TY - JOUR A1 - Scheller, Frieder W. A1 - Scheller, A. T1 - Bi-Enzymelektrode zur Messung von Sorbitol in pharmazeutischen Produkten Y1 - 1996 ER - TY - JOUR A1 - Banks, Jo Ann A1 - Nishiyama, Tomoaki A1 - Hasebe, Mitsuyasu A1 - Bowman, John L. A1 - Gribskov, Michael A1 - dePamphilis, Claude A1 - Albert, Victor A. A1 - Aono, Naoki A1 - Aoyama, Tsuyoshi A1 - Ambrose, Barbara A. A1 - Ashton, Neil W. A1 - Axtell, Michael J. A1 - Barker, Elizabeth A1 - Barker, Michael S. A1 - Bennetzen, Jeffrey L. A1 - Bonawitz, Nicholas D. A1 - Chapple, Clint A1 - Cheng, Chaoyang A1 - Correa, Luiz Gustavo Guedes A1 - Dacre, Michael A1 - DeBarry, Jeremy A1 - Dreyer, Ingo A1 - Elias, Marek A1 - Engstrom, Eric M. A1 - Estelle, Mark A1 - Feng, Liang A1 - Finet, Cedric A1 - Floyd, Sandra K. A1 - Frommer, Wolf B. A1 - Fujita, Tomomichi A1 - Gramzow, Lydia A1 - Gutensohn, Michael A1 - Harholt, Jesper A1 - Hattori, Mitsuru A1 - Heyl, Alexander A1 - Hirai, Tadayoshi A1 - Hiwatashi, Yuji A1 - Ishikawa, Masaki A1 - Iwata, Mineko A1 - Karol, Kenneth G. A1 - Koehler, Barbara A1 - Kolukisaoglu, Uener A1 - Kubo, Minoru A1 - Kurata, Tetsuya A1 - Lalonde, Sylvie A1 - Li, Kejie A1 - Li, Ying A1 - Litt, Amy A1 - Lyons, Eric A1 - Manning, Gerard A1 - Maruyama, Takeshi A1 - Michael, Todd P. A1 - Mikami, Koji A1 - Miyazaki, Saori A1 - Morinaga, Shin-ichi A1 - Murata, Takashi A1 - Müller-Röber, Bernd A1 - Nelson, David R. A1 - Obara, Mari A1 - Oguri, Yasuko A1 - Olmstead, Richard G. A1 - Onodera, Naoko A1 - Petersen, Bent Larsen A1 - Pils, Birgit A1 - Prigge, Michael A1 - Rensing, Stefan A. A1 - Mauricio Riano-Pachon, Diego A1 - Roberts, Alison W. A1 - Sato, Yoshikatsu A1 - Scheller, Henrik Vibe A1 - Schulz, Burkhard A1 - Schulz, Christian A1 - Shakirov, Eugene V. A1 - Shibagaki, Nakako A1 - Shinohara, Naoki A1 - Shippen, Dorothy E. A1 - Sorensen, Iben A1 - Sotooka, Ryo A1 - Sugimoto, Nagisa A1 - Sugita, Mamoru A1 - Sumikawa, Naomi A1 - Tanurdzic, Milos A1 - Theissen, Guenter A1 - Ulvskov, Peter A1 - Wakazuki, Sachiko A1 - Weng, Jing-Ke A1 - Willats, William W. G. T. A1 - Wipf, Daniel A1 - Wolf, Paul G. A1 - Yang, Lixing A1 - Zimmer, Andreas D. A1 - Zhu, Qihui A1 - Mitros, Therese A1 - Hellsten, Uffe A1 - Loque, Dominique A1 - Otillar, Robert A1 - Salamov, Asaf A1 - Schmutz, Jeremy A1 - Shapiro, Harris A1 - Lindquist, Erika A1 - Lucas, Susan A1 - Rokhsar, Daniel A1 - Grigoriev, Igor V. T1 - The selaginella genome identifies genetic changes associated with the evolution of vascular plants JF - Science N2 - Vascular plants appeared similar to 410 million years ago, then diverged into several lineages of which only two survive: the euphyllophytes (ferns and seed plants) and the lycophytes. We report here the genome sequence of the lycophyte Selaginella moellendorffii (Selaginella), the first nonseed vascular plant genome reported. By comparing gene content in evolutionarily diverse taxa, we found that the transition from a gametophyte- to a sporophyte-dominated life cycle required far fewer new genes than the transition from a nonseed vascular to a flowering plant, whereas secondary metabolic genes expanded extensively and in parallel in the lycophyte and angiosperm lineages. Selaginella differs in posttranscriptional gene regulation, including small RNA regulation of repetitive elements, an absence of the trans-acting small interfering RNA pathway, and extensive RNA editing of organellar genes. Y1 - 2011 U6 - https://doi.org/10.1126/science.1203810 SN - 0036-8075 VL - 332 IS - 6032 SP - 960 EP - 963 PB - American Assoc. for the Advancement of Science CY - Washington 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 - Freaney, R. A1 - MacShane, A. A1 - Keaveny, T. V. A1 - MacKenna, M. A1 - Rabenstein, K. A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea A1 - Urban, G. A1 - Moser, I. A1 - Jobst, G. A1 - Manz, A. A1 - Verpoorte, E. A1 - Widmer, M. W. A1 - Diamond, D. A1 - Dempsey, E. A1 - deViteri, F. J. S. A1 - Smyth, M. T1 - Novel instrumentation for real-time monitoring using miniaturized flow systems with integrated biosensors Y1 - 1997 ER - TY - JOUR A1 - Bauer, Christian G. A1 - Eremenko, A. V. A1 - Kühn, A. A1 - Kürzinger, K. A1 - Markower, Alexander A1 - Scheller, Frieder W. T1 - Automated amplifield flow immunoassay for cocaine