@article{AltintasTakidenUteschetal.2019,
  author    = {Altintas, Zeynep and Takiden, Aref and Utesch, Tillmann and Mroginski, Maria A. and Schmid, Bianca and Scheller, Frieder W. and S{\"u}ssmuth, Roderich D.},
  title     = {Integrated approaches toward high-affinity artificial protein binders obtained via computationally simulated epitopes for protein recognition},
  series = {Advanced functional materials},
  volume    = {29},
  journal   = {Advanced functional materials},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201807332},
  pages     = {11},
  year      = {2019},
  abstract  = {Widely used diagnostic tools make use of antibodies recognizing targeted molecules, but additional techniques are required in order to alleviate the disadvantages of antibodies. Herein, molecular dynamic calculations are performed for the design of high affinity artificial protein binding surfaces for the recognition of neuron specific enolase (NSE), a known cancer biomarker. Computational simulations are employed to identify particularly stabile secondary structure elements. These epitopes are used for the subsequent molecular imprinting, where surface imprinting approach is applied. The molecular imprints generated with the calculated epitopes of greater stability (Cys-Ep1) show better binding properties than those of lower stability (Cys-Ep5). The average binding strength of imprints created with stabile epitopes is found to be around twofold and fourfold higher for the NSE derived peptide and NSE protein, respectively. The recognition of NSE is investigated in a wide concentration range, where high sensitivity (limit of detection (LOD) = 0.5 ng mL(-1)) and affinity (dissociation constant (K-d) = 5.3 x 10(-11)m) are achieved using Cys-Ep1 imprints reflecting the stable structure of the template molecules. This integrated approach employing stability calculations for the identification of stabile epitopes is expected to have a major impact on the future development of high affinity protein capturing binders.},
  language  = {en}
}
@incollection{AscheBoeckmannLaueetal.2000,
  author    = {Asche, Hartmut and B{\"o}ckmann, Christine and Laue, Steffen and L{\"o}hmannsr{\"o}ben, Hans-Gerd and Lemke, Matthias and Schober, Lars and Reich, Oliver and L{\"u}ck, Erika and Sch{\"u}tte, Marc and Domsch, Horst and Makower, Alexander and Scheller, Frieder W. and St{\"o}cklein, Wolfgang and Wollenberger, Ursula and Schultze, Rainer and Hengstermann, Theo and Schael, Frank},
  title     = {Umweltforschung f{\"u}r das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-3862},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {176 -- 227},
  year      = {2000},
  language  = {de}
}
@article{BaeumnerGauglitzScheller2010,
  author    = {Baeumner, Antje J. and Gauglitz, Guenter and Scheller, Frieder W.},
  title     = {Focus on bioanalysis},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-010-4203-9},
  year      = {2010},
  abstract  = {Editoria},
  language  = {en}
}
@article{BarminEremenkoOsipovaetal.1999,
  author    = {Barmin, Anatoli V. and Eremenko, Arkadi V. and Osipova, T. and Kurochkin, Iliya and Makower, Alexander and Scheller, Frieder W.},
  title     = {Affinyi fermentometrischeskii analis ingibitorov cholinestarasi},
  year      = {1999},
  language  = {ru}
}
@article{BauerEremenkoEhrentreichFoersteretal.1996,
  author    = {Bauer, Christian G. and Eremenko, A. V. and Ehrentreich-F{\"o}rster, Eva and Bier, Frank Fabian and Makower, Alexander and Halsall, H. B. and Heineman, W. R. and Scheller, Frieder W.},
  title     = {Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid},
  year      = {1996},
  language  = {en}
}
@article{BauerEremenkoKuehnetal.1998,
  author    = {Bauer, Christian G. and Eremenko, A. V. and K{\"u}hn, A. and K{\"u}rzinger, K. and Markower, Alexander and Scheller, Frieder W.},
  title     = {Automated amplifield flow immunoassay for cocaine},
  year      = {1998},
  language  = {en}
}
@article{BauerKuehnGajovicetal.1999,
  author    = {Bauer, Christian G. and K{\"u}hn, A. and Gajovic, Nenad and Skorobogatko, O. V. and Holt, P. J. and Bruce, N. C. and Makower, Alexander and Lowe, Ch. R. and Scheller, Frieder W.},
  title     = {New enzymen sensors for morphine and codeine based on morphine dehydrogenase and laccase},
  year      = {1999},
  language  = {en}
}
@article{BeissenhirtzKwanKoetal.2004,
  author    = {Beissenhirtz, Moritz Karl and Kwan, R. C. H. and Ko, K. M. and Renneberg, Reinhard and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Comparing in vitro electrochemical measurement of superoxide scavenging activity with an in vivo assessment of antioxidant potential in Chinese tonifying herbs},
  year      = {2004},
  abstract  = {The in vitro superoxide scavenging activity (as determined by electrochemical measurement) and the in vivo antioxidant potential (as determined by a mouse model of carbon tetrachloride (CCl4) hepatotoxicity) of methanolic extracts prepared from 10 Chinese tonifying herbs were compared. Electrochemical measurement using a cytochrome c (Cyt. c) sensor showed that all of the tested herbal extracts exhibited a medium superoxide scavenging activity of different potency, as indicated by their IC50 values. The in vivo measurement demonstrated that 80\% of the herbal extracts displayed in vivo antioxidant potential, as assessed by the percentage of protection of the activity of plasma alanine aminotransferases and the hepatic glutathione regeneration capacity under CCl4-intoxicated condition. Although the in vitro antioxidant activity did not correlate quantitatively with the in vivo antioxidant potential, for 8 out of 10 samples a similar tendency was found. The rapid amperometric assessment of antioxidant potential by Cyt. c sensor may offer a convenient and direct method for screening as well as the quality control of herbal products. Copyright (C) 2004 John Wiley Sons, Ltd},
  language  = {en}
}
@article{BeissenhirtzSchellerLisdat2004,
  author    = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Lisdat, Fred},
  title     = {A superoxide sensor based on a multilayer cytochrome c electrode},
  issn      = {0003-2700},
  year      = {2004},
  abstract  = {A novel multilayer cytochrome c electrode for the quantification of superoxide radical concentrations is introduced. The electrode consists of alternating layers of cytochrome c and poly(aniline(sulfonic acid)) on a gold wire electrode. The formation of multilayer structures was proven by SPR experiments. Assemblies with 2-15 protein layers showed electrochemical communication with the gold electrode. For every additional layer, a substantial increase in electrochemically active cytochrome c (cyt. c) was found. For electrodes of more than 10 layers, the increase was more than 1 order of magnitude as compared to monolayer electrode systems. Thermodynamic and kinetic parameters of the electrodes were characterized. The mechanism of electron transfer within the multilayer assembly was studied, with results suggesting a protein-protein electron-transfer model. Electrodes of 2-15 layers were applied to the in vitro quantification of enzymatically generated superoxide, showing superior sensitivity as compared to a monolayer-based sensor. An electrode with 6 cyt. c/PASA layers showed the highest sensitivity of the systems studied, giving an increase in sensitivity of half an order of magnitude versus the that of the monolayer electrode. The stability of the system was optimized using thermal treatment, resulting in no loss in sensor signal or protein loading after 10 successive measurements or 2 days of storage},
