@article{ZhangCasertaYarmanetal.2021,
  author    = {Zhang, Xiaorong and Caserta, Giorgio and Yarman, Aysu and Supala, Eszter and Tadjoung Waffo, Armel Franklin and Wollenberger, Ulla and Gyurcsanyi, Robert E. and Zebger, Ingo and Scheller, Frieder W.},
  title     = {"Out of Pocket" protein binding},
  series = {Chemosensors},
  volume    = {9},
  journal   = {Chemosensors},
  number    = {6},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2227-9040},
  doi       = {10.3390/chemosensors9060128},
  pages     = {13},
  year      = {2021},
  abstract  = {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.},
  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{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{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{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}
}
@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{SongBierScheller1995,
  author    = {Song, Min Ik and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {A method to detect superoxide radicals using teflon membrane and superoxide dismutase},
  year      = {1995},
  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{TellerHalamekMakoweretal.2006,
  author    = {Teller, C. and Halamek, Jan and Makower, Alexander and Fournier, Didier and Schulze, H. and Scheller, Frieder W.},
  title     = {A piezoelectric sensor with propidium as a recognition element for cholinesterases},
  doi       = {10.1016/j.snb.2005.02.053},
  year      = {2006},
  abstract  = {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},
  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{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{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{SchellerSchmid2020,
  author    = {Scheller, Frieder W. and Schmid, Rolf},
  title     = {A tribute to Isao Karube (1942-2020) and his influence on sensor science},
  series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica},
  volume    = {412},
  journal   = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica},
  number    = {28},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-020-02946-5},
  pages     = {7709 -- 7711},
  year      = {2020},
  language  = {en}
}
@article{StoellnerSchellerWarsinke2002,
  author    = {Stoellner, Daniela and Scheller, Frieder W. and Warsinke, Axel},
  title     = {Activation of cellulose membranes with 1,1{\"i}-carbonyldiimidazole or 1-cyano-4-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors},
  year      = {2002},
  language  = {en}
}
@article{MakowerBarminMorzunovaetal.1997,
  author    = {Makower, Alexander and Barmin, Anatoli V. and Morzunova, T. and Eremenko, Arkadi V. and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Affinity enzymomoetric assay for detection of organophosphorus compounds},
  year      = {1997},
  language  = {en}
}
@article{LiuWollenbergerHalameketal.2005,
  author    = {Liu, Songqin and Wollenberger, Ursula and Halamek, Jan and Leupold, Eik and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP},
  year      = {2005},
  abstract  = {A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945},
  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{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{PfeifferSchellerSchubertetal.1993,
  author    = {Pfeiffer, Dorothea and Scheller, Frieder W. and Schubert, Florian and Setz, K.},
  title     = {Amperometric enzyme electrodes for lactate and glucose determinations in highly diluted and undiluted media},
  year      = {1993},
  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{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{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{MakWollenbergerSchelleretal.2003,
  author    = {Mak, Karen K. W. and Wollenberger, Ursula and Scheller, Frieder W. and Renneberg, Reinhard},
  title     = {An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration},
  year      = {2003},
  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{LettauWarsinkeLaschewskyetal.2004,
  author    = {Lettau, Kristian and Warsinke, Axel and Laschewsky, Andr{\´e} and Mosbach, K. and Yilmaz, E. and Scheller, Frieder W.},
