@article{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Sensors},
  volume    = {14},
  journal   = {Sensors},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s140507647},
  pages     = {7647 -- 7654},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@misc{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1046},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47617},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-476173},
  pages     = {10},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@misc{PengYarmanJetzschmannetal.2017,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400627},
  pages     = {11},
  year      = {2017},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 ± 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@article{PengYarmanJetzschmannetal.2016,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis},
  series = {SENSORS},
  volume    = {16},
  journal   = {SENSORS},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s16030272},
  pages     = {1343 -- 1364},
  year      = {2016},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@misc{MengerYarmanErdoessyetal.2016,
  author    = {Menger, Marcus and Yarman, Aysu and Erd{\"o}ssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing},
  series = {Biosensors : open access journal},
  volume    = {6},
  journal   = {Biosensors : open access journal},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios6030035},
  pages     = {4399 -- 4413},
  year      = {2016},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@misc{MengerYarmanErdőssyetal.2017,
  author    = {Menger, Marcus and Yarman, Aysu and Erdőssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and aptamers for recognition of proteins in biomimetic sensing},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400496},
  pages     = {19},
  year      = {2017},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@phdthesis{Lettau2007,
  author    = {Lettau, Kristian},
  title     = {Katalytische molekular gepr{\"a}gte Polymere : Herstellung und Anwendung in einem Thermistor},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-14804},
  school      = {Universit{\"a}t Potsdam},
  year      = {2007},
  abstract  = {Biomakromolek{\"u}le sind in der Natur f{\"u}r viele Abl{\"a}ufe in lebenden Organismen verantwortlich. Dies reicht vom Aufbau der extrazellul{\"a}ren Matrix und dem Cytoskelett {\"u}ber die Erkennung von Botenstoffen durch Rezeptoren bis hin zur Katalyse der verschiedensten Reaktionen in den Zellen selbst. Diese Aufgaben werden zum gr{\"o}ßten Teil von Proteinen {\"u}bernommen, und besonders das spezifische Erkennen der Interaktionspartner ist f{\"u}r alle diese Molek{\"u}le {\"a}ußerst wichtig, um eine fehlerfreie Funktion zu gew{\"a}hrleisten. Als Alternative zur evolutiven Erzeugung von optimalen Bindern und Katalysatoren auf der Basis von Aminos{\"a}uren und Nukleotiden wurden von Wulff, Shea und Mosbach synthetische molekular gepr{\"a}gte Polymere (molecularly imprinted polymers, MIPs) konzipiert. Das Prinzip dieser k{\"u}nstlichen Erkennungselemente beruht auf der Tatsache, dass sich funktionelle Monomere spezifisch um eine Schablone (Templat) anordnen. Werden diese Monomere dann vernetzend polymerisiert, entsteht ein Polymer mit molekularen Kavit{\"a}ten, in denen die Funktionalit{\"a}ten komplement{\"a}r zum Templat fixiert sind. Dadurch ist die selektive Bindung des Templats in diese Kavit{\"a}ten m{\"o}glich. Aufgrund ihrer hohen chemischen und thermischen Stabilit{\"a}t und ihrer geringen Kosten haben "bio-inspirierte" molekular gepr{\"a}gte Polymere das Potential, biologische Erkennungselemente in der Affinit{\"a}tschromatographie sowie in Biosensoren und Biochips zu ersetzen. Trotz einiger publizierter Sensorkonfigurationen steht der große Durchbruch noch aus. Ein Hindernis f{\"u}r Routineanwendungen ist die Signalgenerierung bei Bindung des Analyten an das Polymer. Eine M{\"o}glichkeit f{\"u}r die markerfreie Detektion ist die Benutzung von Kalorimetern, die Bindungs- oder Reaktionsw{\"a}rmen direkt messen k{\"o}nnen. In der Enzymtechnologie wird der Enzym-Thermistor f{\"u}r diesen Zweck eingesetzt, da enzymatische Reaktionen eine Enthalpie in einer Gr{\"o}ßenordnung von 5 - 100 kJ/mol besitzen. In dieser Arbeit wird die Herstellung von katalytisch gepr{\"a}gten Polymeren nach dem Verfahren des Oberfl{\"a}chenpr{\"a}gens erstmalig beschrieben. Die Methode zur Immobilisierung des Templats auf der Oberfl{\"a}che von por{\"o}sem Kieselgel sowie die Polymerzusammensetzung wurden optimiert. Weiter wird die Evaluation der katalytischen Eigenschaften {\"u}ber einen optischen Test, sowie das erste Mal die Kombination eines kalorimetrischen Transduktors - des Thermistors - mit der Analyterkennung durch ein katalytisch aktives MIP gezeigt. Bei diesen Messungen konnte zum ersten Mal gleichzeitig die Bindung/Desorption, sowie die katalytische Umwandlung des Substrats durch konzentrationsabh{\"a}ngige W{\"a}rmesignale nachgewiesen werden.},
