Monooxime bispyridinium reactivators bearing xylene linker synthesis and in vitro evaluation on model of organophosphate-inhibited acetylcholinesterase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F16%3A43875596" target="_blank" >RIV/60162694:G44__/16:43875596 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00179906:_____/16:10324106 RIV/62690094:18470/16:50004700 RIV/00216208:11160/16:10324106

Výsledek na webu

<a href="http://www.eurekaselect.com/135485/article" target="_blank" >http://www.eurekaselect.com/135485/article</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2174/1573406411666151002125640" target="_blank" >10.2174/1573406411666151002125640</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Monooxime bispyridinium reactivators bearing xylene linker synthesis and in vitro evaluation on model of organophosphate-inhibited acetylcholinesterase

Popis výsledku v původním jazyce

Nine novel mono-oxime reactivators bearing xylene linker were synthesized in an effort to improve previously prepared xylene bisoximes and monocarbamoyl-monooximes. The novel compounds were tested in vitro on the model of tabun-, paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte AChE. Their reactivation ability was compared to pralidoxime, asoxime, obidoxime and two previously prepared xylene linked bisoximes (K107, K108). All compounds showed minimal reactivation of tabun-inhibited AChE at selected concentration scale. This finding was explained by molecular modelling study. Bisoximes obidoxime and K108 resulted as the best reactivators for paraoxon-, methylparaoxon-and DFP-inhibited AChE. The loss of non-oxime moiety lead to the loss of reactivation ability within the novel compounds. Though the novel reactivators did not exceed previously known compounds, they confirmed former SAR findings for xylene-linked AChE reactivators.

Název v anglickém jazyce

Monooxime bispyridinium reactivators bearing xylene linker synthesis and in vitro evaluation on model of organophosphate-inhibited acetylcholinesterase

Popis výsledku anglicky

Nine novel mono-oxime reactivators bearing xylene linker were synthesized in an effort to improve previously prepared xylene bisoximes and monocarbamoyl-monooximes. The novel compounds were tested in vitro on the model of tabun-, paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte AChE. Their reactivation ability was compared to pralidoxime, asoxime, obidoxime and two previously prepared xylene linked bisoximes (K107, K108). All compounds showed minimal reactivation of tabun-inhibited AChE at selected concentration scale. This finding was explained by molecular modelling study. Bisoximes obidoxime and K108 resulted as the best reactivators for paraoxon-, methylparaoxon-and DFP-inhibited AChE. The loss of non-oxime moiety lead to the loss of reactivation ability within the novel compounds. Though the novel reactivators did not exceed previously known compounds, they confirmed former SAR findings for xylene-linked AChE reactivators.

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

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Medicinal Chemistry

ISSN

1573-4064

e-ISSN

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Svazek periodika

12

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

AE - Spojené arabské emiráty

Počet stran výsledku

9

Strana od-do

362-370

Kód UT WoS článku

000376450400006

EID výsledku v databázi Scopus

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