TY  - JOUR
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Erdossy, Julia
A1  - Katz, Sagie
A1  - Zebger, Ingo
A1  - Jetzschmann, Katharina J.
A1  - Altintas, Zeynep
A1  - Wollenberger, Ulla
A1  - Gyurcsanyi, Robert E.
A1  - Scheller, Frieder W.
T1  - Electrosynthesized MIPs for transferrin
BT  - Plastibodies or nano-filters?
JF  - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
N2  - Molecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.
KW  - Molecularly imprinted polymer
KW  - Scopoletin
KW  - Transferrin
KW  - Protein adsorption
KW  - Redox marker
Y1  - 2018
U6  - https://doi.org/10.1016/j.bios.2018.01.011
SN  - 0956-5663
SN  - 1873-4235
VL  - 105
SP  - 29
EP  - 35
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Zhang, Xiaorong
A1  - Caserta, Giorgio
A1  - Yarman, Aysu
A1  - Supala, Eszter
A1  - Tadjoung Waffo, Armel Franklin
A1  - Wollenberger, Ulla
A1  - Gyurcsanyi, Robert E.
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - "Out of Pocket" protein binding
BT  - a dilemma of epitope imprinted polymers revealed for human hemoglobin
JF  - Chemosensors
N2  - The epitope imprinting approach applies exposed peptides as templates to synthesize Molecularly Imprinted Polymers (MIPs) for the recognition of the parent protein. While generally the template protein binding to such MIPs is considered to occur via the epitope-shaped cavities, unspecific interactions of the analyte with non-imprinted polymer as well as the detection method used may add to the complexity and interpretation of the target rebinding. To get new insights on the effects governing the rebinding of analytes, we electrosynthesized two epitope-imprinted polymers using the N-terminal pentapeptide VHLTP-amide of human hemoglobin (HbA) as the template. MIPs were prepared either by single-step electrosynthesis of scopoletin/pentapeptide mixtures or electropolymerization was performed after chemisorption of the cysteine extended VHLTP peptide. Rebinding of the target peptide and the parent HbA protein to the MIP nanofilms was quantified by square wave voltammetry using a redox probe gating, surface enhanced infrared absorption spectroscopy, and atomic force microscopy. While binding of the pentapeptide shows large influence of the amino acid sequence, all three methods revealed strong non-specific binding of HbA to both polyscopoletin-based MIPs with even higher affinities than the target peptides.
KW  - Molecularly Imprinted Polymers
KW  - epitope imprinting
KW  - non-specific
KW  - binding
KW  - redox gating
KW  - SEIRA spectroelectrochemistry
Y1  - 2021
U6  - https://doi.org/10.3390/chemosensors9060128
SN  - 2227-9040
VL  - 9
IS  - 6
PB  - MDPI
CY  - Basel
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Sensors based on cytochrome P450 and CYP mimicking systems
JF  - ELECTROCHIMICA ACTA
N2  - Cytochrome P450 enzymes (CYPs) act on more than 90 percent of all drugs currently on the market. The catalytic cycle requires electron supply to the heme iron in the presence of oxygen. Electrochemistry allows to characterise the reaction mechanism of these redox enzymes by observing the electron transfer in real time. According to the number of publications on protein electrochemistry CYP has the third position after glucose oxidase and cytochrome c. CYP based enzyme electrodes for the quantification of drugs, metabolites or pesticides have been developed using different iso-enzymes. A crucial step in the sensor development is the efficiency of coupling the biocatalytic systems with the electrode is. In the 1970s the direct electron transfer of heme and heme peptides called microperoxidases (MPs) was used as model of oxidoreductases. They exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of P450 making heme and MPs to alternate recognition elements in biosensors for the detection of typical CYP substrates. In these enzyme electrodes the signal is generated by the conversion of all substrates thus representing in complex media an overall parameter. By combining the biocatalytic substrate conversion with selective binding to a molecularly imprinted polymer layer the specificity has been improved. Here we discuss different approaches of biosensors based on CYP, microperoxidases and catalytically active MIPs and discuss their potential as recognition elements in biosensors. The performance of these sensors and their further development are discussed. (C) 2013 Elsevier Ltd. All rights reserved.