  title     = {An esterolytic imprinted polymer prepared via a silica-supported transition state analogue},
  year      = {2004},
  abstract  = {In this work we describe a new preparation method for an esterolytic imprinted polymer with catalytic sites on the surface. A template was prepared by immobilizing a transition state analogue (phosphoramidic acid derivative) of an esterolytic reaction within porous silica particles. Polymerization within the pores was carried out using 4- vinylimidazole as a functional monomer and divinylbenzene as a cross-linker. The polymer was released by dissolution of the silica support with hydrofluoric acid and catalytic properties were studied by incubation with three different 4- nitrophenylesters and spectrophotometric determination of the released 4-nitrophenol. For 4-nitrophenyl acetate an activity of 211 nmol min(-1) mg(-1) and a K-m value of 2.2 mmol L-1 was obtained},
  language  = {en}
}
@article{LisdatUtepbergenovHaseloffetal.2001,
  author    = {Lisdat, Fred and Utepbergenov, D. and Haseloff, R. F. and Blasig, Ingolf E. and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Brigelius-Floh{\´e}, Regina},
  title     = {An optical method for the detection of oxidative stress using protein-RNA interaction},
  year      = {2001},
  language  = {en}
}
@article{SchellerBier2004,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Analytical Biochemistry (Editorial)},
  year      = {2004},
  language  = {en}
}
@book{WollenbergerRennebergBieretal.2003,
  author    = {Wollenberger, Ursula and Renneberg, Reinhard and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Analytische Biochemie : eine praktische Einf{\"u}hrung in das Messen mit Biomolek{\"u}len},
  publisher = {John Wiley \& Sons},
  address   = {Hoboken},
  isbn      = {3-527-30166-6},
  pages     = {222 S.},
  year      = {2003},
  language  = {de}
}
@article{Scheller2002,
  author    = {Scheller, Frieder W.},
  title     = {Analytische Biochemie : Entwicklung von Biosensoren und Biochips},
  year      = {2002},
  language  = {de}
}
@article{SchellerTiepnerWarsinke2004,
  author    = {Scheller, Frieder W. and Tiepner, K. and Warsinke, Axel},
  title     = {Anwendung von Biosensoren in der Lebensmittelanalytik},
  isbn      = {3-89947-120-2},
  year      = {2004},
  language  = {de}
}
@article{StrefferKaatzBaueretal.1998,
  author    = {Streffer, Katrin and Kaatz, Helvi and Bauer, Christian G. and Makower, Alexander and Schulmeister, Thomas and Scheller, Frieder W. and Peter, Martin G. and Wollenberger, Ursula},
  title     = {Application of a sensitive catechol detector for determination of tyrosinase inhibitors},
  year      = {1998},
  language  = {en}
}
@article{SchellerLisdatWollenberger2005,
  author    = {Scheller, Frieder W. and Lisdat, Fred and Wollenberger, Ursula},
  title     = {Application of electrically contacted enzymes for biosensors},
  isbn      = {3-527- 30690-0},
  year      = {2005},
  language  = {en}
}
@article{OzcelikayKurbanogluYarmanetal.2020,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Yarman, Aysu and Scheller, Frieder W. and Ozkan, Sibel A.},
  title     = {Au-Pt nanoparticles based molecularly imprinted nanosensor for electrochemical detection of the lipopeptide antibiotic drug Daptomycin},
  series = {Sensors and actuators : B, Chemical},
  volume    = {320},
  journal   = {Sensors and actuators : B, Chemical},
  publisher = {Elsevier Science},
  address   = {Amsterdam},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2020.128285},
  pages     = {7},
  year      = {2020},
  abstract  = {In this work, a novel electrochemical molecularly imprinted polymer (MIP) sensor for the detection of the lipopeptide antibiotic Daptomycin (DAP) is presented which integrates gold decorated platinum nanoparticles (Au-Pt NPs) into the nanocomposite film. The sensor was prepared by electropolymerization of o-phenylenediamine (o-PD) in the presence of DAP using cyclic voltammetry. Cyclic voltammetry and differential pulse voltammetry were applied to follow the changes in the MIP-layer related to rebinding and removal of the target DAP by using the redox marker [Fe(CN)(6)](3-/4-). Under optimized operational conditions, the MIP/Au-Pt NPs/ GCE nanosensor exhibits a linear response in the range of 1-20 pM towards DAP. The limit of detection and limit of quantification were determined to be 0.161pM +/- 0.012 and 0.489pM +/- 0.012, respectively. The sensitivity towards the antibiotics Vancomycin and Erythromycin and the amino acids glycine and tryptophan was below 7 percent as compared with DAP. Moreover, the nanosensor was also successfully used for the detection of DAP in deproteinated human serum samples.},