  language  = {en}
}
@article{BeissenhirtzSchellerLisdat2003,
  author    = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Immobilized cytochrome c sensor in organic / aqueous media for the characterization of hydrophilic and hydrophobic antioxidants},
  year      = {2003},
  language  = {en}
}
@article{BeissenhirtzSchellerStoeckleinetal.2004,
  author    = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and St{\"o}cklein, Walter F. M. and Kurth, D. and M{\"o}hwald, Helmuth and Lisdat, Fred},
  title     = {Electroactive cytochrome c multilayers within a polyelectrolyte assembly},
  year      = {2004},
  language  = {en}
}
@article{BeissenhirtzSchellerViezzolietal.2006,
  author    = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Viezzoli, Maria Silvia and Lisdat, Fred},
  title     = {Engineered superoxide dismutase monomers for superoxide biosensor applications},
  issn      = {0003-2700},
  doi       = {10.1021/Ac051465g},
  year      = {2006},
  abstract  = {Because of its high reaction rate and specificity, the enzyme superoxide dismutase (SOD) offers great potential for the sensitive quantification of superoxide radicals in electrochemical biosensors. In this work, monomeric mutants of human Cu,Zn-SOD were engineered to contain one or two additional cysteine residues, which could be used to bind the protein to gold surfaces, thus making the use of promotor molecules unnecessary. Six mutants were successfully designed, expressed, and purified. All mutants bound directly to unmodified gold surfaces via the sulfur of the cysteine residues and showed a quasireversible, direct electron transfer to the electrode. Thermodynamic and kinetic parameters of the electron transfer were characterized and showed only slight variations between the individual mutants. For one of the mutants, the interaction with the superoxide radical was studied in more detail. For both partial reactions of the dismutation, an interaction between protein and radical could be shown. In an amperometric biosensorial approach, the SOD-mutant electrode was successfully applied for the detection of superoxide radicals. In the oxidation region, the electrode surpassed the sensitivity of the commonly used cytochrome c electrodes by similar to 1 order of magnitude while not being limited by interferences, but the electrode did not fully reach the sensitivity of dimeric Cu,Zn-SOD immobilized on MPA-modified gold},
  language  = {en}
}
@phdthesis{BenkertSchellerSchoessleretal.2000,
  author    = {Benkert, Alexander and Scheller, Frieder W. and Sch{\"o}ssler, W. and Micheel, Burkhard and Warsinke, Axel},
  title     = {Size exclusion redox-labeled immunoassay (SERI) : a new format for homogeneous amperometric creatinine determination},
  year      = {2000},
  language  = {en}
}
@article{BierEhrentreichFoersterBaueretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Bauer, Christian G. and Scheller, Frieder W.},
  title     = {High sensitive competitive immunodetection of 2,4-dichlorophenoxyacetic acid using enzymatic amplification with electrochemical detection},
  year      = {1996},
  language  = {en}
}
@article{BierEhrentreichFoersterDoellingetal.1997,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and D{\"o}lling, R. and Eremenko, A. V. and Scheller, Frieder W.},
  title     = {A redox-label immunosensor on basis of a bi-enzyme electrode},
  year      = {1997},
  language  = {en}
}
@article{BierEhrentreichFoersterMakoweretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Makower, Alexander and Scheller, Frieder W.},
  title     = {An enzymatic amplification cycle for high sensitive immunoassay},
  year      = {1996},
  language  = {en}
}
@article{BierEhrentreichFoersterScheller1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Amplifying bienzyme cycle-linked immunoassays for determination of 2,4- dichlorphenoxyacetic acid},
  year      = {1996},
  language  = {en}
}
@article{BierEhrentreichFoersterSchelleretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and Makower, Alexander and Eremenko, A. V. and Wollenberger, Ursula and Bauer, Christian G. and Pfeiffer, Dorothea and Micheel, Burkhard},
  title     = {Ultrasensitive biosensors},
  year      = {1996},
  language  = {en}
}
@article{BierFuersteKleinjungetal.1997,
  author    = {Bier, Frank Fabian and F{\"u}rste, J. P. and Kleinjung, Frank and Erdmann, V. A. and Scheller, Frieder W.},
  title     = {Nukleins{\"a}uren als Basis f{\"u}r Biosensoren},
  year      = {1997},
  language  = {de}
}
@article{BierKleinjungScheller1997,
  author    = {Bier, Frank Fabian and Kleinjung, Frank and Scheller, Frieder W.},
  title     = {Real time measurement of nucleic acid hybridization using evanescent wave sensors - step towards the genosensor},
  year      = {1997},
  language  = {en}
}
@article{BierScheller1996,
  author    = {Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Label-free observation of DNA-hybridisation and endonuclease activity on a wave guide surface using a grating coupler},
  year      = {1996},
  language  = {en}
}
@article{BierSchellerKlingbeiletal.1993,
  author    = {Bier, Frank Fabian and Scheller, Frieder W. and Klingbeil, Mandy and Oßwald, U.},
  title     = {Biosensoren und Teststreifen f{\"u}r die Umwelt- und Lebensmittelanalytik : eine {\"U}bersicht},
  year      = {1993},
  language  = {de}
}
@misc{BierYinKleinjungetal.1995,
  author    = {Bier, Frank Fabian and Yin, Wen and Kleinjung, Frank and Scheller, Frieder W.},
  title     = {Molekulare Schichten zur Analyse biochemischer Bindungen und Umsatzreaktionen},
  year      = {1995},
  language  = {de}
}
@article{BistolasChristensonRuzgasetal.2004,
  author    = {Bistolas, Nikitas and Christenson, A. and Ruzgas, T. and Jung, Christiane and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Spectroelectrochemistry of cytochrome P450cam},
  year      = {2004},
  abstract  = {The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved},
  language  = {en}
}
@article{BistolasWollenbergerJungetal.2005,
  author    = {Bistolas, Nikitas and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Cytochrome P450 biosensors : a review},
  year      = {2005},
