TY  - JOUR
A1  - Yarman, Aysu
A1  - Kurbanoglu, Sevinc
A1  - Jetzschmann, Katharina J.
A1  - Ozkan, Sibel A.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
T1  - Electrochemical MIP-Sensors for Drugs
JF  - Current Medicinal Chemistry
N2  - In order to replace bio-macromolecules by stable synthetic materials in separation techniques and bioanalysis biomimetic receptors and catalysts have been developed: Functional monomers are polymerized together with the target analyte and after template removal cavities are formed in the "molecularly imprinted polymer" (MIP) which resemble the active sites of antibodies and enzymes. Starting almost 80 years ago, around 1,100 papers on MIPs were published in 2016. Electropolymerization allows to deposit MIPs directly on voltammetric electrodes or chips for quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). For the readout of MIPs for drugs amperometry, differential pulse voltammetry (DPV) and impedance spectroscopy (EIS) offer higher sensitivity as compared with QCM or SPR. Application of simple electrochemical devices allows both the reproducible preparation of MIP sensors, but also the sensitive signal generation. Electrochemical MIP-sensors for the whole arsenal of drugs, e.g. the most frequently used analgesics, antibiotics and anticancer drugs have been presented in literature and tested under laboratory conditions. These biomimetic sensors typically have measuring ranges covering the lower nano-up to millimolar concentration range and they are stable under extreme pH and in organic solvents like nonaqueous extracts.
KW  - Biomimetic sensors
KW  - molecularly imprinted polymers
KW  - drug sensors
KW  - drug imprinting
KW  - electropolymerization
KW  - electrochemical sensors
Y1  - 2018
U6  - https://doi.org/10.2174/0929867324666171005103712
SN  - 0929-8673
SN  - 1875-533X
VL  - 25
IS  - 33
SP  - 4007
EP  - 4019
PB  - Bentham Science Publishers LTD
CY  - Sharjah
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Neumann, Bettina
A1  - Zhang, Xiaorong
A1  - Wollenberger, Ulla
A1  - Cordin, Aude
A1  - Haupt, Karsten
A1  - Scheller, Frieder W.
T1  - Enzymes as Tools in MIP-Sensors
JF  - Chemosensors
N2  - Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.
KW  - enzymatic MIP synthesis
KW  - template digestion
KW  - enzyme tracer
KW  - enzymatic analyte conversion
KW  - molecularly imprinted polymers
Y1  - 2017
U6  - https://doi.org/10.3390/chemosensors5020011
SN  - 2227-9040
VL  - 5
PB  - MDPI
CY  - Basel
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  - 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  - 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  - Xie, B.
A1  - Tang, X.
A1  - Wollenberger, Ursula
A1  - Johansson, G.
A1  - Gorton, Lo
A1  - Scheller, Frieder W.
A1  - Danielsson, B.
T1  - Hybrid biosensor for simultaneous electrochemical and thermal detection
Y1  - 1997
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  - 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  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
T1  - Enhancing biosensor performance using multienzyme systems
Y1  - 1993
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  - 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  -