  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{SchellerScheller1996,
  author    = {Scheller, Frieder W. and Scheller, A.},
  title     = {Bi-Enzymelektrode zur Messung von Sorbitol in pharmazeutischen Produkten},
  year      = {1996},
  language  = {de}
}
@article{SchellerYarman2015,
  author    = {Scheller, Frieder W. and Yarman, Aysu},
  title     = {Bio vs. Mimetika in der Bioanalytik},
  series = {Biochemie und analytische Biochemie},
  volume    = {4},
  journal   = {Biochemie und analytische Biochemie},
  number    = {2},
  issn      = {2161-1009},
  pages     = {2},
  year      = {2015},
  abstract  = {Nat{\"u}rliche Evolution hat geschaffenBiopolymereauf der Basis von Aminos{\"a}uren undNukleotidezeigt hohe chemische Selektivit{\"a}t und katalytische Kraft. Die molekulare Erkennung durch Antik{\"o}rper und die katalytische Umwandlung der Substratmolek{\"u}le durch Enzyme findet in sogenannten Paratopen oder katalytischen Zentren des Makromolek{\"u}ls statt, die typischerweise 10-15 Aminos{\"a}uren umfassen. Die konzertierte Wechselwirkung zwischen den Reaktionspartnern f{\"u}hrt zu Affinit{\"a}ten bis zu nanomolaren Konzentrationen f{\"u}r die Antigenbindung und n{\"a}hert sich einer Million Ums{\"a}tze pro Sekunde anEnzym-katalysierte Reaktionen.},
  language  = {de}
}
@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{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{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{YarmanNagelGajovicEichelmannetal.2011,
  author    = {Yarman, Aysu and Nagel, Thomas and Gajovic-Eichelmann, Nenad and Fischer, Anna and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by Microperoxidase-11 in a Multilayer Architecture of Chitosan Embedded Gold Nanoparticles},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {23},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {3},
  publisher = {Wiley-Blackwell},
  address   = {Malden},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201000535},
  pages     = {611 -- 618},
  year      = {2011},
  abstract  = {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.},
  language  = {en}
}
@article{SchellerWollenbergerLeietal.2002,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Lei, Chenghong and Jin, Wen and Ge, Bixia and Lehmann, Claudia and Lisdat, Fred and Fridman, Vadim},
  title     = {Bioelectrocatalysis by redox enzymes at modified electrodes},
  year      = {2002},
  language  = {en}
}
@article{SigolaevaMarkowerEremenkoetal.2001,
  author    = {Sigolaeva, L. V. and Markower, Alexander and Eremenko, A. V. and Makhaeva, G. F. and Malygin, V. V. and Kurochkin, I. N. and Scheller, Frieder W.},
  title     = {Bioelectrochemical anaysis of neuropathy targes esterase activity in blood},
  year      = {2001},
  language  = {en}
}
@article{SchellerBierNeumann1994,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian and Neumann, B.},
  title     = {Bioindikation in aquatischen {\"O}kosystemen : Bioindikation in limnischen und k{\"u}stennahen {\"O}kosystemen ; Grundlagen, Verfahren und Methoden},
  publisher = {Fischer},
  address   = {Jena},
  pages     = {S. 380 - 386},
  year      = {1994},
  language  = {de}
}
@article{SchellerLettau2003,
  author    = {Scheller, Frieder W. and Lettau, Kristian},
  title     = {Biomimetische Rezeptoren und Biochips},
  year      = {2003},
  language  = {de}
}
@article{WarsinkeBenkertScheller1996,
  author    = {Warsinke, Axel and Benkert, Alexander and Scheller, Frieder W.},
  title     = {Biomolecular modules for creatinine determination},
  year      = {1996},
  language  = {en}
}
@article{Scheller2000,
  author    = {Scheller, Frieder W.},
  title     = {Biomolekulare Erkennungssysteme f{\"u}r die Biochemische Analytik},
