TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.
KW  - Paracetamol
KW  - Molecularly imprinted polymers
KW  - Electropolymerization
KW  - Tyrosinase
KW  - Esterase
KW  - Phenacetin
Y1  - 2016
U6  - https://doi.org/10.1002/elan.201600042
SN  - 1040-0397
SN  - 1521-4109
VL  - 28
SP  - 2222
EP  - 2227
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Jetzschmann, Katharina J.
A1  - Yarman, Aysu
A1  - Rustam, L.
A1  - Kielb, P.
A1  - Urlacher, V. B.
A1  - Fischer, A.
A1  - Weidinger, I. M.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
T1  - Molecular LEGO by domain-imprinting of cytochrome P450 BM3
JF  - Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces
N2  - Hypothesis: Electrosynthesis of the MIP nano-film after binding of the separated domains or holocytochrome BM3 via an engineered anchor should result in domain-specific cavities in the polymer layer. Experiments: Both the two domains and the holo P450 BM3 have been bound prior polymer deposition via a N-terminal engineered his6-anchor to the electrode surface. Each step of MIP preparation was characterized by cyclic voltammetry of the redox-marker ferricyanide. Rebinding after template removal was evaluated by quantifying the suppression of the diffusive permeability of the signal for ferricyanide and by the NADH-dependent reduction of cytochrome c by the reductase domain (BMR). Findings: The working hypothesis is verified by the discrimination of the two domains by the respective MIPs: The holoenzyme P450 BM3 was ca. 5.5 times more effectively recognized by the film imprinted with the oxidase domain (BMO) as compared to the BMR-MIP or the non-imprinted polymer (NIP). Obviously, a cavity is formed during the imprinting process around the hiss-tag-anchored BMR which cannot accommodate the broader BMO or the P450 BM3. The affinity of the MIP towards P450 BM3 is comparable with that to the monomer in solution. The hiss-tagged P450 BM3 binds (30 percent) stronger which shows the additive effect of the interaction with the MIP and the binding to the electrode.
KW  - Molecularly imprinted polymers
KW  - Protein imprinting
KW  - Electropolymerization
KW  - Cytochrome P450
Y1  - 2018
U6  - https://doi.org/10.1016/j.colsurfb.2018.01.047
SN  - 0927-7765
SN  - 1873-4367
VL  - 164
SP  - 240
EP  - 246
PB  - Elsevier
CY  - Amsterdam
ER  -