@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{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{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} } @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} } @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{SchellerKirsteinSchubertetal.1993, author = {Scheller, Frieder W. and Kirstein, Dieter and Schubert, Florian and Pfeiffer, Dorothea and McNeil, C. J.}, title = {Enzymes in electrochemical biosensors}, year = {1993}, 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{HalamekTellerMakoweretal.2006, author = {Halamek, Jan and Teller, Carsten and Makower, Alexander and Fournier, Didier and Scheller, Frieder W.}, title = {EQCN-based cholinesterase biosensors}, issn = {0013-4686}, doi = {10.1016/j.electacta.2006.03.047}, year = {2006}, abstract = {The binding of acetylcholinesterase (AChE) to a propidium-modified piezoelectric quartz crystal and its surface enzymatic activity have been investigated. Propidium binds to a site remote to the active center of AChE - the peripheral anionic site (PAS) - which is located on the rim of the gorge to the active site. The gold electrodes of the quartz crystal were first modified with 11-mercaptoundecanoic acid to which propidium was coupled. AChE binding was monitored by a quartz crystal nanobalance (QCN), followed by amperometric activity evaluation of the AChE loaded on the sensor. Interestingly, the binding is strong but does not inhibit AChE. However, an excess of propidium in solution inhibits the immobilized enzyme. The surface enzymatic activities observed depend on the amount of enzyme and differ according to the type and species, i.e. number of enzyme subunits (Electrophorus electricus tetrameric, Drosophila melanogaster mono- and dimeric form - DmAChE). The operational stability and regeneration, effect of propidium in solution and detection limit for substrate for various AChEs were investigated amperometrically.}, language = {en} } @article{LiuWollenbergerKatterleetal.2006, author = {Liu, Songqin and Wollenberger, Ursula and Katterle, Martin and Scheller, Frieder W.}, title = {Ferroceneboronic acid-based amperometric biosensor for glycated hemoglobin}, issn = {0925-4005}, doi = {10.1016/j.snb.2005.07.011}, year = {2006}, abstract = {An amperometric biosensor for the determination of glycated hemoglobin in human whole blood is proposed. The principle is based on the electrochemical measurement of ferroceneboronic acid (FcBA) that has been specifically bound to the glycated N-terminus. Hemoglobin is immobilized on a zirconium dioxide nanoparticle modified pyrolytic graphite electrode (PGE) in the presence of didodecyldimethylammonium bromide (DDAB). The incubation of this sensor in FcBA solution leads to the formation of an FcBA-modified surface due to the affinity interaction between boronate and the glycated sites of the hemoglobin. The binding of FcBA results in well-defined redox peaks with an E-0' of 0.299 V versus Ag/AgCl (1 M KCl). The square wave voltammetric response of the bound FcBA reflects the amount of glycated hemoglobin at the surface. This signal increases linearily with the degree of glycated hemoglobin from 6.8 to 14.0\% of total immobilized hemoglobin. The scheme was applied to the determination of the fraction of glycated hemoglobin in whole blood samples.}, 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{BaeumnerGauglitzScheller2010, author = {Baeumner, Antje J. and Gauglitz, Guenter and Scheller, Frieder W.}, title = {Focus on bioanalysis}, issn = {1618-2642}, doi = {10.1007/s00216-010-4203-9}, year = {2010}, abstract = {Editoria}, language = {en} } @article{SchellerWagener2004, author = {Scheller, Frieder W. and Wagener, C.}, title = {From gene to life}, year = {2004}, language = {en} } @article{TadjoungWaffoYesildagCasertaetal.2018, author = {Tadjoung Waffo, Armel Franklin and Yesildag, Cigdem and Caserta, Giorgio and Katz, Sagie and Zebger, Ingo and Lensen, Marga C. and Wollenberger, Ulla and Scheller, Frieder W. and Altintas, Zeynep}, title = {Fully electrochemical MIP sensor for artemisinin}, series = {Sensors and actuators : B, Chemical}, volume = {275}, journal = {Sensors and actuators : B, Chemical}, publisher = {Elsevier}, address = {Lausanne}, issn = {0925-4005}, doi = {10.1016/j.snb.2018.08.018}, pages = {163 -- 173}, year = {2018}, abstract = {This study aims to develop a rapid, sensitive and cost-effective biomimetic electrochemical sensor for artemisinin determination in plant extracts and for pharmacokinetic studies. A novel molecularly imprinted polymer (MIP)based electrochemical sensor was developed by electropolymerization of o-phenylenediamine (o-PD) in the presence of artemisinin on gold wire surface for sensitive detection of artemisinin. The experimental parameters, including selection of functional monomer, polymerization conditions, template extraction after polymerization, influence of pH and buffer were all optimized. Every step of imprinted film synthesis were evaluated by employing voltammetry techniques, surface-enhanced infrared absorption spectroscopy (SEIRAS) and atomic force microscopy (AFM). The specificity was further evaluated by investigating non-specific artemisinin binding on non-imprinted polymer (NIP) surfaces and an imprinting factor of 6.8 was achieved. The artemisinin imprinted polymers using o-PD as functional monomer have provided highly stable and effective binding cavities for artemisinin. Cross-reactivity studies with drug molecules showed that the MIPs are highly specific for artemisinin. The influence of matrix effect was further investigated both in artificial plant matrix and diluted human serum. The results revealed a high affinity of artemisinin-MIP with dissociation constant of 7.3 x 10(-9) M and with a detection limit of 0.01 mu M and 0.02 mu M in buffer and plant matrix, respectively.}, language = {en} } @article{WollenbergerJinBernhardtetal.1998, author = {Wollenberger, Ursula and Jin, Wen and Bernhardt, Rita and Lehmann, Claudia and St{\"o}cklein, Walter F. M. and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.}, title = {Funktionalisierung von Elektroden f{\"u}r den direkten heterogenen Elektrotransfer}, year = {1998}, language = {de} } @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{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} } @misc{YarmanScheller2020, author = {Yarman, Aysu and Scheller, Frieder W.}, title = {How reliable is the electrochemical readout of MIP sensors?}, series = {Sensors}, volume = {20}, journal = {Sensors}, number = {9}, publisher = {MDPI}, address = {Basel}, issn = {1424-8220}, doi = {10.3390/s20092677}, pages = {23}, 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{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} } @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{LettauGajovicEichelmannKwaketal.2004, author = {Lettau, Kristian and Gajovic-Eichelmann, N. and Kwak, Young-Keun and Scheller, Frieder W. and Warsinke, Axel}, title = {Hydroxylasen und katalytische Polymere f{\"u}r Biochips}, year = {2004}, language = {de} }