TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Lettau, Kristian
T1  - Biomimetische Rezeptoren und Biochips
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Chen, Jian
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
T1  - Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Ignatov, S.
A1  - Shishniashvili, D.
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
A1  - Lisdat, Fred
T1  - Amperometric biosensor based on a functionalized gold electrode for the detection of antioxidants
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Wollenberger, Ursula
A1  - Bistolas, Nikitas
A1  - Guiseppi-Eli, A.
A1  - Scheller, Frieder W.
T1  - Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Stoellner, Daniela
A1  - Scheller, Frieder W.
A1  - Warsinke, Axel
T1  - Activation of cellulose membranes with 1,1ï-carbonyldiimidazole or 1-cyano-4-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Lei, Chenghong
A1  - Jin, Wen
A1  - Ge, Bixia
A1  - Lehmann, Claudia
A1  - Lisdat, Fred
A1  - Fridman, Vadim
T1  - Bioelectrocatalysis by redox enzymes at modified electrodes
Y1  - 2002
UR  - www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Analytische Biochemie : Entwicklung von Biosensoren und Biochips
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Schmid, Rolf
T1  - A tribute to Isao Karube (1942-2020) and his influence on sensor science
JF  - Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica
KW  - Karube
KW  - Japan
KW  - biosensors
KW  - lifetime achievements
Y1  - 2020
U6  - https://doi.org/10.1007/s00216-020-02946-5
SN  - 1618-2642
SN  - 1618-2650
VL  - 412
IS  - 28
SP  - 7709
EP  - 7711
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Ozcelikay, Goksu
A1  - Kurbanoglu, Sevinc
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
A1  - Ozkan, Sibel A.
T1  - Au-Pt nanoparticles based molecularly imprinted nanosensor for electrochemical detection of the lipopeptide antibiotic drug Daptomycin
JF  - Sensors and actuators : B, Chemical
N2  - 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.
KW  - molecularly imprinted polymer
KW  - Daptomycin
KW  - platinum nanoparticles
KW  - gold
KW  - nanoparticles
KW  - modified electrodes
Y1  - 2020
U6  - https://doi.org/10.1016/j.snb.2020.128285
SN  - 0925-4005
VL  - 320
PB  - Elsevier Science
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Neumann, Bettina
A1  - Zhang, Xiaorong
A1  - Wollenberger, Ulla
A1  - Cordin, Aude
A1  - Haupt, Karsten
A1  - Scheller, Frieder W.
T1  - Enzymes as Tools in MIP-Sensors
JF  - Chemosensors
N2  - Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.
KW  - enzymatic MIP synthesis
KW  - template digestion
KW  - enzyme tracer
KW  - enzymatic analyte conversion
KW  - molecularly imprinted polymers
Y1  - 2017
U6  - https://doi.org/10.3390/chemosensors5020011
SN  - 2227-9040
VL  - 5
PB  - MDPI
CY  - Basel
ER  - 
TY  - JOUR
A1  - Riedel, M.
A1  - Sabir, N.
A1  - Scheller, Frieder W.
A1  - Parak, Wolfgang J.
A1  - Lisdat, Fred
T1  - Connecting quantum dots with enzymes
BT  - mediator-based approaches for the light-directed read-out of glucose and fructose oxidation
JF  - Nanoscale
N2  - The combination of the biocatalytic features of enzymes with the unique physical properties of nanoparticles in a biohybrid system provides a promising approach for the development of advanced bioelectrocatalytic devices. This study describes the construction of photoelectrochemical signal chains based on CdSe/ZnS quantum dot (QD) modified gold electrodes as light switchable elements, and low molecular weight redox molecules for the combination with different biocatalysts. Photoelectrochemical and photoluminescence experiments verify that electron transfer can be achieved between the redox molecules hexacyanoferrate and ferrocene, and the QDs under illumination. Since for both redox mediators a concentration dependent photocurrent change has been found, light switchable enzymatic signal chains are built up with fructose dehydrogenase (FDH) and pyrroloquinoline quinone-dependent glucose dehydrogenase ((PQQ) GDH) for the detection of sugars. After immobilization of the enzymes at the QD electrode the biocatalytic oxidation of the substrates can be followed by conversion of the redox mediator in solution and subsequent detection at the QD electrode. Furthermore, (PQQ) GDH has been assembled together with ferrocenecarboxylic acid on top of the QD electrode for the construction of a funtional biohybrid architecture, showing that electron transfer can be realized from the enzyme over the redox mediator to the QDs and subsequently to the electrode in a completely immobilized fashion. The results obtained here do not only provide the basis for light-switchable biosensing and bioelectrocatalytic applications, but may also open the way for self-driven point-of-care systems by combination with solar cell approaches (power generation at the QD electrode by enzymatic substrate consumption).
