@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{SchellerLettau2003,
  author    = {Scheller, Frieder W. and Lettau, Kristian},
  title     = {Biomimetische Rezeptoren und Biochips},
  year      = {2003},
  language  = {de}
}
@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{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{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{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{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{Scheller2002,
  author    = {Scheller, Frieder W.},
  title     = {Analytische Biochemie : Entwicklung von Biosensoren und Biochips},
  year      = {2002},
  language  = {de}
}
@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}
}
@misc{YarmanJetzschmannNeumannetal.2017,
  author    = {Yarman, Aysu and Jetzschmann, Katharina J. and Neumann, Bettina and Zhang, Xiaorong and Wollenberger, Ulla and Cordin, Aude and Haupt, Karsten and Scheller, Frieder W.},
  title     = {Enzymes as tools in MIP-sensors},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1098},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47464},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-474642},
  pages     = {18},
  year      = {2017},
  abstract  = {Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.},
  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}
}
@misc{YarmanScheller2020,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {How reliable is the electrochemical readout of MIP-sensors?},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  number    = {960},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47160},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-471608},
  pages     = {25},
  year      = {2020},
  abstract  = {Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.},
  language  = {en}
}
@misc{YarmanJetzschmannNeumannetal.2017,
  author    = {Yarman, Aysu and Jetzschmann, Katharina J. and Neumann, Bettina and Zhang, Xiaorong and Wollenberger, Ulla and Cordin, Aude and Haupt, Karsten and Scheller, Frieder W.},
  title     = {Enzymes as Tools in MIP-Sensors},
  series = {Chemosensors},
  volume    = {5},
  journal   = {Chemosensors},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2227-9040},
  doi       = {10.3390/chemosensors5020011},
  pages     = {16},
  year      = {2017},
  abstract  = {Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.},
  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{ZhangYarmanErdossyetal.2018,
  author    = {Zhang, Xiaorong and Yarman, Aysu and Erdossy, Julia and Katz, Sagie and Zebger, Ingo and Jetzschmann, Katharina J. and Altintas, Zeynep and Wollenberger, Ulla and Gyurcsanyi, Robert E. and Scheller, Frieder W.},
  title     = {Electrosynthesized MIPs for transferrin},
  series = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  volume    = {105},
  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.2018.01.011},
  pages     = {29 -- 35},
  year      = {2018},
  abstract  = {Molecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.},
  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}
}
@misc{SchellerZhangYarmanetal.2019,
  author    = {Scheller, Frieder W. and Zhang, Xiaorong and Yarman, Aysu and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E.},
  title     = {Molecularly imprinted polymer-based electrochemical sensors for biopolymers},
  series = {Current opinion in electrochemistry},
  volume    = {14},
  journal   = {Current opinion in electrochemistry},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {2451-9103},
  doi       = {10.1016/j.coelec.2018.12.005},
  pages     = {53 -- 59},
  year      = {2019},
  abstract  = {Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one 'separation plate'; thus, the selectivity does not reach the values of 'bulk' measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an 'overall apparent' signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.},
  language  = {en}
}
@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}
}
@misc{YarmanKurbanogluJetzschmannetal.2018,
  author    = {Yarman, Aysu and Kurbanoglu, Sevinc and Jetzschmann, Katharina J. and Ozkan, Sibel A. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Electrochemical MIP-Sensors for Drugs},
  series = {Current Medicinal Chemistry},
  volume    = {25},
  journal   = {Current Medicinal Chemistry},
  number    = {33},
  publisher = {Bentham Science Publishers LTD},
  address   = {Sharjah},
  issn      = {0929-8673},
  doi       = {10.2174/0929867324666171005103712},
  pages     = {4007 -- 4019},
  year      = {2018},
