@article{TadjoungWaffoYesildagCasertaetal.2018,
  author    = {Tadjoung Waffo, Armel Franklin and Yesildag, Cigdem and Caserta, Giorgio and Katz, Sagie and Zebger, Ingo and Lensen, Marga C. and Wollenberger, Ulla and Scheller, Frieder W. and Altintas, Zeynep},
  title     = {Fully electrochemical MIP sensor for artemisinin},
  series = {Sensors and actuators : B, Chemical},
  volume    = {275},
  journal   = {Sensors and actuators : B, Chemical},
  publisher = {Elsevier},
  address   = {Lausanne},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2018.08.018},
  pages     = {163 -- 173},
  year      = {2018},
  abstract  = {This study aims to develop a rapid, sensitive and cost-effective biomimetic electrochemical sensor for artemisinin determination in plant extracts and for pharmacokinetic studies. A novel molecularly imprinted polymer (MIP)based electrochemical sensor was developed by electropolymerization of o-phenylenediamine (o-PD) in the presence of artemisinin on gold wire surface for sensitive detection of artemisinin. The experimental parameters, including selection of functional monomer, polymerization conditions, template extraction after polymerization, influence of pH and buffer were all optimized. Every step of imprinted film synthesis were evaluated by employing voltammetry techniques, surface-enhanced infrared absorption spectroscopy (SEIRAS) and atomic force microscopy (AFM). The specificity was further evaluated by investigating non-specific artemisinin binding on non-imprinted polymer (NIP) surfaces and an imprinting factor of 6.8 was achieved. The artemisinin imprinted polymers using o-PD as functional monomer have provided highly stable and effective binding cavities for artemisinin. Cross-reactivity studies with drug molecules showed that the MIPs are highly specific for artemisinin. The influence of matrix effect was further investigated both in artificial plant matrix and diluted human serum. The results revealed a high affinity of artemisinin-MIP with dissociation constant of 7.3 x 10(-9) M and with a detection limit of 0.01 mu M and 0.02 mu M in buffer and plant matrix, respectively.},
  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}
}
@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}
}
@incollection{LueckBalderjahnKammetal.2000,
  author    = {L{\"u}ck, Erika and Balderjahn, Ingo and Kamm, Birgit and Greil, Holle and Wallschl{\"a}ger, Hans-Dieter and Jessel, Beate and B{\"o}ckmann, Christine and Oberh{\"a}nsli, Roland and Soyez, Konrad and Schmeer, Ernst and Blumenstein, Oswald and Berndt, Klaus-Peter and Edeling, Thomas and Friedrich, Sabine and Kaden, Klaus and Scheller, Frieder W. and Petersen, Hans-Georg and Asche, Hartmut and Bronstert, Axel and Giest, Hartmut and Gaedke, Ursula and L{\"o}hmannsr{\"o}ben, Hans-Gerd and Jeltsch, Florian and J{\"a}nkel, Ralph and Gzik, Axel and Bork, Hans-Rudolf and Bork, Hans-Rudolf},
  title     = {Umweltforschung f{\"u}r das Land Brandenburg : Arbeitsgruppen und Professuren},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-3797},
  publisher      = {Universit{\"a}t Potsdam},
  year      = {2000},
  language  = {de}
}
@incollection{AscheBoeckmannLaueetal.2000,
  author    = {Asche, Hartmut and B{\"o}ckmann, Christine and Laue, Steffen and L{\"o}hmannsr{\"o}ben, Hans-Gerd and Lemke, Matthias and Schober, Lars and Reich, Oliver and L{\"u}ck, Erika and Sch{\"u}tte, Marc and Domsch, Horst and Makower, Alexander and Scheller, Frieder W. and St{\"o}cklein, Wolfgang and Wollenberger, Ursula and Schultze, Rainer and Hengstermann, Theo and Schael, Frank},
  title     = {Umweltforschung f{\"u}r das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-3862},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {176 -- 227},
  year      = {2000},
  language  = {de}
}