  abstract  = {Cytochrome P450 (CYP) is a large family of enzymes containing heme as the active site. Since their discovery and the elucidation of their structure, they have attracted the interest of scientist for many years, particularly due to their catalytic abilities. Since the late 1970s attempts have concentrated on the construction and development of electrochemical sensors. Although sensors based on mediated electron transfer have also been constructed, the direct electron transfer approach has attracted most of the interest. This has enabled the investigation of the electrochemical properties of the various isoforms of CYP. Furthermore, CYP utilized to construct biosensors for the determination of substrates important in environmental monitoring, pharmaceutical industry and clinical practice. (c) 2004 Elsevier B. V. All rights reserved},
  language  = {en}
}
@article{BogdanovskayaFridmanTarasevichetal.1994,
  author    = {Bogdanovskaya, V. A. and Fridman, Vadim and Tarasevich, M. R. and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by immobilized peroxidase : the reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme},
  year      = {1994},
  language  = {en}
}
@article{BognarSupalaYarmanetal.2022,
  author    = {Bogn{\´a}r, Zs{\´o}fia and Supala, Eszter and Yarman, Aysu and Zhang, Xiaorong and Bier, Frank Fabian and Scheller, Frieder W. and Gyurcsanyi, R{\´o}bert E.},
  title     = {Peptide epitope-imprinted polymer microarrays for selective protein recognition},
  series = {Chemical science / RSC, Royal Society of Chemistry},
  volume    = {13},
  journal   = {Chemical science / RSC, Royal Society of Chemistry},
  number    = {5},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2041-6539},
  doi       = {10.1039/d1sc04502d},
  pages     = {1263 -- 1269},
  year      = {2022},
  abstract  = {We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.},
  language  = {en}
}
@article{BosserdtGajovicEichelmanScheller2013,
  author    = {Bosserdt, Maria and Gajovic-Eichelman, Nenad and Scheller, Frieder W.},
  title     = {Modulation of direct electron transfer of cytochrome c by use of a molecularly imprinted thin film},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {405},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {20},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-013-7009-8},
  pages     = {6437 -- 6444},
  year      = {2013},
  abstract  = {We describe the preparation of a molecularly imprinted polymer film (MIP) on top of a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold, where the template cytochrome c (cyt c) participates in direct electron transfer (DET) with the underlying electrode. To enable DET, a non-conductive polymer film is electrodeposited from an aqueous solution of scopoletin and cyt c on to the surface of a gold electrode previously modified with MUA. The electroactive surface concentration of cyt c was 0.5 pmol cm(-2). In the absence of the MUA layer, no cyt c DET was observed and the pseudo-peroxidatic activity of the scopoletin-entrapped protein, assessed via oxidation of Ampliflu red in the presence of hydrogen peroxide, was only 30 \% of that for the MIP on MUA. This result indicates that electrostatic adsorption of cyt c by the MUA-SAM substantially increases the surface concentration of cyt c during the electrodeposition step, and is a prerequisite for the productive orientation required for DET. After template removal by treatment with sulfuric acid, rebinding of cyt c to the MUA-MIP-modified electrode occurred with an affinity constant of 100,000 mol(-1) L, a value three times higher than that determined by use of fluorescence titration for the interaction between scopoletin and cyt c in solution. The DET of cyt c in the presence of myoglobin, lysozyme, and bovine serum albumin (BSA) reveals that the MIP layer suppresses the effect of competing proteins.},
  language  = {en}
}
@article{ButtermeyerPhilippMalletal.2002,
  author    = {Buttermeyer, R. and Philipp, A. W. and Mall, J. W. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {In vivo measurement of oxygen derived free radicals during reperfusion injury},
  year      = {2002},
  language  = {en}
}
@article{CasertaZhangYarmanetal.2021,
  author    = {Caserta, Giorgio and Zhang, Xiaorong and Yarman, Aysu and Supala, Eszter and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E. and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms},
  series = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  volume    = {381},
  journal   = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  publisher = {Elsevier},
  address   = {New York, NY [u.a.]},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2021.138236},
  pages     = {8},
  year      = {2021},
  abstract  = {Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague. This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c. To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin. This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target. Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy. This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.},
  language  = {en}
}
@article{ChenStoeckleinSchelleretal.2003,
  author    = {Chen, Jian and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode},
  year      = {2003},
  language  = {en}
}
@article{ChenWollenbergerLisdatetal.2000,
  author    = {Chen, Jian and Wollenberger, Ursula and Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Superoxide sensor based on hemin modified electrode},
  year      = {2000},
  language  = {en}
}
@article{ChenWarsinkeGajovicetal.2000,
  author    = {Chen, Ziping and Warsinke, Axel and Gajovic, Nenad and Große, St. and Hu, J. and Kleber, H.-P. and Scheller, Frieder W.},
  title     = {A D-carnitine dehydrogenase electrode for the assessment of enantiomeric purity of L-carnitine preparations},
  year      = {2000},
  language  = {en}
}
@article{DechtriratGajovicEichelmannWojciketal.2014,
  author    = {Dechtrirat, Decha and Gajovic-Eichelmann, Nenad and Wojcik, Felix and Hartmann, Laura and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Electrochemical displacement sensor based on ferrocene boronic acid tracer and immobilized glycan for saccharide binding proteins and E. coli},
  series = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  volume    = {58},
  journal   = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0956-5663},
  doi       = {10.1016/j.bios.2014.02.028},
  pages     = {1 -- 8},
  year      = {2014},