  year      = {2000},
  language  = {de}
}
@article{Scheller2001,
  author    = {Scheller, Frieder W.},
  title     = {Biomolek{\"u}le als Reporter in der Analytik : keine Forschung im Elfenbeinturm},
  year      = {2001},
  language  = {de}
}
@article{StancikMacholanPluhaceketal.1995,
  author    = {Stanc{\´i}k, L. and Machol{\´a}n, L. and Pluhacek, I. and Scheller, Frieder W.},
  title     = {Biosensing of rapeseed glucosinolates using amperometric enzyme electrodes based on membrane-bound glucose oxidase or tyrosinase},
  year      = {1995},
  language  = {en}
}
@article{StancikMacholanScheller1995,
  author    = {Stancik, L. and Machol{\´a}n, L. and Scheller, Frieder W.},
  title     = {Biosensing of tyrosinase inhibitors in nonaqueous solvents},
  year      = {1995},
  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{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{Scheller2000,
  author    = {Scheller, Frieder W.},
  title     = {Biosensor-Stabilit{\"a}t},
  year      = {2000},
  language  = {de}
}
@article{SchellerPfeiffer2000,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Biosensor-Technologie in der Medizin und den Biowissenschaften},
  year      = {2000},
  language  = {de}
}
@article{SchellerBier2003,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Biosensoren},
  year      = {2003},
  language  = {de}
}
@article{SchmidScheller1994,
  author    = {Schmid, Rolf D. and Scheller, Frieder W.},
  title     = {Biosensoren},
  year      = {1994},
  language  = {de}
}
@article{SchellerPfeiffer1994,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Biosensoren : ein wirtschaftlicher Faktor f{\"u}r die Zukunft},
  year      = {1994},
  language  = {de}
}
@article{SchellerBierPfeiffer1995,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian and Pfeiffer, Dorothea},
  title     = {Biosensoren : Grundlagen und Anwendungen},
  year      = {1995},
  language  = {de}
}
@article{Scheller1994,
  author    = {Scheller, Frieder W.},
  title     = {Biosensoren : Konzepte, Technologien, Perspektiven},
  year      = {1994},
  language  = {de}
}
@article{Scheller2001,
  author    = {Scheller, Frieder W.},
  title     = {Biosensoren auf dem Weg zur Biochip-Technologie},
  year      = {2001},
  language  = {de}
}
@article{SchellerBierGajovic1997,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian and Gajovic, Nenad},
  title     = {Biosensoren und Teststreifen f{\"u}r die Umwelt- und Lebensmittelanalytik},
  year      = {1997},
  language  = {de}
}
@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}
}
@article{SchellerKirsteinPfeiffer1994,
  author    = {Scheller, Frieder W. and Kirstein, Dieter and Pfeiffer, Dorothea},
  title     = {Biosensoren, Konzepte, Technologien, Perspektiven},
  year      = {1994},
  language  = {de}
}
@article{Scheller1998,
  author    = {Scheller, Frieder W.},
  title     = {Biosensorik},
  year      = {1998},
  language  = {de}
}
@article{SchellerWarsinkePfeifferetal.2004,
  author    = {Scheller, Frieder W. and Warsinke, Axel and Pfeiffer, Dorothea and Czeponik, J.},
  title     = {Biosensorik / Bioanalytik},
  isbn      = {3-87081-372-5},
  year      = {2004},
  language  = {de}
}
@article{WollenbergerHintscheScheller1995,
  author    = {Wollenberger, Ursula and Hintsche, R. and Scheller, Frieder W.},
  title     = {Biosensors for analytical microsystems},
  year      = {1995},
  language  = {en}
}
@article{WarsinkeStancikMacholanetal.1998,
  author    = {Warsinke, Axel and Stancik, L. and Machol{\´a}n, L. and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Biosensors for food analysis : application of biosensors to food requirements},
  isbn      = {0-85404-750-6},
  year      = {1998},
  language  = {en}
}
@article{PfeifferSchellerMcNeiletal.1995,
  author    = {Pfeiffer, Dorothea and Scheller, Frieder W. and McNeil, C. J. and Schulmeister, Thomas},
  title     = {Cascade-like exponential substrate amplification in enzyme sensors},
  year      = {1995},
  language  = {en}
}
@article{MarkowerWollenbergerHoertnageletal.1997,
  author    = {Markower, Alexander and Wollenberger, Ursula and H{\"o}rtnagel, H. and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Catecholamine detection using enzymatic amplification},
