TY  - JOUR
A1  - Erdossy, Julia
A1  - Horvath, Viola
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Robert E.
T1  - Electrosynthesized molecularly imprinted polymers for protein recognition
JF  - Trends in Analytical Chemistry
N2  - 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.
KW  - Molecularly imprinted polymers
KW  - Proteins
KW  - Surface imprinting
KW  - Electropolymerization
KW  - Nanostructuring
KW  - Hybrid nanofilms
Y1  - 2016
U6  - https://doi.org/10.1016/j.trac.2015.12.018
SN  - 0165-9936
SN  - 1879-3142
VL  - 79
SP  - 179
EP  - 190
PB  - Elsevier
CY  - Oxford
ER  - 
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  -