Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F11%3A39895922" target="_blank" >RIV/00216275:25310/11:39895922 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.2174/157340811799860560" target="_blank" >http://dx.doi.org/10.2174/157340811799860560</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2174/157340811799860560" target="_blank" >10.2174/157340811799860560</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates

Popis výsledku v původním jazyce

Two series A and B of 12 and 7 new carbamate derivates were tested in vitro as acetylcholinesterase inhibitors. The tests were performed in the batch stirred reactor at 25°C, pH 8, ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U mL-1 of the reaction mixture. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by two independent analytical methods, HPLC and pH-stat. For all used inhibitors, the model of competitive irreversible inhibition was valid. The inhibition rate constant k3 and qualified estimation of the absolute acetylcholinesterase concentration in the reaction mixture were calculated. The partition coefficients Kow between n-octanol and water of all used inhibitors were determined. The k3 and Kow values were correlated with the Hammett and Hansch substituent constants and with the calculated docking and binding energies of the reaction between the tested inhibitors and acetylcholinesterase.

Název v anglickém jazyce

Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates

Popis výsledku anglicky

Two series A and B of 12 and 7 new carbamate derivates were tested in vitro as acetylcholinesterase inhibitors. The tests were performed in the batch stirred reactor at 25°C, pH 8, ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U mL-1 of the reaction mixture. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by two independent analytical methods, HPLC and pH-stat. For all used inhibitors, the model of competitive irreversible inhibition was valid. The inhibition rate constant k3 and qualified estimation of the absolute acetylcholinesterase concentration in the reaction mixture were calculated. The partition coefficients Kow between n-octanol and water of all used inhibitors were determined. The k3 and Kow values were correlated with the Hammett and Hansch substituent constants and with the calculated docking and binding energies of the reaction between the tested inhibitors and acetylcholinesterase.

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Current Enzyme Inhibition

ISSN

1573-4080

e-ISSN

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Svazek periodika

7

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

236-243

Kód UT WoS článku

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EID výsledku v databázi Scopus

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