Y1  - 2017
U6  - https://doi.org/10.1039/c7nr00091j
SN  - 2040-3364
SN  - 2040-3372
VL  - 9
SP  - 2814
EP  - 2823
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Erdossy, Julia
A1  - Katz, Sagie
A1  - Zebger, Ingo
A1  - Jetzschmann, Katharina J.
A1  - Altintas, Zeynep
A1  - Wollenberger, Ulla
A1  - Gyurcsanyi, Robert E.
A1  - Scheller, Frieder W.
T1  - Electrosynthesized MIPs for transferrin
BT  - Plastibodies or nano-filters?
JF  - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
N2  - Molecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.
KW  - Molecularly imprinted polymer
KW  - Scopoletin
KW  - Transferrin
KW  - Protein adsorption
KW  - Redox marker
Y1  - 2018
U6  - https://doi.org/10.1016/j.bios.2018.01.011
SN  - 0956-5663
SN  - 1873-4235
VL  - 105
SP  - 29
EP  - 35
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Jetzschmann, Katharina J.
A1  - Yarman, Aysu
A1  - Rustam, L.
A1  - Kielb, P.
A1  - Urlacher, V. B.
A1  - Fischer, A.
A1  - Weidinger, I. M.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
T1  - Molecular LEGO by domain-imprinting of cytochrome P450 BM3
JF  - 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
N2  - 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.
KW  - Molecularly imprinted polymers
KW  - Protein imprinting
KW  - Electropolymerization
KW  - Cytochrome P450
Y1  - 2018
U6  - https://doi.org/10.1016/j.colsurfb.2018.01.047
SN  - 0927-7765
SN  - 1873-4367
VL  - 164
SP  - 240
EP  - 246
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Wollenberger, Ulla
A1  - Gyurcsányi, Róbert E.
T1  - Molecularly imprinted polymer-based electrochemical sensors for biopolymers
JF  - Current opinion in electrochemistry
N2  - Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one ‘separation plate’; thus, the selectivity does not reach the values of ‘bulk’ measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an ‘overall apparent’ signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.
KW  - Electropolymerization
KW  - Direct electron transfer
KW  - Redox marker
KW  - Epitope imprinting
KW  - Biomarker
Y1  - 2018
U6  - https://doi.org/10.1016/j.coelec.2018.12.005
SN  - 2451-9103
VL  - 14
SP  - 53
EP  - 59
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Altintas, Zeynep
A1  - Takiden, Aref
A1  - Utesch, Tillmann
A1  - Mroginski, Maria A.
A1  - Schmid, Bianca
A1  - Scheller, Frieder W.
A1  - Süssmuth, Roderich D.
T1  - Integrated approaches toward high-affinity artificial protein binders obtained via computationally simulated epitopes for protein recognition
JF  - Advanced functional materials
N2  - 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.
KW  - artificial protein binders
KW  - cancer markers
KW  - computationally simulated epitopes
KW  - molecular imprinting
KW  - protein recognition
Y1  - 2019
U6  - https://doi.org/10.1002/adfm.201807332
SN  - 1616-301X
SN  - 1616-3028
VL  - 29
IS  - 15
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Kurbanoglu, Sevinc
A1  - Jetzschmann, Katharina J.
A1  - Ozkan, Sibel A.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
T1  - Electrochemical MIP-Sensors for Drugs
JF  - Current Medicinal Chemistry
N2  - In order to replace bio-macromolecules by stable synthetic materials in separation techniques and bioanalysis biomimetic receptors and catalysts have been developed: Functional monomers are polymerized together with the target analyte and after template removal cavities are formed in the "molecularly imprinted polymer" (MIP) which resemble the active sites of antibodies and enzymes. Starting almost 80 years ago, around 1,100 papers on MIPs were published in 2016. Electropolymerization allows to deposit MIPs directly on voltammetric electrodes or chips for quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). For the readout of MIPs for drugs amperometry, differential pulse voltammetry (DPV) and impedance spectroscopy (EIS) offer higher sensitivity as compared with QCM or SPR. Application of simple electrochemical devices allows both the reproducible preparation of MIP sensors, but also the sensitive signal generation. Electrochemical MIP-sensors for the whole arsenal of drugs, e.g. the most frequently used analgesics, antibiotics and anticancer drugs have been presented in literature and tested under laboratory conditions. These biomimetic sensors typically have measuring ranges covering the lower nano-up to millimolar concentration range and they are stable under extreme pH and in organic solvents like nonaqueous extracts.
KW  - Biomimetic sensors
KW  - molecularly imprinted polymers
KW  - drug sensors
KW  - drug imprinting
KW  - electropolymerization
KW  - electrochemical sensors
Y1  - 2018
U6  - https://doi.org/10.2174/0929867324666171005103712
SN  - 0929-8673
SN  - 1875-533X
VL  - 25
IS  - 33
SP  - 4007
EP  - 4019
PB  - Bentham Science Publishers LTD
CY  - Sharjah
ER  - 
TY  - JOUR
A1  - Jetzschmann, Katharina J.
