TY - JOUR A1 - Yarman, Aysu T1 - Electrosynthesized Molecularly Imprinted Polymer for Laccase Using the Inactivated Enzyme as the Target JF - Bulletin of the Korean chemical society N2 - The first molecularly imprinted polymer (MIP) for the recognition of the copper-enzyme laccase was successfully prepared by electropolymerizing scopoletin in the presence of alkaline-inactivated enzyme. Laccase-MIP and the control polymer without laccase (nonimprinted polymer, NIP) were characterized by voltammetry using the redox marker ferricyanide. After electropolymerization, the signals for ferricyanide for both the MIP and the NIP were almost completely suppressed and increased after removal of the target from the polymer layer. Rebinding of both inactivated and active laccase decreased the ferricyanide peak currents to almost equal extent. The relative decrease of signal suppression approached saturation above 10 nM. Furthermore, the surface activity of rebound laccase toward the oxidation of catechol was investigated. The surface activity approached saturation above 10 nM, a value close to the value of the measurements with ferricyanide. Interaction of NIP with laccase brought about a six times smaller signal of catechol oxidation. KW - Molecularly imprinted polymers KW - Biomimetic sensors KW - Laccase KW - Electropolymerization KW - Scopoletin Y1 - 2018 U6 - https://doi.org/10.1002/bkcs.11413 SN - 1229-5949 VL - 39 IS - 4 SP - 483 EP - 488 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Zhang, Xiaorong A1 - Yarman, Aysu A1 - Erdossy, Julia A1 - Katz, Sagie A1 - Zebger, Ingo A1 - Jetzschmann, Katharina J. A1 - Altintas, Zeynep A1 - Wollenberger, Ulla A1 - Gyurcsanyi, Robert E. A1 - Scheller, Frieder W. T1 - Electrosynthesized MIPs for transferrin BT - Plastibodies or nano-filters? JF - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics N2 - Molecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered. KW - Molecularly imprinted polymer KW - Scopoletin KW - Transferrin KW - Protein adsorption KW - Redox marker Y1 - 2018 U6 - https://doi.org/10.1016/j.bios.2018.01.011 SN - 0956-5663 SN - 1873-4235 VL - 105 SP - 29 EP - 35 PB - Elsevier CY - Oxford ER -