@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} } @article{CasertaZhangYarmanetal.2021, author = {Caserta, Giorgio and Zhang, Xiaorong and Yarman, Aysu and Supala, Eszter and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E. and Zebger, Ingo and Scheller, Frieder W.}, title = {Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms}, series = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)}, volume = {381}, journal = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)}, publisher = {Elsevier}, address = {New York, NY [u.a.]}, issn = {0013-4686}, doi = {10.1016/j.electacta.2021.138236}, pages = {8}, year = {2021}, abstract = {Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague. This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c. To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin. This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target. Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy. This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.}, language = {en} } @article{LoewBogdanoffHerrmannetal.2006, author = {Loew, Noya and Bogdanoff, Peter and Herrmann, Iris and Wollenberger, Ursula and Scheller, Frieder W. and Katterle, Martin}, title = {Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide}, series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis}, volume = {18}, journal = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis}, number = {23}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1040-0397}, doi = {10.1002/elan.200603664}, pages = {2324 -- 2330}, year = {2006}, abstract = {A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found.}, language = {en} } @article{ButtermeyerPhilippMalletal.2002, author = {Buttermeyer, R. and Philipp, A. W. and Mall, J. W. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred}, title = {In vivo measurement of oxygen derived free radicals during reperfusion injury}, year = {2002}, 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{BeissenhirtzSchellerLisdat2003, author = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Lisdat, Fred}, title = {Immobilized cytochrome c sensor in organic / aqueous media for the characterization of hydrophilic and hydrophobic antioxidants}, year = {2003}, 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} } @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{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{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} }