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  - Menger, Marcus
A1  - Yarman, Aysu
A1  - Erdössy, Júlia
A1  - Yildiz, Huseyin Bekir
A1  - Gyurcsányi, Róbert E.
A1  - Scheller, Frieder W.
T1  - MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing
JF  - Biosensors : open access journal
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.
KW  - biomimetic recognition elements
KW  - aptamers
KW  - molecularly imprinted polymers
KW  - chemical sensors
KW  - aptasensors
KW  - in vitro selection
KW  - SELEX
Y1  - 2016
U6  - https://doi.org/10.3390/bios6030035
SN  - 2079-6374
VL  - 6
SP  - 4399
EP  - 4413
PB  - MDPI
CY  - Basel
ER  -