Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F12%3A39894709" target="_blank" >RIV/00216275:25310/12:39894709 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11160/12:10124283 RIV/62157124:16370/12:43871097

Výsledek na webu

<a href="http://dx.doi.org/10.3390/molecules170910142" target="_blank" >http://dx.doi.org/10.3390/molecules170910142</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/molecules170910142" target="_blank" >10.3390/molecules170910142</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking

Popis výsledku v původním jazyce

A series of twenty-five novel salicylanilide N-alkylcarbamates were investigated as potential acetylcholinesterase inhibitors. The compounds were tested for their ability to inhibit acetylcholinesterase (AChE) from electric eel (Electrophorus electricusL.). Experimental lipophilicity was determined, and the structure-activity relationships are discussed. The mode of binding in the active site of AChE was investigated by molecular docking. All the discussed compounds expressed significantly higher AChEinhibitory activity than rivastigmine and slightly lower than galanthamine. Disubstitution by chlorine in C-(3,C-4)' of the aniline ring and the optimal length of hexyl-undecyl alkyl chains in the carbamate moiety provided the most active AChE inhibitors. Monochlorination in C-(4)' exhibited slightly more effective AChE inhibitors than in C-(3)'. Generally it can be stated that compounds with higher lipophilicity showed higher inhibition, and the activity of the compounds is strongly dep

Název v anglickém jazyce

Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking

Popis výsledku anglicky

A series of twenty-five novel salicylanilide N-alkylcarbamates were investigated as potential acetylcholinesterase inhibitors. The compounds were tested for their ability to inhibit acetylcholinesterase (AChE) from electric eel (Electrophorus electricusL.). Experimental lipophilicity was determined, and the structure-activity relationships are discussed. The mode of binding in the active site of AChE was investigated by molecular docking. All the discussed compounds expressed significantly higher AChEinhibitory activity than rivastigmine and slightly lower than galanthamine. Disubstitution by chlorine in C-(3,C-4)' of the aniline ring and the optimal length of hexyl-undecyl alkyl chains in the carbamate moiety provided the most active AChE inhibitors. Monochlorination in C-(4)' exhibited slightly more effective AChE inhibitors than in C-(3)'. Generally it can be stated that compounds with higher lipophilicity showed higher inhibition, and the activity of the compounds is strongly dep

Druh

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

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Molecules

ISSN

1420-3049

e-ISSN

—

Svazek periodika

17

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

17

Strana od-do

10142-10158

Kód UT WoS článku

000309269700013

EID výsledku v databázi Scopus

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