A1  - Tank, Steffen
A1  - Jagerszki, Gyula
A1  - Gyurcsanyi, Robert E.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
T1  - Bio-Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam
JF  - ChemElectroChem
N2  - 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.
KW  - cytochrome P450
KW  - direct electron transfer
KW  - electropolymerization
KW  - molecularly imprinted polymers
KW  - protein imprinting
Y1  - 2019
U6  - https://doi.org/10.1002/celc.201801851
SN  - 2196-0216
VL  - 6
IS  - 6
SP  - 1818
EP  - 1823
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Kleinjung, Frank
A1  - Scheller, Frieder W.
T1  - Real time measurement of nucleic acid hybridization using evanescent wave sensors - step towards the genosensor
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Detection of progesterone in whole blood samples
N2  - 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%.
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Biosensoren
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Analytical Biochemistry (Editorial)
Y1  - 2004
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bauer, Christian G.
A1  - Makower, Alexander
A1  - Wollenberger, Ursula
A1  - Warsinke, Axel
A1  - Bier, Frank Fabian
T1  - Immunoassays using enzymatic amplification electrodes
Y1  - 2002
SN  - 0-7484-0791-X
ER  - 
TY  - JOUR
A1  - Kleinjung, Frank
A1  - Klußmann, S.
A1  - Erdmann, V. A.
A1  - Scheller, Frieder W.
A1  - Fürste, J. P.
A1  - Bier, Frank Fabian
T1  - Novel binders in biosensorics : hight affinity RNA for smal analytes
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bauer, Christian G.
A1  - Markower, Alexander
A1  - Wollenberger, Ursula
A1  - Warsinke, Axel
A1  - Bier, Frank Fabian
T1  - Coupling of immunoassays with enzymatic recycling electrodes
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Schmidt, Peter Michael
A1  - Matthes, E.
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Nachweis der Telomeraseaktivität in Zellkulturen mittels eines faseroptischen Sensors
Y1  - 2001
ER  - 
TY  - BOOK
A1  - Wollenberger, Ursula
A1  - Renneberg, Reinhard
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Analytische Biochemie : eine praktische Einführung in das Messen mit Biomolekülen
Y1  - 2003
SN  - 3-527-30166-6
PB  - John Wiley & Sons
CY  - Hoboken
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Trends in der Bioanalytik
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Dölling, R.
A1  - Eremenko, A. V.
A1  - Scheller, Frieder W.
T1  - A redox-label immunosensor on basis of a bi-enzyme electrode
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Makower, Alexander
A1  - Barmin, Anatoli V.
A1  - Morzunova, T.
A1  - Eremenko, Arkadi V.
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Affinity enzymomoetric assay for detection of organophosphorus compounds
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
T1  - Amplifying bienzyme cycle-linked immunoassays for determination of 2,4- dichlorphenoxyacetic acid
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Label-free observation of DNA-hybridisation and endonuclease activity on a wave guide surface using a grating coupler
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Stöcklein, Walter F. M.
A1  - Makower, Alexander
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Enzyme sensors and enzyme amplifification systems
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Fürste, J. P.
A1  - Kleinjung, Frank
A1  - Erdmann, V. A.
A1  - Scheller, Frieder W.
T1  - Nukleinsäuren als Basis für Biosensoren
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
A1  - Gajovic, Nenad
T1  - Biosensoren und Teststreifen für die Umwelt- und Lebensmittelanalytik
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Bauer, Christian G.
A1  - Scheller, Frieder W.
T1  - High sensitive competitive immunodetection of 2,4-dichlorophenoxyacetic acid using enzymatic amplification with electrochemical detection
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
A1  - Makower, Alexander
A1  - Eremenko, A. V.
A1  - Wollenberger, Ursula
A1  - Bauer, Christian G.
A1  - Pfeiffer, Dorothea
A1  - Micheel, Burkhard
T1  - Ultrasensitive biosensors
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Ghindilis, A. L.
A1  - Makower, Alexander
A1  - Bauer, Christian G.
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Determination of p-aminophenol and catecholamines at picomolar concentrations based on recycling enzyme amplification
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Makower, Alexander
A1  - Bier, Frank Fabian
A1  - Wollenberger, Ursula
A1  - Ghindilis, A. L.
A1  - Eremenko, A. V.
A1  - Pfeiffer, Dorothea
T1  - Enzymsensoren zur Bestimmung subnanomolarer Konzentrationen
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Makower, Alexander
A1  - Scheller, Frieder W.
