Monooxime-monocarbamoyl bispyridinium xylene linked reactivators of acetylcholinesterase - synthesis, in vitro and toxicity evaluation, and docking studies

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F10%3A00002295" target="_blank" >RIV/60162694:G44__/10:00002295 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/44555601:13440/10:00005548 RIV/00216208:11160/10:00300569

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Monooxime-monocarbamoyl bispyridinium xylene linked reactivators of acetylcholinesterase - synthesis, in vitro and toxicity evaluation, and docking studies

Popis výsledku v původním jazyce

New series of twenty six monooxime-monocarbamoyl xylene linked bispyridinium compounds was prepared. The known reactivators (pralidoxime, HI-6, obidoxime, trimedoxime, methoxime, K107, K108 and K203) and the prepared compounds were tested in vitro on a model of tabun- and paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte acetylcholinesterase. Although their reactivation ability against tabun did not exceed the previously known compounds, some newly prepared compounds showed promising ability in reactivation of pesticide-inhibited AChE. The acute toxicity of the novel compounds was determined. The docking study for tabun-inhibited AChE was performed for 3 compounds of interest. The structure-activity relationship (SAR) study confirmed apparent influence of xylene linkage and carbamoyl moiety on the reactivation ability and toxicity.

Název v anglickém jazyce

Monooxime-monocarbamoyl bispyridinium xylene linked reactivators of acetylcholinesterase - synthesis, in vitro and toxicity evaluation, and docking studies

Popis výsledku anglicky

New series of twenty six monooxime-monocarbamoyl xylene linked bispyridinium compounds was prepared. The known reactivators (pralidoxime, HI-6, obidoxime, trimedoxime, methoxime, K107, K108 and K203) and the prepared compounds were tested in vitro on a model of tabun- and paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte acetylcholinesterase. Although their reactivation ability against tabun did not exceed the previously known compounds, some newly prepared compounds showed promising ability in reactivation of pesticide-inhibited AChE. The acute toxicity of the novel compounds was determined. The docking study for tabun-inhibited AChE was performed for 3 compounds of interest. The structure-activity relationship (SAR) study confirmed apparent influence of xylene linkage and carbamoyl moiety on the reactivation ability and toxicity.

Druh

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

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

ChemMedChem

ISSN

1860-7179

e-ISSN

—

Svazek periodika

5

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

—

Kód UT WoS článku

000274538600009

EID výsledku v databázi Scopus

—