KW  - Cytochrome P450
KW  - Microperoxidases
KW  - Catalytically active molecularly imprinted polymers
KW  - Biosensors
KW  - Personalised medicine
Y1  - 2013
U6  - https://doi.org/10.1016/j.electacta.2013.03.154
SN  - 0013-4686
SN  - 1873-3859
VL  - 110
SP  - 63
EP  - 72
PB  - PERGAMON-ELSEVIER SCIENCE LTD
CY  - OXFORD
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Schulz, Christopher
A1  - Sygmund, Cristoph
A1  - Ludwig, Roland
A1  - Gorton, Lo
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Third generation ATP sensor with enzymatic analyte recycling
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - For the first time the direct electron transfer of an enzyme - cellobiose dehydrogenase, CDH - has been coupled with the hexokinase catalyzed competition for glucose in a sensor for ATP. To enhance the signal output for ATP, pyruvate kinase was coimmobilized to recycle ADP by the phosphoenolpyruvate driven reaction. The new sensor overcomes the limit of 1:1 stoichiometry of the sequential or competitive conversion of ATP by effective enzymatic recycling of the analyte. The anodic oxidation of the glucose converting CDH proceeds at electrode potentials below 0 mV vs. Ag vertical bar AgCl thus potentially interfering substances like ascorbic acid or catecholamines do not influence the measuring signal. The combination of direct electron transfer of CDH with the enzymatic recycling results in an interference-free and oxygen-independent measurement of ATP in the lower mu molar concentration range with a lower limit of detection of 63.3 nM (S/N=3).
KW  - ATP
KW  - Third generation sensor
KW  - Enzymatic recycling
KW  - Cellobiose dehydrogenase
KW  - Hexokinase
KW  - Pyruvate kinase
Y1  - 2014
U6  - https://doi.org/10.1002/elan.201400231
SN  - 1040-0397
SN  - 1521-4109
VL  - 26
IS  - 9
SP  - 2043
EP  - 2048
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - How reliable is the electrochemical readout of MIP sensors?
JF  - Sensors
N2  - Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.
KW  - molecularly imprinted polymers
KW  - electropolymerization
KW  - direct electron
KW  - transfer
KW  - catalysis
KW  - redox marker
KW  - gate effect
Y1  - 2020
U6  - https://doi.org/10.3390/s20092677
SN  - 1424-8220
VL  - 20
IS  - 9
PB  - MDPI
CY  - Basel
ER  - 
TY  - GEN
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - How reliable is the electrochemical readout of MIP-sensors?
T2  - Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe
N2  - Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 960 
KW  - molecularly imprinted polymers
KW  - electropolymerization
KW  - direct electron transfer
KW  - catalysis
KW  - redox marker
KW  - gate effect
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-471608
SN  - 1866-8372
IS  - 960
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - Coupling biocatalysis with molecular imprinting in a biomimetic sensor
JF  - Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
KW  - biomimetic sensors
KW  - electropolymers
KW  - enzymes
KW  - hierarchical structures
KW  - molecularly imprinted polymers
Y1  - 2013
U6  - https://doi.org/10.1002/anie.201305368
SN  - 1433-7851
SN  - 1521-3773
VL  - 52
IS  - 44
SP  - 11521
EP  - 11525
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - The first electrochemical MIP sensor for tamoxifen
JF  - Sensors
N2  - We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.
KW  - molecularly imprinted polymers
KW  - anticancer drug
KW  - tamoxifen
KW  - electropolymerisation
Y1  - 2014
U6  - https://doi.org/10.3390/s140507647
SN  - 1424-8220
VL  - 14
IS  - 5
SP  - 7647
EP  - 7654
PB  - MDPI
CY  - Basel
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.