  abstract  = {In order to replace bio-macromolecules by stable synthetic materials in separation techniques and bioanalysis biomimetic receptors and catalysts have been developed: Functional monomers are polymerized together with the target analyte and after template removal cavities are formed in the "molecularly imprinted polymer" (MIP) which resemble the active sites of antibodies and enzymes. Starting almost 80 years ago, around 1,100 papers on MIPs were published in 2016. Electropolymerization allows to deposit MIPs directly on voltammetric electrodes or chips for quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). For the readout of MIPs for drugs amperometry, differential pulse voltammetry (DPV) and impedance spectroscopy (EIS) offer higher sensitivity as compared with QCM or SPR. Application of simple electrochemical devices allows both the reproducible preparation of MIP sensors, but also the sensitive signal generation. Electrochemical MIP-sensors for the whole arsenal of drugs, e.g. the most frequently used analgesics, antibiotics and anticancer drugs have been presented in literature and tested under laboratory conditions. These biomimetic sensors typically have measuring ranges covering the lower nano-up to millimolar concentration range and they are stable under extreme pH and in organic solvents like nonaqueous extracts.},
  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}
}
@misc{OzcelikayKurbanogluZhangetal.2019,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Zhang, Xiaorong and S{\"o}z, {\c{C}}ağla Kosak and Wollenberger, Ulla and Ozkan, Sibel A. and Yarman, Aysu and Scheller, Frieder W.},
  title     = {Electrochemical MIP Sensor for Butyrylcholinesterase},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1138},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-50185},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-501854},
  pages     = {13},
  year      = {2019},
  abstract  = {Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range.},
  language  = {en}
}
@misc{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1046},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47617},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-476173},
  pages     = {10},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@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{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{SchellerBier2003,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Biosensoren},
  year      = {2003},
  language  = {de}
}
@article{SchellerBier2004,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Analytical Biochemistry (Editorial)},
  year      = {2004},
  language  = {en}
}
@article{SchellerBauerMakoweretal.2002,
  author    = {Scheller, Frieder W. and Bauer, Christian G. and Makower, Alexander and Wollenberger, Ursula and Warsinke, Axel and Bier, Frank Fabian},
  title     = {Immunoassays using enzymatic amplification electrodes},
  isbn      = {0-7484-0791-X},
  year      = {2002},
  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{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{SchmidtMatthesSchelleretal.2001,
  author    = {Schmidt, Peter Michael and Matthes, E. and Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Nachweis der Telomeraseaktivit{\"a}t in Zellkulturen mittels eines faseroptischen Sensors},
  year      = {2001},
  language  = {de}
}
@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{SchellerBier2002,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Trends in der Bioanalytik},
  year      = {2002},
  language  = {de}
}
@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{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{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{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{StoeckleinMakowerBieretal.1997,
  author    = {St{\"o}cklein, Walter F. M. and Makower, Alexander and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Enzyme sensors and enzyme amplifification systems},
  year      = {1997},
  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{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{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{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{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{SchellerMakowerBieretal.1995,
  author    = {Scheller, Frieder W. and Makower, Alexander and Bier, Frank Fabian and Wollenberger, Ursula and Ghindilis, A. L. and Eremenko, A. V. and Pfeiffer, Dorothea},
  title     = {Enzymsensoren zur Bestimmung subnanomolarer Konzentrationen},
  year      = {1995},
  language  = {de}
}
@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{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{SchellerBierPfeiffer1995,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian and Pfeiffer, Dorothea},
  title     = {Biosensoren : Grundlagen und Anwendungen},
  year      = {1995},
  language  = {de}
}
@article{SchellerMakowerGhindilisetal.1995,
  author    = {Scheller, Frieder W. and Makower, Alexander and Ghindilis, A. L. and Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Wollenberger, Ursula and Bauer, Christian G. and Micheel, Burkhard and Pfeiffer, Dorothea and Szeponik, Jan and Michael, N. and Kaden, H.},
  title     = {Enzyme sensors for subnanomolar concentrations},
  year      = {1995},
  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}
}
@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{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{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{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{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{SchellerYarmanBachmannetal.2014,
