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Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates
Authors: Kovářová Markéta | Khan Mahmud T.H. | Komers Karel | Pařík Patrik | Čegan Alexander | Zatloukalová Martina
Year: 2011
Type of publication: článek v odborném periodiku
Name of source: Current Enzyme Inhibition
Publisher name: Bentham Science Publishers Ltd.
Place: Bussum
Page from-to: 236-243
Titles:
Language Name Abstract Keywords
cze Kinetika in vitro inhibice acetylcholinesterázy pomocí devatenácti nových karbamát Dvě série A a B obsahující 12 a 7 nových karbamátů byly testovány in vitro jako acetylcholinesterázové inhibitory. Testy byly zpracovány v reaktoru při 25°C, pH 8, iontové síle 0,11 M a katalytické aktivitě enzymu v připravené reakční směsi 0,14 U ml-1.Závislosti koncentrací jednotlivých látek v reakční směsi byly sledovány dvěma nezávislými analytickými metodami, HPLC a pH-stat. Ze získaných dat byla vypočtena inhibiční rychlost. acetylcholin; hydrolýza; enzymatický; in vitro; karbamát; inhibice; kinetika
eng Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates 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. Acetylcholine; hydrolysis; enzymatic; in vitro; acetylcholinesterase; carbamates; inhibition; kinetics; HPLC; docking energies

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