KW  - Paracetamol
KW  - Molecularly imprinted polymers
KW  - Electropolymerization
KW  - Tyrosinase
KW  - Esterase
KW  - Phenacetin
Y1  - 2016
U6  - https://doi.org/10.1002/elan.201600042
SN  - 1040-0397
SN  - 1521-4109
VL  - 28
SP  - 2222
EP  - 2227
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - GEN
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - The first electrochemical MIP sensor for tamoxifen
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1046 
KW  - molecularly imprinted polymers
KW  - anticancer drug
KW  - tamoxifen
KW  - electropolymerisation
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-476173
SN  - 1866-8372
IS  - 1046
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Nagel, Thomas
A1  - Gajovic-Eichelmann, Nenad
A1  - Fischer, Anna
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by Microperoxidase-11 in a Multilayer Architecture of Chitosan Embedded Gold Nanoparticles
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - We report on the redox behaviour of the microperoxidase-11 (MP-11) which has been electrostatically immobilized in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode. MP-11 contains a covalently bound heme c as the redox active group that exchanges electrons with the electrode via the gold nanoparticles. Electroactive surface concentration of MP-11 at high scan rate is between 350+/-50 pmol cm(-2), which reflects a multilayer process. The formal potential (E degrees') of MP-11 in the gold nanoparticles-chitosan film was estimated to be -(267.7+/-2.9) mV at pH 7.0. The heterogeneous electron transfer rate constant (k(s)) starts at 1.21 s(-1) and levels off at 6.45 s(-1) in the scan rate range from 0.1 to 2.0 V s(-1). Oxidation and reduction of MP-11 by hydrogen peroxide and superoxide, respectively have been coupled to the direct electron transfer of MP-11.
KW  - Microperoxidase
KW  - Direct electron transfer
KW  - Nanoparticles
KW  - Hydrogen peroxide
KW  - Superoxide
KW  - Bioelectrocatalysis
Y1  - 2011
U6  - https://doi.org/10.1002/elan.201000535
SN  - 1040-0397
VL  - 23
IS  - 3
SP  - 611
EP  - 618
PB  - Wiley-Blackwell
CY  - Malden
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Kurbanoğlu, Sevinç
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - Simple and robust
BT  - the claims of protein sensing by molecularly imprinted polymers
JF  - Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers
N2  - A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 % of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.
KW  - Molecularly imprinted polymer
KW  - Plastibodies
KW  - Functional scaffolds
KW  - Biomimetic sensors
KW  - Proteins
Y1  - 2021
U6  - https://doi.org/10.1016/j.snb.2020.129369
SN  - 0925-4005
SN  - 1873-3077
VL  - 330
PB  - Elsevier Science
CY  - Amsterdam [u.a.]
ER  - 
TY  - JOUR
A1  - 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  - GEN
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
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1098 
KW  - enzymatic MIP synthesis
KW  - template digestion
KW  - enzyme tracer
KW  - enzymatic analyte conversion
KW  - molecularly imprinted polymers
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-474642
SN  - 1866-8372
IS  - 1098
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  - GEN
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
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 945 
KW  - bioelectrocatalysis
KW  - sulfite
KW  - sulfite oxidase
KW  - cytochrome c
KW  - multilayer
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-431176
SN  - 1866-8372
IS  - 945
SP  - 225
EP  - 233
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  - GEN
A1  - Peng, Lei
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Jeoung, Jae-Hun
A1  - Schad, Daniel
A1  - Dobbek, Holger
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis
N2  - For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of −184.4 ± 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 362 
KW  - molecularly imprinted polymers
KW  - self-assembled monolayer
KW  - direct electron transfer
KW  - hydrogen peroxide
KW  - bioelectrocatalysis
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400627
ER  - 
TY  - JOUR
A1  - Peng, Lei
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Jeoung, Jae-Hun
A1  - Schad, Daniel
A1  - Dobbek, Holger
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis
JF  - SENSORS
N2  - For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).
KW  - hydrogen peroxide
KW  - bioelectrocatalysis
KW  - molecularly imprinted polymers
KW  - direct electron transfer
KW  - self-assembled monolayer
Y1  - 2016
U6  - https://doi.org/10.3390/s16030272
SN  - 1424-8220
VL  - 16
SP  - 1343
EP  - 1364
PB  - MDPI
CY  - Basel
ER  -