  author    = {Scheller, Frieder W. and Yarman, Aysu and Bachmann, Till and Hirsch, Thomas and Kubick, Stefan and Renneberg, Reinhard and Schumacher, Soeren and Wollenberger, Ursula and Teller, Carsten and Bier, Frank Fabian},
  title     = {Future of biosensors: a personal view},
  series = {Advances in biochemical engineering, biotechnology},
  volume    = {140},
  journal   = {Advances in biochemical engineering, biotechnology},
  editor    = {Gu, MB and Kim, HS},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {978-3-642-54143-8; 978-3-642-54142-1},
  issn      = {0724-6145},
  doi       = {10.1007/10_2013_251},
  pages     = {1 -- 28},
  year      = {2014},
  abstract  = {Biosensors representing the technological counterpart of living senses have found routine application in amperometric enzyme electrodes for decentralized blood glucose measurement, interaction analysis by surface plasmon resonance in drug development, and to some extent DNA chips for expression analysis and enzyme polymorphisms. These technologies have already reached a highly advanced level and need minor improvement at most. The dream of the "100-dollar' personal genome may come true in the next few years provided that the technological hurdles of nanopore technology or of polymerase-based single molecule sequencing can be overcome. Tailor-made recognition elements for biosensors including membrane-bound enzymes and receptors will be prepared by cell-free protein synthesis. As alternatives for biological recognition elements, molecularly imprinted polymers (MIPs) have been created. They have the potential to substitute antibodies in biosensors and biochips for the measurement of low-molecular-weight substances, proteins, viruses, and living cells. They are more stable than proteins and can be produced in large amounts by chemical synthesis. Integration of nanomaterials, especially of graphene, could lead to new miniaturized biosensors with high sensitivity and ultrafast response. In the future individual therapy will include genetic profiling of isoenzymes and polymorphic forms of drug-metabolizing enzymes especially of the cytochrome P450 family. For defining the pharmacokinetics including the clearance of a given genotype enzyme electrodes will be a useful tool. For decentralized online patient control or the integration into everyday "consumables' such as drinking water, foods, hygienic articles, clothing, or for control of air conditioners in buildings and cars and swimming pools, a new generation of "autonomous' biosensors will emerge.},
  language  = {en}
}
@article{StoeckleinWarsinkeScheller1997,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides},
  year      = {1997},
  language  = {en}
}
@article{SchellerSchubertFederowitz1997,
  author    = {Scheller, Frieder W. and Schubert, Frank and Federowitz, J.},
  title     = {Present state and frontiers in biosensorics},
  year      = {1997},
  language  = {en}
}
@article{StoeckleinScheller1997,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Enzymes and antibodies in organic media : analytical applications},
  year      = {1997},
  language  = {en}
}
@article{WollenbergerLisdatScheller1997,
  author    = {Wollenberger, Ursula and Lisdat, Fred and Scheller, Frieder W.},
  title     = {Enzymatic substrade recycling electrodes},
  year      = {1997},
  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{XieTangWollenbergeretal.1997,
  author    = {Xie, B. and Tang, X. and Wollenberger, Ursula and Johansson, G. and Gorton, Lo and Scheller, Frieder W. and Danielsson, B.},
  title     = {Hybrid biosensor for simultaneous electrochemical and thermal detection},
  year      = {1997},
  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{SzeponikMoellerPfeifferetal.1997,
  author    = {Szeponik, Jan and M{\"o}ller, B. and Pfeiffer, Dorothea and Lisdat, Fred and Wollenberger, Ursula and Makower, Alexander and Scheller, Frieder W.},
  title     = {Ultrasensitive bienzyme sensor for adrenaline},
  year      = {1997},
  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{WelzelKossmehlEngelmannetal.1997,
  author    = {Welzel, H.-P. and Kossmehl, G. and Engelmann, G. and Neumann, B. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins},
  year      = {1997},
  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{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{EhrentreichFoersterScheller1997,
  author    = {Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Charakterisierung antioxidativer Substanzen mit einem Superoxidsensor},
  year      = {1997},
  language  = {de}
}
@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{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{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{WollenbergerDrungilieneStoeckleinetal.1996,
  author    = {Wollenberger, Ursula and Drungiliene, A. and St{\"o}cklein, Walter F. M. and Kulys, J. and Scheller, Frieder W.},