  abstract  = {Pathogens such as viruses and bacteria use their envelope proteins and their adhesin lectins to recognize the glycan residues presented on the cell surface of the target tissues. This principle of recognition is used in a new electrochemical displacement sensor for the protein concanavalin A (ConA). A gold electrode was first modified with a self-assembled monolayer of a thiolated mannose/OEG conjugate and a ferrocene boroxol derivative was pre-assembled as reporter molecule onto the mannose surface. The novel tracer molecule based on a 2-hydroxymethyl phenyl boronic acid derivative binds even at neutral pH to the saccharides which could expand the application towards biological samples (i.e., urine and feces). Upon the binding of ConA, the tracer was displaced and washed away from the sensor surface leading to a decrease in the electrochemical signal. Using square wave voltammetry (SWV), the concentration of ConA in the sample solution could be determined in the dynamic concentration range established from 38 nmol L-1 to 5.76 mu mol L-1 with a reproducible detection limit of 1 mu g mL(-1) (38 nmol L-1) based on the signal-to-noise ratio (S/N=3) with fast response of 15 min. The new reporter molecule showed a reduced non-specific displacement by BSA and ribonuclease A. The sensor was also successfully transferred to the first proof of principle for the detection of Escherichia coli exhibiting a detection limit of approximately 6 x 102 cells/mL Specificity of the displacement by target protein ConA and E. coli was demonstrated since the control proteins (i.e., BSA and RNaseA) and the control E. coli strain, which lack of type 1 fimbriae, were ineffective. (C) 2014 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@article{EhrentreichFoersterScheller1997,
  author    = {Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Charakterisierung antioxidativer Substanzen mit einem Superoxidsensor},
  year      = {1997},
  language  = {de}
}
@article{EhrentreichFoersterSchellerBier2003,
  author    = {Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Detection of progesterone in whole blood samples},
  year      = {2003},
  abstract  = {The progesterone concentration in blood samples can be utilised as a marker for the diagnosis of early pregnancy, endocrinopathy and virilism. Here, we describe a method for progesterone detection and measurement in whole blood samples by a surface sensitive biosensor used in conjunction with an integrated optical grating coupler. This device determines refractive index changes near the biosensor's surface. Hence, biological species bound to a surface layer can be measured in real-time without any label. For the measurements, we have modified the indirect competitive immonoassay principle. The concentration of the progesterone antibody was kept at 1 µg/ml. Progesterone concentration was determined in buffer solution and whole blood in a range between 0.005 and 10 ng/ml. The detection limit was determined to be 3 pM. The relative standard deviation was calculated to be 3.5\%.},
  language  = {en}
}
@article{EhrentreichFoersterSchellerMcNeil1997,
  author    = {Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and McNeil, C. J.},
  title     = {Biosensor zur in vivo Messung von Superoxidradikalen},
  year      = {1997},
  language  = {de}
}
@article{EhrentreichFoersterShishniashviliSongetal.1998,
  author    = {Ehrentreich-F{\"o}rster, Eva and Shishniashvili, D. and Song, Min Ik and Scheller, Frieder W.},
  title     = {Study of antioxidative substances by means of a ssuperoxide sensor},
  year      = {1998},
  language  = {en}
}
@misc{ErdossyHorvathYarmanetal.2016,
  author    = {Erdossy, Julia and Horvath, Viola and Yarman, Aysu and Scheller, Frieder W. and Gyurcsanyi, Robert E.},
  title     = {Electrosynthesized molecularly imprinted polymers for protein recognition},
  series = {Trends in Analytical Chemistry},
  volume    = {79},
  journal   = {Trends in Analytical Chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0165-9936},
  doi       = {10.1016/j.trac.2015.12.018},
  pages     = {179 -- 190},
  year      = {2016},
  abstract  = {Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@article{EremenkoMakowerBaueretal.1997,
  author    = {Eremenko, A. V. and Makower, Alexander and Bauer, Christian G. and Kurochkin, I. N. and Scheller, Frieder W.},
  title     = {A bienzyme electrode for tyrosine containing peptides determination},
  year      = {1997},
  language  = {en}
}
@article{EremenkoMakowerJinetal.1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Jin, Wen and R{\"u}ger, P. and Scheller, Frieder W.},
  title     = {Biosensor based on an enzyme modified electrode for highly - sensitive measurement of polyphenols},
  year      = {1995},
  language  = {en}
}
@article{EremenkoMakowerScheller1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Measurement of nanomolar diphenols by substrate recycling coupled to a pH- sensitive electrode},
  year      = {1995},
  language  = {en}
}
@article{EremenkoBauerMakoweretal.1998,
  author    = {Eremenko, Arkadi V. and Bauer, Christian G. and Makower, Alexander and Kanne, Beate and Baumgarten, Horst and Scheller, Frieder W.},
  title     = {The development of a non-competitive immunoenzymometric Assay (IEMA) of cocaine},
  year      = {1998},
  language  = {en}
}
@article{FrascavonGrabergFengetal.2010,
  author    = {Frasca, Stefano and von Graberg, Till and Feng, Jiu-Ju and Thomas, Arne and Smarsly, Bernd M. and Weidinger, Inez M. and Scheller, Frieder W. and Hildebrandt, Peter and Wollenberger, Ursula},
  title     = {Mesoporous indium tin oxide as a novel platform for bioelectronics},
  issn      = {1867-3880},
  doi       = {10.1002/cctc.201000047},
  year      = {2010},
  abstract  = {Stable immobilization and reversible electrochemistry of cytochrome c in a tranparent indium tin oxide film with a well-defined mesoporosity (mpITO) is demonstrated. the transparency and good conductivity, in combination with the large surface area of mpITO, allow the incorporation of a high amount of elelctroactive biomolecules and their electrochemical and spectroscopic investigation. UV/Vis and resonance Raman spectroscopy, in combination with direct protein voltammetry are employed for the characterization of cytochrome c immobilized in the mpITO and reveal no perturbant of the structural of the integrity of the redox protein. The potential of this modified material as a biosensor detection of superoxide anions is also demonstrated.},
  language  = {en}
}
@article{FreaneyMacShaneKeavenyetal.1997,
  author    = {Freaney, R. and MacShane, A. and Keaveny, T. V. and MacKenna, M. and Rabenstein, K. and Scheller, Frieder W. and Pfeiffer, Dorothea and Urban, G. and Moser, I. and Jobst, G. and Manz, A. and Verpoorte, E. and Widmer, M. W. and Diamond, D. and Dempsey, E. and deViteri, F. J. S. and Smyth, M.},
  title     = {Novel instrumentation for real-time monitoring using miniaturized flow systems with integrated biosensors},
  year      = {1997},
  language  = {en}
}
@article{FridmanWollenbergerBogdanovskayaetal.2000,
  author    = {Fridman, Vadim and Wollenberger, Ursula and Bogdanovskaya, V. A. and Lisdat, Fred and Ruzgas, T. and Lindgren, A. and Gorton, Lo and Scheller, Frieder W.},
  title     = {Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator},
  year      = {2000},
  language  = {en}
}
@article{GajovicBinyaminWarsinkeetal.2000,
  author    = {Gajovic, Nenad and Binyamin, Gary and Warsinke, Axel and Scheller, Frieder W. and Heller, A.},
  title     = {Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum},
  year      = {2000},
  language  = {en}
}