  language  = {de}
}
@misc{YarmanScheller2020,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {How reliable is the electrochemical readout of MIP-sensors?},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  number    = {960},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47160},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-471608},
  pages     = {25},
  year      = {2020},
  abstract  = {Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.},
  language  = {en}
}
@misc{YarmanScheller2020,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {How reliable is the electrochemical readout of MIP sensors?},
  series = {Sensors},
  volume    = {20},
  journal   = {Sensors},
  number    = {9},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s20092677},
  pages     = {23},
  year      = {2020},
  abstract  = {Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.},
  language  = {en}
}
@misc{YarmanJetzschmannNeumannetal.2017,
  author    = {Yarman, Aysu and Jetzschmann, Katharina J. and Neumann, Bettina and Zhang, Xiaorong and Wollenberger, Ulla and Cordin, Aude and Haupt, Karsten and Scheller, Frieder W.},
  title     = {Enzymes as tools in MIP-sensors},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1098},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47464},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-474642},
  pages     = {18},
  year      = {2017},
  abstract  = {Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.},
  language  = {en}
}
@misc{YarmanJetzschmannNeumannetal.2017,
  author    = {Yarman, Aysu and Jetzschmann, Katharina J. and Neumann, Bettina and Zhang, Xiaorong and Wollenberger, Ulla and Cordin, Aude and Haupt, Karsten and Scheller, Frieder W.},
  title     = {Enzymes as Tools in MIP-Sensors},
  series = {Chemosensors},
  volume    = {5},
  journal   = {Chemosensors},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2227-9040},
  doi       = {10.3390/chemosensors5020011},
  pages     = {16},
  year      = {2017},
  abstract  = {Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.},
  language  = {en}
}
@misc{YarmanKurbanogluJetzschmannetal.2018,
  author    = {Yarman, Aysu and Kurbanoglu, Sevinc and Jetzschmann, Katharina J. and Ozkan, Sibel A. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Electrochemical MIP-Sensors for Drugs},
  series = {Current Medicinal Chemistry},
  volume    = {25},
  journal   = {Current Medicinal Chemistry},
  number    = {33},
  publisher = {Bentham Science Publishers LTD},
  address   = {Sharjah},
  issn      = {0929-8673},
  doi       = {10.2174/0929867324666171005103712},
  pages     = {4007 -- 4019},
  year      = {2018},
  abstract  = {In order to replace bio-macromolecules by stable synthetic materials in separation techniques and bioanalysis biomimetic receptors and catalysts have been developed: Functional monomers are polymerized together with the target analyte and after template removal cavities are formed in the "molecularly imprinted polymer" (MIP) which resemble the active sites of antibodies and enzymes. Starting almost 80 years ago, around 1,100 papers on MIPs were published in 2016. Electropolymerization allows to deposit MIPs directly on voltammetric electrodes or chips for quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). For the readout of MIPs for drugs amperometry, differential pulse voltammetry (DPV) and impedance spectroscopy (EIS) offer higher sensitivity as compared with QCM or SPR. Application of simple electrochemical devices allows both the reproducible preparation of MIP sensors, but also the sensitive signal generation. Electrochemical MIP-sensors for the whole arsenal of drugs, e.g. the most frequently used analgesics, antibiotics and anticancer drugs have been presented in literature and tested under laboratory conditions. These biomimetic sensors typically have measuring ranges covering the lower nano-up to millimolar concentration range and they are stable under extreme pH and in organic solvents like nonaqueous extracts.},
  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{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{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}
}