New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008862" target="_blank" >RIV/00216224:14310/03:00008862 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors

Popis výsledku v původním jazyce

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 bysplitting 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 surfa

Název v anglickém jazyce

New principle for the direct real-time monitoring of interaction of cholinesterase and its inhibitors

Popis výsledku anglicky

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 bysplitting 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 surfa

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/OC%20518.30" target="_blank" >OC 518.30: Sledování interakcí biomakromolekul s biovrstvami v různých konformačních stavech pomocí piezoelektrických biosensorů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biosensors & Bioelectronics

ISSN

0956-5663

e-ISSN

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Svazek periodika

18

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

1329-1337

Kód UT WoS článku

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EID výsledku v databázi Scopus

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