  year      = {1997},
  language  = {en}
}
@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{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{StoeckleinWarsinkeMicheeletal.1998,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Micheel, Burkhard and H{\"o}hne, Wolfgang and Woller, Jochen and Kempter, Gerhard and Scheller, Frieder W.},
  title     = {Characterization of a monoclonal antibody and its Fab fragment against diphenylurea hapten with BIA},
  isbn      = {3-8154-3540-4},
  year      = {1998},
  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{LoewSchellerWollenberger2004,
  author    = {Loew, Noya and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Characterization of self-assembling of glucose dehydrogenase in mono- and multilayers on gold electrodes},
  year      = {2004},
  abstract  = {Glucose dehydrogenase (GDH) was assembled electrostatically onto QCM-gold electrodes by their sequential deposition with anionic polyelectrolytes such as PSS and PASA. For the layer-by-layer arrangements both the microgravimetric and the electrochemical sensor signal were followed. Increasing amounts of GDH were deposited by stepwise formation of alternating layers of GDH and PSS or PASA. The mass increase was about 1.88 mug/cm(2) for one GDH/ PASA bilayer and 2.4 mug/cm(2) for a GDH/PSS bilayer. The addition of phenolic compounds resulted in an oxidation current, which could be catalytically increased by the GDH catalysed reaction in the presence of glucose. The system functions as glucose sensor when quinones are present in nonlimiting amount. The amperometric response was already diffusion limited when a single layer of GDH was adsorbed. The sensor sensitivity increased by a factor of 10 when MSA was used instead of MUA as initial electrode modifier},
  language  = {en}
}
@article{NeumannYarmanWollenbergeretal.2014,
  author    = {Neumann, Bettina and Yarman, Aysu and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Characterization of the enhanced peroxidatic activity of amyloid beta peptide-hemin complexes towards neurotransmitters},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {406},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {14},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-014-7822-8},
  pages     = {3359 -- 3364},
  year      = {2014},
  abstract  = {Binding of heme to the amyloid peptides A beta 40/42 is thought to be an initial step in the development of symptoms in the early stages of Alzheimer's disease by enhancing the intrinsic peroxidatic activity of heme. We found considerably higher acceleration of the reaction for the physiologically relevant neurotransmitters dopamine and serotonin than reported earlier for the artificial substrate 3,3',5,5'-tetramethylbenzidine (TMB). Thus, the binding of hemin to A beta peptides might play an even more crucial role in the early stages of Alzheimer's disease than deduced from these earlier results. To mimic complex formation, a new surface architecture has been developed: The interaction between the truncated amyloid peptide A beta 1-16 and hemin immobilized on an aminohexanethiol spacer on a gold electrode has been analyzed by cyclic voltammetry. The resulting complex has a redox pair with a 25 mV more cathodic formal potential than hemin alone.},
  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{LeiWollenbergerScheller2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Clay based direct electrochemistry of myoglobin},
  year      = {2000},
  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{SchellerPfeiffer1997,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Commercial devices based on amperometric biosensors},
  year      = {1997},
  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{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{HockScheller2001,
  author    = {Hock, Bertold and Scheller, Frieder W.},
  title     = {Conclusions and outlook},
  year      = {2001},
  language  = {en}
}
@article{RiedelSabirSchelleretal.2017,
  author    = {Riedel, M. and Sabir, N. and Scheller, Frieder W. and Parak, Wolfgang J. and Lisdat, Fred},