T1  - An enzymatic amplification cycle for high sensitive immunoassay
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Song, Min Ik
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - A method to detect superoxide radicals using teflon membrane and superoxide dismutase
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
A1  - Pfeiffer, Dorothea
T1  - Biosensoren : Grundlagen und Anwendungen
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Makower, Alexander
A1  - Ghindilis, A. L.
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Wollenberger, Ursula
A1  - Bauer, Christian G.
A1  - Micheel, Burkhard
A1  - Pfeiffer, Dorothea
A1  - Szeponik, Jan
A1  - Michael, N.
A1  - Kaden, H.
T1  - Enzyme sensors for subnanomolar concentrations
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Jin, Wen
A1  - Wollenberger, Ursula
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Construction and characterization of multi-layer-enzyme electrode : covalent binding of quinoprotein glucose dehydrogenase onto gold electrodes
Y1  - 1995
ER  - 
TY  - GEN
A1  - Bier, Frank Fabian
A1  - Yin, Wen
A1  - Kleinjung, Frank
A1  - Scheller, Frieder W.
T1  - Molekulare Schichten zur Analyse biochemischer Bindungen und Umsatzreaktionen
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Kleinjung, Frank
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Messungen an Nukleinsäuren mittels evaneszenten Feldes
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
A1  - Klingbeil, Mandy
A1  - Oßwald, U.
T1  - Biosensoren und Teststreifen für die Umwelt- und Lebensmittelanalytik : eine Übersicht
Y1  - 1993
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
A1  - Neumann, B.
T1  - Bioindikation in aquatischen Ökosystemen : Bioindikation in limnischen und küstennahen Ökosystemen ; Grundlagen, Verfahren und Methoden
Y1  - 1994
PB  - Fischer
CY  - Jena
ER  - 
TY  - JOUR
A1  - Dechtrirat, Decha
A1  - Gajovic-Eichelmann, Nenad
A1  - Wojcik, Felix
A1  - Hartmann, Laura
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Electrochemical displacement sensor based on ferrocene boronic acid tracer and immobilized glycan for saccharide binding proteins and E. coli
JF  - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
N2  - 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.
KW  - Ferrocene benzoboroxol biosensor
KW  - Concanavalin A
KW  - Displacement
KW  - Escherichia coli
KW  - Ferrocene boronic acid
KW  - Self-assembled monolayer
Y1  - 2014
U6  - https://doi.org/10.1016/j.bios.2014.02.028
SN  - 0956-5663
SN  - 1873-4235
VL  - 58
SP  - 1
EP  - 8
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Yarman, Aysu
A1  - Bachmann, Till
A1  - Hirsch, Thomas
A1  - Kubick, Stefan
A1  - Renneberg, Reinhard
A1  - Schumacher, Soeren
A1  - Wollenberger, Ursula
A1  - Teller, Carsten
A1  - Bier, Frank Fabian
ED  - Gu, MB
ED  - Kim, HS
T1  - Future of biosensors: a personal view
JF  - Advances in biochemical engineering, biotechnology
JF  - Advances in Biochemical Engineering-Biotechnology
N2  - Biosensors representing the technological counterpart of living senses have found routine application in amperometric enzyme electrodes for decentralized blood glucose measurement, interaction analysis by surface plasmon resonance in drug development, and to some extent DNA chips for expression analysis and enzyme polymorphisms. These technologies have already reached a highly advanced level and need minor improvement at most. The dream of the "100-dollar' personal genome may come true in the next few years provided that the technological hurdles of nanopore technology or of polymerase-based single molecule sequencing can be overcome. Tailor-made recognition elements for biosensors including membrane-bound enzymes and receptors will be prepared by cell-free protein synthesis. As alternatives for biological recognition elements, molecularly imprinted polymers (MIPs) have been created. They have the potential to substitute antibodies in biosensors and biochips for the measurement of low-molecular-weight substances, proteins, viruses, and living cells. They are more stable than proteins and can be produced in large amounts by chemical synthesis. Integration of nanomaterials, especially of graphene, could lead to new miniaturized biosensors with high sensitivity and ultrafast response. In the future individual therapy will include genetic profiling of isoenzymes and polymorphic forms of drug-metabolizing enzymes especially of the cytochrome P450 family. For defining the pharmacokinetics including the clearance of a given genotype enzyme electrodes will be a useful tool. For decentralized online patient control or the integration into everyday "consumables' such as drinking water, foods, hygienic articles, clothing, or for control of air conditioners in buildings and cars and swimming pools, a new generation of "autonomous' biosensors will emerge.
KW  - Biosensors
KW  - Molecularly imprinted polymers
KW  - Personalized medicine
Y1  - 2014
SN  - 978-3-642-54143-8; 978-3-642-54142-1
U6  - https://doi.org/10.1007/10_2013_251
SN  - 0724-6145
VL  - 140
SP  - 1
EP  - 28
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Stöcklein, Walter F. M.
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
T1  - Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides
Y1  - 1997
ER  -