| MAKOWER, Alexander, Jan HALÁMEK, Petr SKLÁDAL, Franz KERNCHENC and Frieder SCHELLER. New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors. Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, 2003, vol. 18, No 11, p. 1329-1337. ISSN 0956-5663. |
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@article{488275,
author = {Makower, Alexander and Halámek, Jan and Skládal, Petr and Kernchenc, Franz and Scheller, Frieder},
article_location = {Oxford},
article_number = {11},
keywords = {cholinesterase; inhibitor; piezoelectric; biosensor; real-time},
language = {eng},
issn = {0956-5663},
journal = {Biosensors & Bioelectronics},
title = {New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors},
volume = {18},
year = {2003}
}
TY - JOUR
ID - 488275
AU - Makower, Alexander - Halámek, Jan - Skládal, Petr - Kernchenc, Franz - Scheller, Frieder
PY - 2003
TI - New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors
JF - Biosensors & Bioelectronics
VL - 18
IS - 11
SP - 1329-1337
EP - 1329-1337
PB - Elsevier Advanced Technology
SN - 09565663
KW - cholinesterase
KW - inhibitor
KW - piezoelectric
KW - biosensor
KW - real-time
N2 - A new method for the sensitive detection of cholinesterase inhibitors based on real-time monitoring using a piezoelectric biosensor. The cholinesterase inhibitor paraoxon was immobilized on the sensing surface via a chelate complex as the recognition element. At first, the conjugate of N?mercaptoundecanoic acid (MUA) with Ná, Ná-bis (carboxymethyl)-L-Lysine (NTA-Lys) was chemisorbed to form a self-assembled monolayer on the surface of the gold electrode of the piezosensor. In the next step, paraoxon-spacer-hexahistidine conjugate was linked to the MUA-Lys-NTA layer via the chelate complex with Ni2+. The paraoxon-modified surface thus obtained was applied for the binding of human butyrylcholinesterase. Regeneration of the sensing surface was achieved by splitting the chelate complex with EDTA and depositing a fresh layer of Ni2+ followed by addition of the paraoxon-spacer-hexahistidine. In the presence of free inhibitors like diisopropylfluorphosphate (DFP), binding of BChE to the surface-bound paraoxon was decreased. In this way, a competitive affinity assay for organophosphorus compounds was developed. The limit of detection for DFP as a model compound was 10 nmol/l (approx. 2 mg/l). This new concept seems suitable for constructing biosensors for the group-specific detection of cholinesterase-inhibiting substances like insecticides in the field.
ER -
MAKOWER, Alexander, Jan HALÁMEK, Petr SKLÁDAL, Franz KERNCHENC and Frieder SCHELLER. New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors. \textit{Biosensors \&{} Bioelectronics}. Oxford: Elsevier Advanced Technology, 2003, vol.~18, No~11, p.~1329-1337. ISSN~0956-5663.
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