epitope-imprinted poly-scopoletin layer for binding of the C-terminal peptide and cytochrome c (Cyt c): The MIP binds both the target peptide and the parent protein almost eight times stronger than the non-imprinted polymer with affinities in the lower micromolar range. Exchange of only one amino acid in the peptide decreases the binding by a factor of five. (iii) MUA-poly-scopoletin MIP for cytochrome c: Cyt c bound to the MIP covered gold electrode exhibits direct electron transfer with a redox potential and rate constant typical for the native protein. The MIP cover layer suppresses the displacement of the target protein by BSA or myoglobin. The combination of protein imprinted polymers with an efficient electron transfer is a new concept for characterizing electroactive proteins such as Cyt c. The competition with other proteins shows that the MIP binds its target Cyt c preferentially and that molecular shape and the charge of protein determine the binding of interfering proteins.
KW  - Molecularly imprinted polymers
KW  - Microperoxidase-11
KW  - Cytochrome c
KW  - Catalytically active MIPs
KW  - Epitope imprinting
KW  - Monoclonal MIPs
Y1  - 2015
U6  - https://doi.org/10.1002/elan.201400592
SN  - 1040-0397
SN  - 1521-4109
VL  - 27
IS  - 3
SP  - 573
EP  - 586
PB  - Wiley-VCH
CY  - Weinheim
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  - 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  - 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  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Warsinke, Axel
A1  - Lisdat, Fred
T1  - Research and development in biosensors
Y1  - 2001
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  - Hock, Bertold
A1  - Scheller, Frieder W.
T1  - Conclusions and outlook
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Ignatov, S.
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
A1  - Lisdat, Fred
T1  - Detection of the antioxidant activity detection of flavonoids by using superoxide sensor
Y1  - 2001
SN  - 1-58603-164-3
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Meyerhoff, M. E.
A1  - Scheller, Frieder W.
T1  - Signal chains with cytochromes at SAM modified gold electrodes
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Krause, B.
A1  - Ehrlich, A.
A1  - Bienert, H.
A1  - Scheller, Frieder W.
T1  - Nucleic acid-promoted electron transfer to cytochrome c
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biosensoren auf dem Weg zur Biochip-Technologie
Y1  - 2001
UR  - http://bisc.ch/de/focus_bioelektronik_1_d.pdf
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biomoleküle als Reporter in der Analytik : keine Forschung im Elfenbeinturm
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  - Scheller, Frieder W.
A1  - Pfeiffer, Dorothea
T1  - Biosensor-Technologie in der Medizin und den Biowissenschaften
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Fridman, Vadim
A1  - Wollenberger, Ursula
A1  - Bogdanovskaya, V. A.
A1  - Lisdat, Fred
A1  - Ruzgas, T.
A1  - Lindgren, A.
A1  - Gorton, Lo
A1  - Scheller, Frieder W.
T1  - Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Makower, Alexander
A1  - Barmin, Anatoli V.
A1  - Scheller, Frieder W.
T1  - Eine neue Methode zur hochempfindlichen Analyse von Pestiziden
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Warsinke, Axel
A1  - Benkert, Alexander
A1  - Scheller, Frieder W.
T1  - Electrochemical immunoassays
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Gajovic, Nenad
A1  - Binyamin, Gary
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
A1  - Heller, A.
T1  - Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Clay based direct electrochemistry of myoglobin
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Wollenberger, Ursula
A1  - Jung, Christiane
A1  - Scheller, Frieder W.
T1  - Clay-bridged electron transfer between cytochrome P450(cam) and electrode
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Scheller, Frieder W.
T1  - Principles of sensorial radical detection - a minireview
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Chen, Ziping
A1  - Warsinke, Axel
A1  - Gajovic, Nenad
A1  - Große, St.
A1  - Hu, J.
A1  - Kleber, H.-P.
A1  - Scheller, Frieder W.
T1  - A D-carnitine dehydrogenase electrode for the assessment of enantiomeric purity of L-carnitine preparations
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biomolekulare Erkennungssysteme für die Biochemische Analytik
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biosensor-Stabilität
Y1  - 2000
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  - 
TY  - JOUR
A1  - Chen, Jian
A1  - Wollenberger, Ursula
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
T1  - Superoxide sensor based on hemin modified electrode
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Ju, Huangxian
A1  - Liu, Songqin
A1  - Ge, Bixia
A1  - Lisdat, Fred
A1  - Scheller, Frieder W.
T1  - Electrochemistry of cytochrome c immobilized on colloidal gold modified carbon paste electrodes and its electrocatalytic activity
Y1  - 2000
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  - Scheller, Frieder W.
T1  - Deutliche Signale setzen [Leitartikel]
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Huang, T.
A1  - Warsinke, Axel
A1  - Koroljova-Skorobogatko, O. V.
A1  - Makower, Alexander
A1  - Kuwana, T.
A1  - Scheller, Frieder W.
T1  - A bienzyme carbon paste electrode for the sensitive detection of NADPH and the measurement of glucose-6- phosphate dehydrogenase
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
T1  - Oligonucleotide-modified electrodes for fast electron transfer to cytochrome c
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Ehrentreich-Förster, Eva
A1  - Reszka, R.
A1  - Scheller, Frieder W.
T1  - SOD activity measurement using cytochrome c modified electrode
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Gajovic, Nenad
A1  - Warsinke, Axel
A1  - Huang, T.
A1  - Schulmeister, Thomas
A1  - Scheller, Frieder W.
T1  - Characterization and mathematical modelling of a novel bienzyme electrode for L-malate with cofactor recycling
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Bauer, Christian G.
