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  - 
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  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Wollenberger, Ulla
A1  - Gyurcsányi, Róbert E.
T1  - Molecularly imprinted polymer-based electrochemical sensors for biopolymers
JF  - Current opinion in electrochemistry
N2  - Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one ‘separation plate’; thus, the selectivity does not reach the values of ‘bulk’ measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an ‘overall apparent’ signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.
KW  - Electropolymerization
KW  - Direct electron transfer
KW  - Redox marker
KW  - Epitope imprinting
KW  - Biomarker
Y1  - 2018
U6  - https://doi.org/10.1016/j.coelec.2018.12.005
SN  - 2451-9103
VL  - 14
SP  - 53
EP  - 59
PB  - Elsevier
CY  - Amsterdam
ER  -