  title     = {Direct electrocatalytic determination of dissolved peroxidases},
  year      = {1996},
  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{MakowerEremenkoStrefferetal.1996,
  author    = {Makower, Alexander and Eremenko, A. V. and Streffer, Katrin and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds},
  year      = {1996},
  language  = {en}
}
@article{SpricigoRichterLeimkuehleretal.2010,
  author    = {Spricigo, Roberto and Richter, Claudia and Leimk{\"u}hler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Sulfite biosensor based on osmium redox polymer wired sulfite oxidase},
  issn      = {0927-7757},
  doi       = {10.1016/j.colsurfa.2009.09.001},
  year      = {2010},
  abstract  = {A biosensor, based on a redoxactive osmium polymer and sulfite oxidase on screen-printed electrodes, is presented here as a promising method for the detection of sulfite. A catalytic oxidative current was generated when a sample containing sulfite was pumped over the carbon screen-printed electrode modified with osmium redox polymer wired sulfite oxidase. A stationary value was reached after approximately 50 s and a complete measurement lasted no more than 3 min. The electrode polarized at -0.1 V (vs. Ag vertical bar AgCl 1M KCl) permits minimizing the influence of interfering substances, since these compounds can be unspecific oxidized at higher potentials. Because of the good stability of the protein film on the electrode surface, a well functioning biosensor-flow system was possible to construct. The working stability and reproducibility were further enhanced by the addition of bovine serum albumin generating a more long-term stable and biocompatible protein environment. The optimized biosensor showed a stable signal for more than a week of operation and a coefficient of variation of 4.8\% for 12 successive measurements. The lower limit of detection of the sensor was 0.5 mu M sulfite and the response was linear until 100 mu M. The high sensitivity permitted a 1:500 dilution of wine samples. The immobilization procedure and the operational conditions granted minimized interferences. Additionally, repeating the immobilization procedure to form several layers of wired SO further increased the sensitivity of such a sensor. Finally. the applicability of the developed sulfite biosensor was tested on real samples, such as white and red wines.},
  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{PaeschkeHintscheWollenbergeretal.1995,
  author    = {Paeschke, Manfred and Hintsche, Rainer and Wollenberger, Ursula and Jin, Wen and Scheller, Frieder W.},
  title     = {Dynamic redox recycling of cytochrome c},
  issn      = {0022-0728},
  year      = {1995},
  language  = {en}
}
@article{SchellerPfeiffer1994,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Biosensoren : ein wirtschaftlicher Faktor f{\"u}r die Zukunft},
  year      = {1994},
  language  = {de}
}
@article{Scheller1994,
  author    = {Scheller, Frieder W.},
  title     = {Biosensoren : Konzepte, Technologien, Perspektiven},
  year      = {1994},
  language  = {de}
}
@article{SchellerKirsteinPfeiffer1994,
  author    = {Scheller, Frieder W. and Kirstein, Dieter and Pfeiffer, Dorothea},
  title     = {Biosensoren, Konzepte, Technologien, Perspektiven},
  year      = {1994},
  language  = {de}
}
@article{SchellerHeiduschka1994,
  author    = {Scheller, Frieder W. and Heiduschka, P.},
  title     = {Preparation of an electrode surface with a high density of binding sites by an electrochemical reduction of a poly (nitrophenol) film},
  year      = {1994},
  language  = {en}
}
@article{SchmidScheller1994,
  author    = {Schmid, Rolf D. and Scheller, Frieder W.},
  title     = {Biosensoren},
  year      = {1994},
  language  = {de}
}
@article{LisdatDronovMoehwaldetal.2009,
  author    = {Lisdat, Fred and Dronov, Roman and M{\"o}hwald, Helmuth and Scheller, Frieder W. and Kurth, Dirk G.},
  title     = {Self-assembly of electro-active protein architectures on electrodes for the construction of biomimetic signal chains},
  issn      = {1359-7345},
  doi       = {10.1039/B813559b},
  year      = {2009},
  abstract  = {The layer-by-layer adsorption technique based on the consecutive deposition of oppositely charged species is for the preparation of protein multilayers with fully electro-active protein molecules. The methodology was established with cytochrome c and the polyelectrolyte sulfonated polyaniline (PASA). The technique is also useful for the construction of bi-protein architectures confining protein-protein communication to an electrode. Following natural examples of protein complexes with defined signal transfer, cytochrome c was arranged with enzymes such as xanthine oxidase, bilirubin oxidase, laccase, and sulfite oxidase in self-assembled multilayer architectures. Thus, biomimetic signal chains from the enzyme substrate via the enzyme and cytochrome c towards the electrode can be established. Communication between proteins immobilised in multiple layers on the electrode can be achieved by in situ generation of small shuttle molecules or more advantageously by direct interprotein electron transfer. This allows the construction of new sensing electrodes, the properties of which can be tuned by the number of deposited protein layers. The mechanism of electron transfer within such protein assemblies on gold electrodes will be discussed.},
