@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}
}
@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}
}