@article{GajovicHabermuellerWarsinkeetal.1999,
  author    = {Gajovic, Nenad and Haberm{\"u}ller, K. and Warsinke, Axel and Schuhmann, W. and Scheller, Frieder W.},
  title     = {A pyruvate oxidase electrode based on an electrochemically deposited redox polymer},
  year      = {1999},
  language  = {en}
}
@article{GajovicWarsinkeHuangetal.1999,
  author    = {Gajovic, Nenad and Warsinke, Axel and Huang, T. and Schulmeister, Thomas and Scheller, Frieder W.},
  title     = {Characterization and mathematical modelling of a novel bienzyme electrode for L-malate with cofactor recycling},
  year      = {1999},
  language  = {en}
}
@article{GajovicWarsinkeScheller1997,
  author    = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Comparsion of two enzyme sequences for a novel L-malate biosensor},
  year      = {1997},
  language  = {en}
}
@article{GajovicWarsinkeScheller1995,
  author    = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.},
  title     = {A novel multienzyme electrode for the determination of citrate},
  year      = {1995},
  language  = {en}
}
@article{GajovicWarsinkeScheller1998,
  author    = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.},
  title     = {A bienzyme electrode for L-malate based on a novel and general design},
  year      = {1998},
  language  = {en}
}
@article{GeSchellerLisdat2003,
  author    = {Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Electrochemistry of immobilized CuZnSOD and FeSOD and their interaction with superoxide radicals},
  year      = {2003},
  abstract  = {Copper, zinc superoxide dismutase (CuZnSOD) from bovine erythrocytes and iron superoxide dismutase from Escherichia coli (FeSOD) were immobilized on 3-mercaptopropionic acid (MPA)-modified gold electrodes, respectively. The characterization of the SOD electrodes showed a quasi-reversible, electrochemical redox behavior with a formal potential of 47 {\~n} 4 mV and -154 {\~n} 5 mV (vs. Ag/AgCl, 1 M KCl) for surface adsorbed CuZnSOD and FeSOD, respectively. The heterogeneous electron transfer rate constants were determined to be about 65 and 35/s, respectively. Covalent fixation of both SODs was also feasible with only slight changes in the formal potential. The interaction of superoxide radicals (O2-) with the SOD electrode was investigated. No catalytic current could be observed. However, due to the fast cyclic reaction of SOD with superoxide, the communication of the protein with the electrode was strongly influenced. The amperometric detection of superoxide radicals is discussed.},
  language  = {en}
}
@article{GhindilisMakowerBaueretal.1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Bauer, Christian G. and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Determination of p-aminophenol and catecholamines at picomolar concentrations based on recycling enzyme amplification},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Laccase - glucose dehydrogenase recycling enzyme electrode based on potentiometric mediatorless electrocatalytic detection},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Nanomolar determination of the ferrocene derivatives using a recycling enzyme electrode : development of the redox label immunoassay},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Potentiometric enzyme electrodes based on substrate recycling and mediatorless bioelectrocatalysis},
  year      = {1995},
  language  = {en}
}
@article{HalamekMakowerKnoescheetal.2005,
  author    = {Halamek, Jan and Makower, Alexander and Kn{\"o}sche, Kristina and Skladal, Petr and Scheller, Frieder W.},
  title     = {Piezoelectric affinity sensors for cocaine and cholinesterase inhibitors},
  year      = {2005},
  abstract  = {We report here the development of piezoelectric affinity sensors for cocaine and cholinesterase inhibitors based on the formation of affinity complexes between an immobilized cocaine derivative and an anti-cocaine antibody or cholinesterase. For both binding reactions benzoylecgonine-1,8-diamino-3,4-dioxaoctane (BZE-DADOO) was immobilized on the surface of the sensor. For immobilization. pre-conjugated BZE-DADOO with 11-mercaptomonoundecanoic acid (MUA) via 2- (5-norbornen-2,3-dicarboximide)-1,1,3,3-tetramethyluronium-tetrafluoro borate (TNTU) allowed the formation of a chemisorbed monolayer on the piezosensor surface. The detection of cocaine was based oil a competitive assay. The change of frequency measured after 300 s of the binding reaction was used as the signal. The maximum binding of the antibody resulted in a frequency decrease of 35 Hz (with an imprecision 3\%, n = 3) while the presence of 100 pmol I-1 cocaine decreased the binding by 11\%. The limit of detection was consequently below 100 pmol I-1 for cocaine. The total time of one analysis was 15 min. This BZE-DADOO-modified sensor was adapted for the detection of organophosphates. BZE-DADOO - a competitive inhibitor - served as binding element for cholinesterase in a competitive assay. (C) 2004 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{HalamekTellerMakoweretal.2006,
  author    = {Halamek, Jan and Teller, Carsten and Makower, Alexander and Fournier, Didier and Scheller, Frieder W.},
  title     = {EQCN-based cholinesterase biosensors},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2006.03.047},
  year      = {2006},
  abstract  = {The binding of acetylcholinesterase (AChE) to a propidium-modified piezoelectric quartz crystal and its surface enzymatic activity have been investigated. Propidium binds to a site remote to the active center of AChE - the peripheral anionic site (PAS) - which is located on the rim of the gorge to the active site. The gold electrodes of the quartz crystal were first modified with 11-mercaptoundecanoic acid to which propidium was coupled. AChE binding was monitored by a quartz crystal nanobalance (QCN), followed by amperometric activity evaluation of the AChE loaded on the sensor. Interestingly, the binding is strong but does not inhibit AChE. However, an excess of propidium in solution inhibits the immobilized enzyme. The surface enzymatic activities observed depend on the amount of enzyme and differ according to the type and species, i.e. number of enzyme subunits (Electrophorus electricus tetrameric, Drosophila melanogaster mono- and dimeric form - DmAChE). The operational stability and regeneration, effect of propidium in solution and detection limit for substrate for various AChEs were investigated amperometrically.},
  language  = {en}
}
@article{HalamekTellerZeraviketal.2006,
  author    = {Halamek, Jan and Teller, Carsten and Zeravik, Jiri and Fournier, Didier and Makower, Alexander and Scheller, Frieder W.},
  title     = {Characterization of binding of cholinesterases to surface immobilized ligands},
  issn      = {0003-2719},
  doi       = {10.1080/00032710600713107},
  year      = {2006},