  language  = {en}
}
@article{LoewWollenbergerSchelleretal.2009,
  author    = {Loew, Noya and Wollenberger, Ursula and Scheller, Frieder W. and Katterle, Martin},
  title     = {Direct electrochemistry and spectroelectrochemistry of osmium substituted horseradish peroxidase},
  issn      = {1567-5394},
  doi       = {10.1016/j.bioelechem.2009.03.015},
  year      = {2009},
  abstract  = {In this contribution the substitution of the central protoporphyrin IX iron complex of horseradish peroxidase by the respective osmium porphyrin complex is described. The direct electrochemical reduction of the Os containing horseradish peroxidase (OsHRP) was achieved at ITO and modified glassy carbon electrodes and in combination with spectroscopy revealed the three redox couples (OsHRP)-H-III/(OsHRP)-H-IV, (OsHRP)-H-IV/(OsHRP)-H-V and (OsHRP)-H-V/ (OsHRP)-H-VI. The midpoint potentials differ dependent on the electrode material used with E-1/2 (Os-III/IV) of -0.4 V (ITO) and -0.25 V (GC), E-1/2 (Os-IV/V) of -0.16 V (ITO) and +0.10 V (GC), and E-1/2 (Os-V/VI)of +018 V (ITO), respectively Moreover, with immobilised OsHRP the direct electrocatalytic reduction of hydrogen peroxide and tert-butyl hydroperoxide was observed. In comparison to electrodes modified with native HRP the sensitivity of the OsHRP-electrode for tert-butyl hydroperoxide is higher.},
  language  = {en}
}
@article{SchulmeisterScheller1996,
  author    = {Schulmeister, Thomas and Scheller, Frieder W.},
  title     = {The mathematics of exponential signal amplification in amperometric three enzyme electrodes},
  year      = {1996},
  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{StoeckleinSchellerAbuknesha1995,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Abuknesha, Rhamadan},
  title     = {Effects of organic solvents on semicontinuous immunochemical detection of coumarin derivatives},
  year      = {1995},
  language  = {en}
}
@article{StoeckleinScheller1995,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Einsatz von Enzymen und Antik{\"o}rpern in organischen L{\"o}sungsmitteln},
  year      = {1995},
  language  = {de}
}
@article{WollenbergerHintscheScheller1995,
  author    = {Wollenberger, Ursula and Hintsche, R. and Scheller, Frieder W.},
  title     = {Biosensors for analytical microsystems},
  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{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{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{LisdatWollenbergerPaeschkeetal.1998,
  author    = {Lisdat, Fred and Wollenberger, Ursula and Paeschke, Manfred and Scheller, Frieder W.},
  title     = {Sensitive catecholamine measurement using a monoenzymatic recycling system},
  year      = {1998},
  language  = {en}
}
@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{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{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{RiedelBeyersdorfRadeckNeumannetal.1995,
  author    = {Riedel, K. and Beyersdorf-Radeck, Baerbel and Neumann, B. and Scheller, Frieder W. and Schmid, Rolf D.},
  title     = {Microbial sensors for determination of aromatics and their chloro derivatives. Part III: Determination of chlorinated phenols using a biosensor containing Trichosporon beigelii (cutaneum)},
  year      = {1995},
  language  = {en}
}
@article{ShumyantsevaIvanovBistolasetal.2004,
  author    = {Shumyantseva, V. V. and Ivanov, Y. D. and Bistolas, Nikitas and Scheller, Frieder W. and Archakov, Alexander I. and Wollenberger, Ursula},
  title     = {Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles},
  year      = {2004},
  abstract  = {A method for construction of biosensors with membranous cytochrome P450 isoenzymes was developed based on clay/ detergent/protein mixed films. Thin films of sodium montmorillonite colloid with incorporated cytochrome P450 2134 (CYP2B4) with nonionic detergent were prepared on glassy carbon electrodes. The modified electrodes were electrochemically characterized, and bio-electrocatalytic reactions were followed. CYP2B4 can be reduced fast on clay- modified glassy carbon electrodes in the presence of the nonionic detergent Tween 80. In anaerobic solutions, reversible oxidation and reduction is obtained with a formal potential between -0.292 and - 0.305 V vs Ag/AgCl 1 M KCl depending on the preparation of the biosensor. In air-saturated solution, bio-electrocatalytic reduction currents can be obtained with the CYP2B4-modified electrode on addition of typical substrates such as aminopyrine and benzphetamine. This reaction was suppressed when methyrapone, an inhibitor of P450 reactions, was present. Measurement of product formation also indicates the bioelectrocatialysis by CYP2B4},
  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}
}