TY - JOUR A1 - Yarman, Aysu A1 - Dechtrirat, Decha A1 - Bosserdt, Maria A1 - Jetzschmann, Katharina J. A1 - Gajovic-Eichelmann, Nenad A1 - Scheller, Frieder W. T1 - Cytochrome c-derived hybrid systems based on moleculary imprinted polymers JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - Hybrid architectures which combine a MIP with an immobilized affinity ligand or a biocatalyst sum up the advantages of both components. In this paper, hybrid architectures combining a layer of a molecularly imprinted electropolymer with a mini-enzyme or a self-assembled monolayer will be presented. (i) Microperoxidase-11 (MP-11) catalyzed oxidation of the drug aminopyrine on a product-imprinted sublayer: The peroxide dependent conversion of the analyte aminopyrine takes place in the MP-11 containing layer on top of a product-imprinted electropolymer on the indicator electrode. The hierarchical architecture resulted in the elimination of interfering signals for ascorbic acid and uric acid. An advantage of the new hierarchical structure is the separation of MIP formation by electropolymerization and immobilization of the catalyst. In this way it was for the first time possible to integrate an enzyme with a MIP layer in a sensor configuration. This combination has the potential to be transferred to other enzymes, e.g. P450, opening the way to clinically important analytes. (ii) Epitope-imprinted poly-scopoletin layer for binding of the C-terminal peptide and cytochrome c (Cyt c): The MIP binds both the target peptide and the parent protein almost eight times stronger than the non-imprinted polymer with affinities in the lower micromolar range. Exchange of only one amino acid in the peptide decreases the binding by a factor of five. (iii) MUA-poly-scopoletin MIP for cytochrome c: Cyt c bound to the MIP covered gold electrode exhibits direct electron transfer with a redox potential and rate constant typical for the native protein. The MIP cover layer suppresses the displacement of the target protein by BSA or myoglobin. The combination of protein imprinted polymers with an efficient electron transfer is a new concept for characterizing electroactive proteins such as Cyt c. The competition with other proteins shows that the MIP binds its target Cyt c preferentially and that molecular shape and the charge of protein determine the binding of interfering proteins. KW - Molecularly imprinted polymers KW - Microperoxidase-11 KW - Cytochrome c KW - Catalytically active MIPs KW - Epitope imprinting KW - Monoclonal MIPs Y1 - 2015 U6 - https://doi.org/10.1002/elan.201400592 SN - 1040-0397 SN - 1521-4109 VL - 27 IS - 3 SP - 573 EP - 586 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Yarman, Aysu A1 - Badalyan, Artavazd A1 - Gajovic-Eichelmann, Nenad A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Enzyme electrode for aromatic compounds exploiting the catalytic activities of microperoxidase-11 JF - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics N2 - Microperoxidase-11 (MR-11) which has been immobilised in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode catalyzes the conversion of aromatic substances. This peroxide-dependent catalysis of microperoxidase has been applied in an enzyme electrode for the first time to indicate aromatic compounds such as aniline. 4-fluoroaniline, catechol and p-aminophenol. The electrode signal is generated by the cathodic reduction of the quinone or quinoneimine which is formed in the presence of both MP-II and peroxide from the substrate. The same sensor principle will be extended to aromatic drugs. KW - Microperoxidase-11 KW - Nanoparticles KW - p-Aminophenol KW - Aniline KW - Catechol KW - 4-Fluoroaniline KW - Biosensors Y1 - 2011 U6 - https://doi.org/10.1016/j.bios.2011.09.004 SN - 0956-5663 VL - 30 IS - 1 SP - 320 EP - 323 PB - Elsevier CY - Oxford ER -