Y1 - 1998 ER - TY - JOUR A1 - Fridman, Vadim A1 - Wollenberger, Ursula A1 - Bogdanovskaya, V. A. A1 - Lisdat, Fred A1 - Ruzgas, T. A1 - Lindgren, A. A1 - Gorton, Lo A1 - Scheller, Frieder W. T1 - Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator Y1 - 2000 ER - TY - JOUR A1 - Kapp, A. A1 - Beissenhirtz, Moritz Karl A1 - Geyer, F. A1 - Scheller, F. A1 - Viezzoli, Maria Silvia A1 - Lisdat, Fred T1 - Electrochemical and sensorial behavior of SOD mutants immobilized on gold electrodes in aqueous/organic solvent mixtures JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - A cysteine mutant of a monomeric human Cu, Zn-SOD (Glycine 61, Serine 142) has been immobilized directly on gold electrodes using the thiol groups introduced. The electrochemical behavior of the surface confined protein was studied in mixtures of aqueous buffer and DMSO up to an organic solvent content of 60%. The formal potential was found to be rather independent of the DMSO content. However, half peak width increased and the redoxactive amount clearly decreased with raising DMSO content. In addition, the kinetics of the heterogeneous electron transfer became slower; but still a quasireversible electrochemical conversion of the mutant SOD was feasible. Thus, the electrodes were applied for sensorial superoxide detection. At a potential of +220 mV vs. Ag/AgCl advantage was taken of the partial oxidation reaction of the enzyme. A defined superoxide signal was obtained in solutions up to 40% DMSO. The sensitivity of the mutant electrodes decreased linearly with the organic solvent content in solution but was still higher compared to conventional cyt.c based sensors. At DMSO concentrations higher than 40% no sensor response was detected. KW - SOD KW - mutants KW - gold electrodes KW - DMSO KW - electrochemistry Y1 - 2006 U6 - https://doi.org/10.1002/elan.200603620 SN - 1040-0397 VL - 18 SP - 1909 EP - 1915 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Ozcelikay, Goksu A1 - Kurbanoglu, Sevinc A1 - Zhang, Xiaorong A1 - Söz, Çağla Kosak A1 - Wollenberger, Ulla A1 - Ozkan, Sibel A. A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - Electrochemical MIP Sensor for Butyrylcholinesterase JF - Polymers N2 - 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. KW - molecularly imprinted polymers KW - biomimetic sensors KW - butyrylcholinesterase KW - o-phenylenediamine KW - rivastigmine Y1 - 2019 U6 - https://doi.org/10.3390/polym11121970 SN - 2073-4360 VL - 11 IS - 12 PB - MDPI CY - Basel ER - TY - JOUR A1 - Bistolas, Nikitas A1 - Christenson, A. A1 - Ruzgas, T. A1 - Jung, Christiane A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Spectroelectrochemistry of cytochrome P450cam N2 - The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved Y1 - 2004 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 - Buttermeyer, R. A1 - Philipp, A. W. A1 - Mall, J. W. A1 - Ge, Bixia A1 - Scheller, Frieder W. A1 - Lisdat, Fred T1 - In vivo measurement of oxygen derived free radicals during reperfusion injury Y1 - 2002 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 - 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 - 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 - GEN A1 - Ozcelikay, Goksu A1 - Kurbanoglu, Sevinc A1 - Zhang, Xiaorong A1 - Söz, Çağla Kosak A1 - Wollenberger, Ulla A1 - Ozkan, Sibel A. A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - Electrochemical MIP Sensor for Butyrylcholinesterase T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - 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. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1138 KW - molecularly imprinted polymers KW - biomimetic sensors KW - butyrylcholinesterase KW - o-phenylenediamine KW - rivastigmine Y1 - 2021 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-501854 SN - 1866-8372 IS - 1138 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 - 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 - 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 - Bauer, Christian G. A1 - Eremenko, A. V. A1 - Ehrentreich-Förster, Eva A1 - Bier, Frank Fabian A1 - Makower, Alexander A1 - Halsall, H. B. A1 - Heineman, W. R. A1 - Scheller, Frieder W. T1 - Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid Y1 - 1996 ER -