TY - GEN A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Neumann, Bettina A1 - Zhang, Xiaorong A1 - Wollenberger, Ulla A1 - Cordin, Aude A1 - Haupt, Karsten A1 - Scheller, Frieder W. T1 - Enzymes as tools in MIP-sensors T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - 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. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1098 KW - enzymatic MIP synthesis KW - template digestion KW - enzyme tracer KW - enzymatic analyte conversion KW - molecularly imprinted polymers Y1 - 2021 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-474642 SN - 1866-8372 IS - 1098 ER - TY - JOUR A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Neumann, Bettina A1 - Zhang, Xiaorong A1 - Wollenberger, Ulla A1 - Cordin, Aude A1 - Haupt, Karsten A1 - Scheller, Frieder W. T1 - Enzymes as Tools in MIP-Sensors JF - Chemosensors N2 - 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. KW - enzymatic MIP synthesis KW - template digestion KW - enzyme tracer KW - enzymatic analyte conversion KW - molecularly imprinted polymers Y1 - 2017 U6 - https://doi.org/10.3390/chemosensors5020011 SN - 2227-9040 VL - 5 PB - MDPI CY - Basel ER - TY - GEN A1 - Peng, Lei A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Jeoung, Jae-Hun A1 - Schad, Daniel A1 - Dobbek, Holger A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis N2 - 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). T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 362 KW - molecularly imprinted polymers KW - self-assembled monolayer KW - direct electron transfer KW - hydrogen peroxide KW - bioelectrocatalysis Y1 - 2017 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400627 ER - TY - GEN A1 - Menger, Marcus A1 - Yarman, Aysu A1 - Erdőssy, Júlia A1 - Yildiz, Huseyin Bekir A1 - Gyurcsányi, Róbert E. A1 - Scheller, Frieder W. T1 - MIPs and aptamers for recognition of proteins in biomimetic sensing N2 - 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. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 357 KW - biomimetic recognition elements KW - aptamers KW - molecularly imprinted polymers KW - chemical sensors KW - aptasensors KW - in vitro selection KW - SELEX Y1 - 2017 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400496 ER -