@article{JetzschmannTankJagerszkietal.2019,
  author    = {Jetzschmann, Katharina J. and Tank, Steffen and Jagerszki, Gyula and Gyurcsanyi, Robert E. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Bio-Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam},
  series = {ChemElectroChem},
  volume    = {6},
  journal   = {ChemElectroChem},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {2196-0216},
  doi       = {10.1002/celc.201801851},
  pages     = {1818 -- 1823},
  year      = {2019},
  abstract  = {A new approach for synthesizing a vectorially imprinted polymer (VIP) is presented for the microbial cytochrome P450cam enzyme. A surface attached binding motif of a natural reaction partner of the target protein, putidaredoxin (Pdx), is the anchor to the underlying transducer. The 15 amino acid peptide anchor, which stems from the largest continuous amino acid chain within the binding site of Pdx was modified: (i) internal cysteines were replaced by serines to prevent disulfide bond formation; (ii) 2 ethylene glycol units were attached to the N-terminus as a spacer region; and (iii) an N-terminal cysteine was added to allow the immobilization on the gold electrode surface. Immobilization on GCE was achieved via an N-(1-pyrenyl)maleimide (NPM) cross-linker. In this way oriented immobilization of P450cam was accomplished by binding it to a peptide-modified gold or glassy carbon electrode (GCE) prior to the electrosynthesis of a polymer nanofilm around the immobilized target. This VIP nanofilm enabled reversible oriented docking of P450cam as it is indicated by the catalytic oxygen reduction via direct electron transfer between the enzyme and the underlying electrode. Catalysis of oxygen reduction by P450cam bound to the VIP-modified GCE was used to measure rebinding to the VIP. The mild coupling of an oxidoreductase with the electrode may be appropriate for realizing electrode-driven substrate conversion by instable P450 enzymes without the need of NADPH co-factor.},
  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{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}
}
@misc{SchellerZhangYarmanetal.2019,
  author    = {Scheller, Frieder W. and Zhang, Xiaorong and Yarman, Aysu and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E.},
  title     = {Molecularly imprinted polymer-based electrochemical sensors for biopolymers},
  series = {Current opinion in electrochemistry},
  volume    = {14},
  journal   = {Current opinion in electrochemistry},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {2451-9103},
  doi       = {10.1016/j.coelec.2018.12.005},
  pages     = {53 -- 59},
  year      = {2019},
  abstract  = {Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one 'separation plate'; thus, the selectivity does not reach the values of 'bulk' measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an 'overall apparent' signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.},
  language  = {en}
}