TY  - JOUR
A1  - Bauer, Christian G.
A1  - Eremenko, A. V.
A1  - Ehrentreich-Förster, Eva
A1  - Bier, Frank Fabian
A1  - Makower, Alexander
A1  - Halsall, H. B.
A1  - Heineman, W. R.
A1  - Scheller, Frieder W.
T1  - Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Schubert, Florian
A1  - Bier, Frank Fabian
T1  - Vom Biosensor zur Nanobiotechnologie
Y1  - 1995
ER  - 
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  - 
TY  - JOUR
A1  - Bier, Frank Fabian
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
A1  - Makower, Alexander
A1  - Eremenko, A. V.
A1  - Wollenberger, Ursula
A1  - Bauer, Christian G.
A1  - Pfeiffer, Dorothea
A1  - Micheel, Burkhard
T1  - Ultrasensitive biosensors
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Szeponik, Jan
A1  - Möller, B.
A1  - Pfeiffer, Dorothea
A1  - Lisdat, Fred
A1  - Wollenberger, Ursula
A1  - Makower, Alexander
A1  - Scheller, Frieder W.
T1  - Ultrasensitive bienzyme sensor for adrenaline
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Makower, Alexander
A1  - Eremenko, A. V.
A1  - Streffer, Katrin
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Tribute to Guenter Gauglitz (Editorial)
Y1  - 2009
UR  - http://www.springerlink.com/content/100417
U6  - https://doi.org/10.1007/s00216-008-2548-0
SN  - 1618-2642
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bier, Frank Fabian
T1  - Trends in der Bioanalytik
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Nießner, Reinhard
A1  - Broekaert, J.
A1  - Einax, J. W.
A1  - Scheller, Frieder W.
A1  - Stöcklein, Walter F. M.
T1  - Trendbericht analytische Biochemie 2000/2001
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Bistolas, Nikitas
A1  - Liu, Songqin
A1  - Jänchen, Michael
A1  - Katterle, Martin
A1  - Wollenberger, Ursula
T1  - Thirty years of haemoglobin electrochemistry
N2  - Electrochemical investigations of the blood oxygen carrier protein include both mediated and direct electron transfer. The reaction of haemoglobin (Hb) with typical mediators, e.g., ferricyanide, can be quantified by measuring the produced ferrocyanide which is equivalent to the Hb concentration. Immobilization of the mediator within the electrode body allows reagentless electrochemical measuring of Hb. On the other hand, entrapment of the protein within layers of polyclectrolytes, lipids, nanoparticles of clay or gold leads to a fast heterogeneous electron exchange of the partially denatured Hb. (c) 2005 Elsevier B.V. All rights reserved
Y1  - 2005
ER  -