@misc{ErdossyHorvathYarmanetal.2016,
  author    = {Erdossy, Julia and Horvath, Viola and Yarman, Aysu and Scheller, Frieder W. and Gyurcsanyi, Robert E.},
  title     = {Electrosynthesized molecularly imprinted polymers for protein recognition},
  series = {Trends in Analytical Chemistry},
  volume    = {79},
  journal   = {Trends in Analytical Chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0165-9936},
  doi       = {10.1016/j.trac.2015.12.018},
  pages     = {179 -- 190},
  year      = {2016},
  abstract  = {Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.},
  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}
}