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  -