TY  - JOUR
A1  - Ozcelikay, Goksu
A1  - Kurbanoglu, Sevinc
A1  - Zhang, Xiaorong
A1  - Söz, Çağla Kosak
A1  - Wollenberger, Ulla
A1  - Ozkan, Sibel A.
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - Electrochemical MIP Sensor for Butyrylcholinesterase
JF  - Polymers
N2  - Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range.
KW  - molecularly imprinted polymers
KW  - biomimetic sensors
KW  - butyrylcholinesterase
KW  - o-phenylenediamine
KW  - rivastigmine
Y1  - 2019
U6  - https://doi.org/10.3390/polym11121970
SN  - 2073-4360
VL  - 11
IS  - 12
PB  - MDPI
CY  - Basel
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  - 
TY  - THES
A1  - Zhang, Xiaorong
T1  - Electrosynthesis and characterization of molecularly imprinted polymers for peptides and proteins
Y1  - 2019
ER  -