A1  - Kühn, A.
A1  - Gajovic, Nenad
A1  - Skorobogatko, O. V.
A1  - Holt, P. J.
A1  - Bruce, N. C.
A1  - Makower, Alexander
A1  - Lowe, Ch. R.
A1  - Scheller, Frieder W.
T1  - New enzymen sensors for morphine and codeine based on morphine dehydrogenase and laccase
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Kleinjung, Frank
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
T1  - Changing functionality of surfaces by directed self-assembly using oligonucleotides - the oligo-tag
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Barmin, Anatoli V.
A1  - Eremenko, Arkadi V.
A1  - Osipova, T.
A1  - Kurochkin, Iliya
A1  - Makower, Alexander
A1  - Scheller, Frieder W.
T1  - Affinyi fermentometrischeskii analis ingibitorov cholinestarasi
Y1  - 1999
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  - Lei, Chenghong
A1  - Lisdat, Fred
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Cytochrome c : Clay-modified electrode
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Yarman, Aysu
T1  - Bio vs. Mimetika in der Bioanalytik
T1  - Bio vs. Mimetics in Bioanalysis: An Editorial
BT  - ein Editorial
JF  - Biochemie und analytische Biochemie
N2  - Natürliche Evolution hat geschaffenBiopolymereauf der Basis von Aminosäuren undNukleotidezeigt hohe chemische Selektivität und katalytische Kraft. Die molekulare Erkennung durch Antikörper und die katalytische Umwandlung der Substratmoleküle durch Enzyme findet in sogenannten Paratopen oder katalytischen Zentren des Makromoleküls statt, die typischerweise 10-15 Aminosäuren umfassen. Die konzertierte Wechselwirkung zwischen den Reaktionspartnern führt zu Affinitäten bis zu nanomolaren Konzentrationen für die Antigenbindung und nähert sich einer Million Umsätze pro Sekunde anEnzym-katalysierte Reaktionen.
N2  - Natural evolution has created biopolymers on the basis of amino
acids and nucleotides showing high chemical selectivity and catalytic
power. Molecular recognition by antibodies and catalytic conversion
of the substrate molecules by enzymes take place in so called paratopes or catalytic centres of the macromolecule which comprise typically 10-15 amino acids. The concerted interaction between the reaction partners result in affinities down to nanomolar concentrations for the antigen binding and approaches one million turnovers per second in enzyme-catalyzed reactions.
Nucleic acids bind complimentary single stranded nucleic acids by
base pairing (hybridisation) with nanomolar affinities but also interact highly specific with proteins, e.g. transcription factors, and lowmolecular weight molecules and even with ions.
Biomimetic binders and catalysts have been generated using
“evolution in the test tube” of non-natural nucleotides or total
chemical synthesis of (molecularly imprinted) polymers in order to
substitute the biological pendants in bioanalysis.
Y1  - 2015
SN  - 2161-1009
VL  - 4
IS  - 2
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  - Bognár, Zsófia
A1  - Supala, Eszter
A1  - Yarman, Aysu
A1  - Zhang, Xiaorong
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Róbert E.
T1  - Peptide epitope-imprinted polymer microarrays for selective protein recognition
BT  - application for SARS-CoV-2 RBD protein
JF  - Chemical science / RSC, Royal Society of Chemistry
N2  - We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.
Y1  - 2021
U6  - https://doi.org/10.1039/d1sc04502d
SN  - 2041-6539
VL  - 13
IS  - 5
SP  - 1263
EP  - 1269
PB  - Royal Society of Chemistry
CY  - Cambridge
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  - 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  - Yarman, Aysu
A1  - Kurbanoğlu, Sevinç
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - Simple and robust
BT  - the claims of protein sensing by molecularly imprinted polymers
JF  - Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers
N2  - A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 % of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.
KW  - Molecularly imprinted polymer
KW  - Plastibodies
KW  - Functional scaffolds
KW  - Biomimetic sensors
KW  - Proteins
Y1  - 2021
U6  - https://doi.org/10.1016/j.snb.2020.129369
SN  - 0925-4005
SN  - 1873-3077
VL  - 330
PB  - Elsevier Science
CY  - Amsterdam [u.a.]
ER  - 
TY  - JOUR
A1  - Caserta, Giorgio
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Supala, Eszter
A1  - Wollenberger, Ulla
A1  - Gyurcsányi, Róbert  E.
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms
JF  - Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)
N2  - Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague. 
This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c. 
To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin. 
This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target. 
Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy. 
This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.
KW  - SEIRA spectroelectrochemistry
KW  - peptide imprinting
KW  - electrosynthesis
KW  - MIP
KW  - glycated peptide
Y1  - 2021
U6  - https://doi.org/10.1016/j.electacta.2021.138236
SN  - 0013-4686
SN  - 1873-3859
VL  - 381
PB  - Elsevier
CY  - New York, NY [u.a.]
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
T1  - Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology
Y1  - 1996
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  - Schubert, Florian
A1  - Bier, Frank Fabian
T1  - Vom Biosensor zur Nanobiotechnologie
Y1  - 1995
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  - 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  - 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  - Pfeiffer, Dorothea
A1  - Schubert, Florian
A1  - Wollenberger, Ursula
T1  - Enzyme - based electrodes
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
T1  - Enhancing biosensor performance using multienzyme systems
Y1  - 1993
ER  - 
TY  - GEN
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
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).
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 362 
KW  - molecularly imprinted polymers
KW  - self-assembled monolayer
KW  - direct electron transfer
KW  - hydrogen peroxide
KW  - bioelectrocatalysis
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400627
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  -