  abstract  = {We summarize here the development of various piezoelectric biosensors utilizing cholinesterase (ChE) as the recognition element. In our work we studied the interaction between cholinesterase and its ligands (propidium, carnitine, benzylgonine-1,8-diamino-3,4-dioxaoctane (BZE-DADOO) and paraoxon). The sensor modification was based on a self-assembled monolayer (SAM) of a thiol compound (11-mercaptoundecanoic acid) on the gold electrode and the subsequent covalent coupling of the cholinesterase ligand to this SAM. The ligand-modified piezoelectric sensors were placed in a flow system to allow the on-line monitoring of cholinesterase binding and the enzymatic activity quantification by amperometry. Cholinesterases from different species-acetylcholinesterase (AChE) from Electrophorus electricus , AChE from Drosophila melanogaster , and butyrylcholinesterase (BChE) of human origin-were tested on the various immobilized ligands. Our research allowed the development of a competitive assay for the detection of organophosphates in river water samples using the BZE-DADOO-modified piezosensor. Another direction of research was pointed on the characterization of the interactions between ChE and its ligands. The kinetic binding constants were derived using a one- to-one binding model},
  language  = {en}
}
@article{HalamekWollenbergerStoeckleinetal.2007,
  author    = {Hal{\´a}mek, Jan and Wollenberger, Ursula and St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Development of a biosensor for glycated hemoglobin},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2007.03.059},
  year      = {2007},
  abstract  = {The development of an electrochemical piezoelectric sensor for the detection of glycated hemoglobin is presented. The total hemoglobin (Hb) content is monitored with a mass-sensitive quartz crystal modified with surfactants, and the glycated fraction of the immobilized Hb is determined by subsequent voltarnmetric measurement of the coupled ferroceneboronic acid. Different modifications of the sensor were tested for their hemoglobin binding ability. Deoxycholate (DOCA) was found to be the most suitable among the examined modifiers. Piezoelectric quartz crystals with gold electrodes were modified with DOCA by covalent binding to a pre-formatted 4-aminothiophenol monolayer. The properties of the Hb binding to DOCA and the pH effect on this interaction were studied. In the proposed assay for glycated hemoglobin at first an Hb sample is incubated with ferroceneboronic acid (FcBA), which binds to the fructosyl residue of the glycated Hb. Then this preincubated Hb sample is allowed to interact with the DOCA-modified piezoelectric quartz crystal. The binding is monitored by quartz crystal nanobalance QCN). The amount of FcBA present on the sensor surface is determined by square wave voltammetry. The binding of FcBA results in well-defined peaks with an EO' of +200 mV versus Ag/AgC1 (1 M KC1). The peak height depends on the degree of glycated Hb in the sample ranging from 0\% to 20\% of total Hb. The regeneration of the sensing surface is achieved by pepsin digestion of the deposited Hb. Thus the sensor can be re-used more than 30 times.},
  language  = {en}
}
@article{HalamekWollenbergerStoeckleinetal.2007,
  author    = {Hal{\´a}mek, Jan and Wollenberger, Ursula and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Signal amplification in immunoassays using labeling via boronic acid binding to the sugar moiety of immunoglobulin G : proof of concept for glycated hemoglobin},
  issn      = {0003-2719},
  doi       = {10.1080/00032710701327096},
  year      = {2007},
  abstract  = {A novel electrochemical immunoassay based on the multiple affinity labeling of the indicator antibody with an electro-active tag is presented. The concept is illustrated for the determination of the glycated hemoglobin HbA1c in hemoglobin samples. Hemoglobin is adsorbed to the surfactant-modified surface of a piezoelectric quartz crystal. Whereas the quartz crystal nanobalance is used to validate the total Hb binding, the HbA1c on the sensor surface is recognized by an antibody and quantified electrochemically after the sugar moieties of the antibody have been labeled in-situ with ferroceneboronic acid. The sensitivity of this sensor is about threefold higher than the sensitivity of a hemoglobin sensor, where the ferroceneboronic acid is bound directly to HbA1c.},
  language  = {en}
}
@article{HockScheller2001,
  author    = {Hock, Bertold and Scheller, Frieder W.},
  title     = {Conclusions and outlook},
  year      = {2001},
  language  = {en}
}
@article{HuangWarsinkeKoroljovaSkorobogatkoetal.1999,
  author    = {Huang, T. and Warsinke, Axel and Koroljova-Skorobogatko, O. V. and Makower, Alexander and Kuwana, T. and Scheller, Frieder W.},
  title     = {A bienzyme carbon paste electrode for the sensitive detection of NADPH and the measurement of glucose-6- phosphate dehydrogenase},
  year      = {1999},
  language  = {en}
}
@article{HuangWarsinkeKuwanaetal.1998,
  author    = {Huang, T. and Warsinke, Axel and Kuwana, T. and Scheller, Frieder W.},
  title     = {The determination of L-phenylalanine based on a novel NADH-detecting biosensor},
  year      = {1998},
  language  = {en}
}
@article{IgnatovGeSchelleretal.2001,
  author    = {Ignatov, S. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Detection of the antioxidant activity detection of flavonoids by using superoxide sensor},
  isbn      = {1-58603-164-3},
  year      = {2001},
  language  = {en}
}
@article{IgnatovShishniashviliGeetal.2002,
  author    = {Ignatov, S. and Shishniashvili, D. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Amperometric biosensor based on a functionalized gold electrode for the detection of antioxidants},
  year      = {2002},
  language  = {en}
}
@article{IlievKaishevaSchelleretal.1995,
  author    = {Iliev, I. and Kaisheva, A. and Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Amperometric gas-diffusion / enzyme electrode},
  year      = {1995},
  language  = {en}
}
@article{JetzschmannJagerszkiDechtriratetal.2015,
  author    = {Jetzschmann, Katharina J. and Jagerszki, Gyula and Dechtrirat, Decha and Yarman, Aysu and Gajovic-Eichelmann, Nenad and Gilsing, Hans-Detlev and Schulz, Burkhard and Gyurcsanyi, Robert E. and Scheller, Frieder W.},
  title     = {Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition},
  series = {Advanced functional materials},
  volume    = {25},
  journal   = {Advanced functional materials},
  number    = {32},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201501900},
  pages     = {5178 -- 5183},
  year      = {2015},
  abstract  = {Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid.},
  language  = {en}
}
@article{JetzschmannTankJagerszkietal.2019,
  author    = {Jetzschmann, Katharina J. and Tank, Steffen and Jagerszki, Gyula and Gyurcsanyi, Robert E. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Bio-Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam},
  series = {ChemElectroChem},
  volume    = {6},
  journal   = {ChemElectroChem},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {2196-0216},
