TY  - JOUR
A1  - Jetzschmann, Katharina J.
A1  - Jagerszki, Gyula
A1  - Dechtrirat, Decha
A1  - Yarman, Aysu
A1  - Gajovic-Eichelmann, Nenad
A1  - Gilsing, Hans-Detlev
A1  - Schulz, Burkhard
A1  - Gyurcsanyi, Robert E.
A1  - Scheller, Frieder W.
T1  - Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition
JF  - Advanced functional materials
N2  - Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid.
KW  - acetylcholinesterase
KW  - biomimetic sensors
KW  - molecularly imprinted electropolymers
KW  - peripheral anionic site
KW  - propidium
Y1  - 2015
U6  - https://doi.org/10.1002/adfm.201501900
SN  - 1616-301X
SN  - 1616-3028
VL  - 25
IS  - 32
SP  - 5178
EP  - 5183
PB  - Wiley-VCH
CY  - Weinheim
ER  -