@article{YarmanScheller2013,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {Coupling biocatalysis with molecular imprinting in a biomimetic sensor},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {52},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {44},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201305368},
  pages     = {11521 -- 11525},
  year      = {2013},
  language  = {en}
}
@article{Yarman2017,
  author    = {Yarman, Aysu},
  title     = {Development of a molecularly imprinted polymer-based electrochemical sensor for tyrosinase},
  series = {Turkish journal of chemistry},
  volume    = {42},
  journal   = {Turkish journal of chemistry},
  number    = {2},
  publisher = {T{\"u}rkiye Bilimsel ve Teknik Ara{\c{s}}t{\i}rma Kurumu},
  address   = {Ankara},
  issn      = {1300-0527},
  doi       = {10.3906/kim-1708-68},
  pages     = {346 -- 354},
  year      = {2017},
  abstract  = {For the first time a molecularly imprinted polymer (MIP)-based sensor for tyrosinase is described. This sensor is based on the electropolymerization of scopoletin or o-phenylenediamine in the presence of tyrosinase from mushrooms, which has a high homology to the human enzyme. The template was removed either by treatment with proteinase Kor by alkaline treatment. The measuring signal was generated either by measuring the formation of a product by the target enzyme or by evaluation of the permeability of the redox marker ferricyanide. The o-phenylenediamine-based MIP sensor has a linear measuring range up to 50 nM of tyrosinase with a limit of detection of 3.97 nM (R 2 = 0.994) and shows good discrimination towards other proteins, e.g., bovine serum albumin and cytochrome c.},
  language  = {en}
}
@article{OzcelikayKurbanogluZhangetal.2019,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Zhang, Xiaorong and S{\"o}z, {\c{C}}ağla Kosak and Wollenberger, Ulla and Ozkan, Sibel A. and Yarman, Aysu and Scheller, Frieder W.},
  title     = {Electrochemical MIP Sensor for Butyrylcholinesterase},
  series = {Polymers},
  volume    = {11},
  journal   = {Polymers},
  number    = {12},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2073-4360},
  doi       = {10.3390/polym11121970},
  pages     = {11},
  year      = {2019},
  abstract  = {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.},
  language  = {en}
}
@misc{OzcelikayKurbanogluZhangetal.2019,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Zhang, Xiaorong and S{\"o}z, {\c{C}}ağla Kosak and Wollenberger, Ulla and Ozkan, Sibel A. and Yarman, Aysu and Scheller, Frieder W.},
  title     = {Electrochemical MIP Sensor for Butyrylcholinesterase},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1138},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-50185},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-501854},
  pages     = {13},
  year      = {2019},
  abstract  = {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.},
  language  = {en}
}
@article{JetzschmannJagerszkiDechtriratetal.2015,
  author    = {Jetzschmann, Katharina J. and Jagerszki, Gyula and Dechtrirat, Decha and Yarman, Aysu and Gajovic-Eichelmann, Nenad and Gilsing, Hans-Detlev and Schulz, Burkhard and Gyurcsanyi, Robert E. and Scheller, Frieder W.},
  title     = {Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition},
  series = {Advanced functional materials},
  volume    = {25},
  journal   = {Advanced functional materials},
  number    = {32},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201501900},
  pages     = {5178 -- 5183},
  year      = {2015},
  abstract  = {Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid.},
  language  = {en}
}