  doi       = {10.1002/celc.201801851},
  pages     = {1818 -- 1823},
  year      = {2019},
  abstract  = {A new approach for synthesizing a vectorially imprinted polymer (VIP) is presented for the microbial cytochrome P450cam enzyme. A surface attached binding motif of a natural reaction partner of the target protein, putidaredoxin (Pdx), is the anchor to the underlying transducer. The 15 amino acid peptide anchor, which stems from the largest continuous amino acid chain within the binding site of Pdx was modified: (i) internal cysteines were replaced by serines to prevent disulfide bond formation; (ii) 2 ethylene glycol units were attached to the N-terminus as a spacer region; and (iii) an N-terminal cysteine was added to allow the immobilization on the gold electrode surface. Immobilization on GCE was achieved via an N-(1-pyrenyl)maleimide (NPM) cross-linker. In this way oriented immobilization of P450cam was accomplished by binding it to a peptide-modified gold or glassy carbon electrode (GCE) prior to the electrosynthesis of a polymer nanofilm around the immobilized target. This VIP nanofilm enabled reversible oriented docking of P450cam as it is indicated by the catalytic oxygen reduction via direct electron transfer between the enzyme and the underlying electrode. Catalysis of oxygen reduction by P450cam bound to the VIP-modified GCE was used to measure rebinding to the VIP. The mild coupling of an oxidoreductase with the electrode may be appropriate for realizing electrode-driven substrate conversion by instable P450 enzymes without the need of NADPH co-factor.},
  language  = {en}
}
@article{JetzschmannYarmanRustametal.2018,
  author    = {Jetzschmann, Katharina J. and Yarman, Aysu and Rustam, L. and Kielb, P. and Urlacher, V. B. and Fischer, A. and Weidinger, I. M. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Molecular LEGO by domain-imprinting of cytochrome P450 BM3},
  series = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  volume    = {164},
  journal   = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0927-7765},
  doi       = {10.1016/j.colsurfb.2018.01.047},
  pages     = {240 -- 246},
  year      = {2018},
  abstract  = {Hypothesis: Electrosynthesis of the MIP nano-film after binding of the separated domains or holocytochrome BM3 via an engineered anchor should result in domain-specific cavities in the polymer layer. Experiments: Both the two domains and the holo P450 BM3 have been bound prior polymer deposition via a N-terminal engineered his6-anchor to the electrode surface. Each step of MIP preparation was characterized by cyclic voltammetry of the redox-marker ferricyanide. Rebinding after template removal was evaluated by quantifying the suppression of the diffusive permeability of the signal for ferricyanide and by the NADH-dependent reduction of cytochrome c by the reductase domain (BMR). Findings: The working hypothesis is verified by the discrimination of the two domains by the respective MIPs: The holoenzyme P450 BM3 was ca. 5.5 times more effectively recognized by the film imprinted with the oxidase domain (BMO) as compared to the BMR-MIP or the non-imprinted polymer (NIP). Obviously, a cavity is formed during the imprinting process around the hiss-tag-anchored BMR which cannot accommodate the broader BMO or the P450 BM3. The affinity of the MIP towards P450 BM3 is comparable with that to the monomer in solution. The hiss-tagged P450 BM3 binds (30 percent) stronger which shows the additive effect of the interaction with the MIP and the binding to the electrode.},
  language  = {en}
}
@article{JinBernhardtStoeckleinetal.1998,
  author    = {Jin, Wen and Bernhardt, Rita and St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Direct electron transfer of adrenodoxin-a [2Fe-2S] protein-- and its mutants on modified gold electrode},
  year      = {1998},
  language  = {en}
}
@article{JinWollenbergerBieretal.1995,
  author    = {Jin, Wen and Wollenberger, Ursula and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Construction and characterization of multi-layer-enzyme electrode : covalent binding of quinoprotein glucose dehydrogenase onto gold electrodes},
  year      = {1995},
  language  = {en}
}
@article{JinWollenbergerKaergeletal.1997,
  author    = {Jin, Wen and Wollenberger, Ursula and K{\"a}rgel, E. and Schunck, W.-H. and Scheller, Frieder W.},
  title     = {Electrochemical investigation of the intermolecular electron transfer between cytochrome c and NADPH-cytochrome P450-reductase},
  year      = {1997},
  language  = {en}
}
@article{JinWollenbergerScheller1998,
  author    = {Jin, Wen and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {PQQ as redox shuttle for quinoprotein glucose dehydrogenase},
  year      = {1998},
  language  = {en}
}
@article{JuLiuGeetal.2000,
  author    = {Ju, Huangxian and Liu, Songqin and Ge, Bixia and Lisdat, Fred and Scheller, Frieder W.},
  title     = {Electrochemistry of cytochrome c immobilized on colloidal gold modified carbon paste electrodes and its electrocatalytic activity},
  year      = {2000},
  language  = {en}
}
@article{KaishevaIlievKazarevaetal.1996,
  author    = {Kaisheva, A. and Iliev, I. and Kazareva, R. and Christov, S. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Enzyme/gas diffusion electrodes for determination of phenol},
  year      = {1996},
  language  = {en}
}
@article{KappBeissenhirtzGeyeretal.2006,
  author    = {Kapp, Andreas and Beissenhirtz, Moritz Karl and Geyer, F. and Scheller, Frieder W. and Viezzoli, Maria Silvia and Lisdat, Fred},
  title     = {Electrochemical and sensorial behaviour of SOD mutants immobilized on gold electrodes in aqueous / organic solvent mixtures},
  issn      = {1040-0397},
  doi       = {10.1002/elan.200603620},
  year      = {2006},
  language  = {en}
}
@article{KatterleWollenbergerScheller1997,
  author    = {Katterle, Martin and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Electrochemistry of hemoglobin at modified silver electrodes is not a redox-process of iron protoporhyrin IX},
  year      = {1997},
  language  = {en}
}
@article{KirsteinKirsteinSchelleretal.1998,
  author    = {Kirstein, Dieter and Kirstein, Lincoln and Scheller, Frieder W. and Borcherding, H.},
  title     = {Amperometric nitrate biosensors on the basis of Pseudomonas stutzeri nitrate reductase},
  year      = {1998},
  language  = {en}
}
@article{KirsteinKirsteinSchelleretal.1994,
  author    = {Kirstein, Dieter and Kirstein, Lincoln and Scheller, Frieder W. and Dieckmann, St. and Ronnenberg, J. and Beckmann, Dieter and Weckenbrock, E.},
  title     = {Elektroenzymatische Reduktion von Nitrat},
  year      = {1994},
  language  = {de}
}
@article{KleinjungBeierWarsinkeetal.1997,
  author    = {Kleinjung, Frank and Beier, Frank F. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Fibre-optic genosensor for specific determination of femtomolar DNA oligomers},
  year      = {1997},
  language  = {en}
}
@article{KleinjungBierScheller1995,
