@article{ZhangCasertaYarmanetal.2021, author = {Zhang, Xiaorong and Caserta, Giorgio and Yarman, Aysu and Supala, Eszter and Tadjoung Waffo, Armel Franklin and Wollenberger, Ulla and Gyurcsanyi, Robert E. and Zebger, Ingo and Scheller, Frieder W.}, title = {"Out of Pocket" protein binding}, series = {Chemosensors}, volume = {9}, journal = {Chemosensors}, number = {6}, publisher = {MDPI}, address = {Basel}, issn = {2227-9040}, doi = {10.3390/chemosensors9060128}, pages = {13}, year = {2021}, abstract = {The epitope imprinting approach applies exposed peptides as templates to synthesize Molecularly Imprinted Polymers (MIPs) for the recognition of the parent protein. While generally the template protein binding to such MIPs is considered to occur via the epitope-shaped cavities, unspecific interactions of the analyte with non-imprinted polymer as well as the detection method used may add to the complexity and interpretation of the target rebinding. To get new insights on the effects governing the rebinding of analytes, we electrosynthesized two epitope-imprinted polymers using the N-terminal pentapeptide VHLTP-amide of human hemoglobin (HbA) as the template. MIPs were prepared either by single-step electrosynthesis of scopoletin/pentapeptide mixtures or electropolymerization was performed after chemisorption of the cysteine extended VHLTP peptide. Rebinding of the target peptide and the parent HbA protein to the MIP nanofilms was quantified by square wave voltammetry using a redox probe gating, surface enhanced infrared absorption spectroscopy, and atomic force microscopy. While binding of the pentapeptide shows large influence of the amino acid sequence, all three methods revealed strong non-specific binding of HbA to both polyscopoletin-based MIPs with even higher affinities than the target peptides.}, language = {en} } @article{HuangWarsinkeKoroljovaSkorobogatkoetal.1999, author = {Huang, T. and Warsinke, Axel and Koroljova-Skorobogatko, O. V. and Makower, Alexander and Kuwana, T. and Scheller, Frieder W.}, title = {A bienzyme carbon paste electrode for the sensitive detection of NADPH and the measurement of glucose-6- phosphate dehydrogenase}, year = {1999}, language = {en} } @article{GajovicWarsinkeScheller1998, author = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.}, title = {A bienzyme electrode for L-malate based on a novel and general design}, year = {1998}, 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{LettauWarsinkeKatterleetal.2006, author = {Lettau, Kristian and Warsinke, Axel and Katterle, Martin and Danielsson, Bengt and Scheller, Frieder W.}, title = {A bifunctional molecularly imprinted polymer (MIP): analysis of binding and catalysis by a thermistor}, doi = {10.1002/anie.200601796}, year = {2006}, abstract = {Binding or catalysis? Both can be distinguished with a molecularly imprinted polymer (MIP) by the different patterns of heat generation. The catalytically active sites, like in the corresponding enzyme, generate a steady-state temperature increase. Thus, enzyme-like catalysis and antibody-analogue binding are analyzed simultaneously in a bifunctional MIP for the first time (see scheme).}, language = {en} } @article{ChenWarsinkeGajovicetal.2000, author = {Chen, Ziping and Warsinke, Axel and Gajovic, Nenad and Große, St. and Hu, J. and Kleber, H.-P. and Scheller, Frieder W.}, title = {A D-carnitine dehydrogenase electrode for the assessment of enantiomeric purity of L-carnitine preparations}, year = {2000}, 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{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{TellerHalamekMakoweretal.2006, author = {Teller, C. and Halamek, Jan and Makower, Alexander and Fournier, Didier and Schulze, H. and Scheller, Frieder W.}, title = {A piezoelectric sensor with propidium as a recognition element for cholinesterases}, doi = {10.1016/j.snb.2005.02.053}, year = {2006}, abstract = {A piezoelectric biosensor has been developed on the basis of the reversible acetylcholinesterase (AChE) inhibitor propidium. The propidium cation was bound to a 11-mercaptoundecanoic acid monolayer on gold-coated quartz crystals. The immobilization was done via activation of carboxyl groups by 1,3-dicyclohexylcarbodiimide (DCC). Different types of cholinesterases (acetyl- and butyryl-ChE) from different origins were tested for their binding ability towards the immobilized propidium. Binding Studies were performed in a flow system, Furthermore, catalytically active and organophosphate-inhibited enzyme were compared re-aiding their binding capability. The binding constants were derived by using an one to one binding model and a refined model also including rebinding effects. It was shown that organophosphorylation of the active site hardly influences the affinity of AChE towards propidium. Furthermore the propidium-based biosensor provides equal sensitivity as compared with piezolelectric sensors with immobilized paraoxon- an active site ligand of AChE. (c) 2005 Elsevier B.V. All rights reserved}, language = {en} } @article{GajovicHabermuellerWarsinkeetal.1999, author = {Gajovic, Nenad and Haberm{\"u}ller, K. and Warsinke, Axel and Schuhmann, W. and Scheller, Frieder W.}, title = {A pyruvate oxidase electrode based on an electrochemically deposited redox polymer}, year = {1999}, language = {en} }