@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{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{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{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{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{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}
}