  author    = {Kleinjung, Frank and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Messungen an Nukleins{\"a}uren mittels evaneszenten Feldes},
  year      = {1995},
  language  = {de}
}
@article{KleinjungEhrentreichFoersterScheller1999,
  author    = {Kleinjung, Frank and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Changing functionality of surfaces by directed self-assembly using oligonucleotides - the oligo-tag},
  year      = {1999},
  language  = {en}
}
@article{KleinjungKlussmannErdmannetal.1998,
  author    = {Kleinjung, Frank and Klußmann, S. and Erdmann, V. A. and Scheller, Frieder W. and F{\"u}rste, J. P. and Bier, Frank Fabian},
  title     = {Novel binders in biosensorics : hight affinity RNA for smal analytes},
  year      = {1998},
  language  = {en}
}
@article{KleuserStoeckleinPieperFuerstetal.2004,
  author    = {Kleuser, U. and St{\"o}cklein, Walter F. M. and Pieper-F{\"u}rst, U. and Scheller, Frieder W.},
  title     = {Partikelverst{\"a}rkte Oberfl{\"a}chenplasmonresonanz f{\"u}r die Quantifizierung von Matrix Metalloproteinase-2},
  year      = {2004},
  language  = {de}
}
@article{KnoescheHalamekMakoweretal.2003,
  author    = {Kn{\"o}sche, Kristina and Hal{\´a}mek, Jan and Makower, Alexander and Fournier, Didier and Scheller, Frieder W.},
  title     = {Molecular recognition of cocaine by acetylcholinesterases for affinity purification and bio-sensing},
  year      = {2003},
  language  = {en}
}
@article{KrylovBeissenhirtzAdamzigetal.2004,
  author    = {Krylov, Andrey V. and Beissenhirtz, Moritz Karl and Adamzig, Holger and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Thick-film electrodes for measurement of superoxide and hydrogen peroxide based on direct protein-electrode contacts},
  year      = {2004},
  abstract  = {Cytochrome c was immobilized on screen-printed thick-film gold electrodes by a self-assembly approach using mixed monolayers of mercaptoundecanoic acid and mercaptoundecanol. Cyclic voltammetry revealed quasi-reversible electrochemical behavior of the covalently fixed protein with a formal potential of +10 mV vs. Ag/AgCl. Polarized at +150 mV vs. Ag/AgCl the electrode was found to be sensitive to superoxide radicals in the range 300-1200 nmol L-1. Compared with metal needle electrodes sensitivity and reproducibility could be improved and combined with the easiness of preparation. This allows the fabrication of disposable sensors for nanomolar superoxide concentrations. By changing the electrode potential the sensor can be switched from response to superoxide radicals to hydrogen peroxide-another reactive oxygen species. H2O2 sensitivity can be provided in the range 10-1000 mumol L-1 which makes the electrode suitable for oxidative stress studies},
  language  = {en}
}
@article{KroeningSchellerWollenbergeretal.2004,
  author    = {Kr{\"o}ning, Steffen and Scheller, Frieder W. and Wollenberger, Ursula and Lisdat, Fred},
  title     = {Myoglobin-Clay Electrode for Nitric Oxide (NO) Detection in Solution},
  year      = {2004},
  language  = {en}
}
@article{KulysDrungilieneWollenbergeretal.1997,
  author    = {Kulys, J. and Drungiliene, A. and Wollenberger, Ursula and Krikstopaitis, K. and Scheller, Frieder W.},
  title     = {Electroanalytical determination of peroxidases and laccases on carbon paste electrodes},
  year      = {1997},
  language  = {en}
}
@article{KulysDrungilieneWollenbergeretal.1998,
  author    = {Kulys, J. and Drungiliene, A. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Membrane covered carbon paste electrode for the electrochemical determination of perioxidase and microperoxidase in a flow system},
  year      = {1998},
  language  = {en}
}
@article{KulysKrikstopaitisSchelleretal.2004,
  author    = {Kulys, J. and Krikstopaitis, K. and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Electrochemical parameters of phenoxazine derivatives in solution and at monolayer-modified gold electrodes},
  year      = {2004},
  abstract  = {Electrochemical properties of beta-(10-phenoxazinyl) propylamine (APPX) and beta-(10-phenoxazinyl) propionic acid (PPX) have been studied in solution, and in immobilized state on gold electrodes modified with monolayers of cystamine and mercaptoundecanoic acid. A reversible diffusion-controlled process of APPX and PPX was observed at a bare gold electrode. The electrochemical conversion of both compounds at modified gold electrodes was a quasireversible diffusion-controlled process. The redox potential of immobilized APPX (443 mV) was similar to the potential in solution, while the value of the immobilized PPX was 131 mV higher than in solution. The immobilized mediators were electrocatalytically active in the fungal peroxidase-catalyzed hydrogen peroxide reduction},
  language  = {en}
}
@article{LehmannWollenbergerBrigeliusFloheetal.1998,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by a selenoenzyme},
  year      = {1998},
  language  = {en}
}
@article{LehmannWollenbergerBrigeliusFloheetal.2001,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide},
  year      = {2001},
  language  = {en}
}
@article{LeiLisdatWollenbergeretal.1999,
  author    = {Lei, Chenghong and Lisdat, Fred and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Cytochrome c : Clay-modified electrode},
  year      = {1999},
  language  = {en}
}
@article{LeiWollenbergerBistolasetal.2002,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Bistolas, Nikitas and Guiseppi-Eli, A. and Scheller, Frieder W.},
  title     = {Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles},
  year      = {2002},
  language  = {en}
}
@article{LeiWollenbergerJungetal.2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Clay-bridged electron transfer between cytochrome P450(cam) and electrode},
  year      = {2000},
  language  = {en}
}
@article{LeiWollenbergerScheller2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Clay based direct electrochemistry of myoglobin},
  year      = {2000},
  language  = {en}
}
@article{LettauGajovicEichelmannKwaketal.2004,
  author    = {Lettau, Kristian and Gajovic-Eichelmann, N. and Kwak, Young-Keun and Scheller, Frieder W. and Warsinke, Axel},
  title     = {Hydroxylasen und katalytische Polymere f{\"u}r Biochips},
  year      = {2004},
  language  = {de}
}
@article{LettauWarsinkeKatterleetal.2006,
  author    = {Lettau, Kristian and Warsinke, Axel and Katterle, Martin and Danielsson, Bengt and Scheller, Frieder W.},
  title     = {A bifunctional molecularly imprinted polymer (MIP): analysis of binding and catalysis by a thermistor},
  doi       = {10.1002/anie.200601796},
  year      = {2006},
  abstract  = {Binding or catalysis? Both can be distinguished with a molecularly imprinted polymer (MIP) by the different patterns of heat generation. The catalytically active sites, like in the corresponding enzyme, generate a steady-state temperature increase. Thus, enzyme-like catalysis and antibody-analogue binding are analyzed simultaneously in a bifunctional MIP for the first time (see scheme).},
  language  = {en}
}