  title     = {Connecting quantum dots with enzymes},
  series = {Nanoscale},
  volume    = {9},
  journal   = {Nanoscale},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2040-3364},
  doi       = {10.1039/c7nr00091j},
  pages     = {2814 -- 2823},
  year      = {2017},
  abstract  = {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).},
  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{PfeifferYangSchelleretal.1997,
  author    = {Pfeiffer, Dorothea and Yang, L. and Scheller, Frieder W. and Kissinger, P. T.},
  title     = {Continous measurement of lactate in microdialysate},
  year      = {1997},
  language  = {en}
}
@article{YarmanScheller2013,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {Coupling biocatalysis with molecular imprinting in a biomimetic sensor},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {52},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {44},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201305368},
  pages     = {11521 -- 11525},
  year      = {2013},
  language  = {en}
}
@article{SchellerBauerMarkoweretal.2001,
  author    = {Scheller, Frieder W. and Bauer, Christian G. and Markower, Alexander and Wollenberger, Ursula and Warsinke, Axel and Bier, Frank Fabian},
  title     = {Coupling of immunoassays with enzymatic recycling electrodes},
  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{SchellerJinEhrentreichFoersteretal.1999,
  author    = {Scheller, Frieder W. and Jin, Wen and Ehrentreich-F{\"o}rster, Eva and Ge, Bixia and Lisdat, Fred and B{\"u}ttemeyer, R. and Wollenberger, Ursula},
  title     = {Cytochrome c based superoxide sensor for in vivo application},
  year      = {1999},
  language  = {en}
}
@misc{YarmanDechtriratBosserdtetal.2015,
  author    = {Yarman, Aysu and Dechtrirat, Decha and Bosserdt, Maria and Jetzschmann, Katharina J. and Gajovic-Eichelmann, Nenad and Scheller, Frieder W.},
  title     = {Cytochrome c-derived hybrid systems based on moleculary imprinted polymers},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {27},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201400592},
  pages     = {573 -- 586},
  year      = {2015},
  abstract  = {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.},
  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{StoeckleinWarsinkeMicheeletal.1997,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Micheel, Burkhard and H{\"o}hne, Wolfgang and Woller, Jochen and Kempter, Gerhard and Scheller, Frieder W.},
  title     = {Detection of diphenylurea derivatives with biospecific interaction analysis (BIA) : Kinetic investigations},
  year      = {1997},
  language  = {en}
}
@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{PieperFuerstKleuserStoeckleinetal.2004,
  author    = {Pieper-F{\"u}rst, U. and Kleuser, U. and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor},
  year      = {2004},
  abstract  = {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},
  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{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{VijgenboomVijgenboomTeppneretal.2001,
  author    = {Vijgenboom, E. and Vijgenboom, E. and Teppner, A. W. J. W. and Makower, Alexander and Scheller, Frieder W. and Canters, Gerard W. and Wollenberger, Ursula},
  title     = {Determination of phenolic compounds using recombinant tyrosinanse from Streptomyces antibioticus},
  year      = {2001},
  language  = {en}
}
@article{Scheller1999,
  author    = {Scheller, Frieder W.},
  title     = {Deutliche Signale setzen [Leitartikel]},
  year      = {1999},
  language  = {de}
}
@article{WollenbergerNeumannScheller1998,
  author    = {Wollenberger, Ursula and Neumann, B. and Scheller, Frieder W.},
  title     = {Development of a biomimetic alkane sensor f},
  year      = {1998},
  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{StoeckleinWarsinkeMicheeletal.1998,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Micheel, Burkhard and Kempter, Gerhard and H{\"o}hne, Wolfgang and Scheller, Frieder W.},
  title     = {Diphenylurea hapten sensing with a monoclonal antibody and its Fab fragment : kinetic and thermodynamic investigations},
  year      = {1998},
  language  = {en}
}