Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F15%3A50003670" target="_blank" >RIV/62690094:18450/15:50003670 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00179906:_____/15:10296242

Výsledek na webu

<a href="http://dx.doi.org/10.1080/07391102.2014.989408" target="_blank" >http://dx.doi.org/10.1080/07391102.2014.989408</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/07391102.2014.989408" target="_blank" >10.1080/07391102.2014.989408</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents

Popis výsledku v původním jazyce

Nerve agents are organophosphates acting as potent inhibitors of acetylcholinesterase (AChE), the enzyme responsible for the hydrolysis of acetylcholine and, consequently, the termination of the transmission of nerve impulses. The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. In this sense, the oximes are compounds capable of removing the nerve agent and reactivate the enzyme. Here, we have applied amethodology involving theoretical docking and Quantum Mechanics/Molecular Mechanics, using the softwares Molegro(R) and Spartan(R), to evaluate the kinetic constants of reactivation and the interactions of the oxime BI-6 with AChE inhibited by differentorganophosphorus compounds in comparison to in vitro data. Results confirm that this method is suitable for the prediction of kinetic and thermodynamic parameters of oximes, which may be useful in the design and selection of new and more

Název v anglickém jazyce

Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents

Popis výsledku anglicky

Nerve agents are organophosphates acting as potent inhibitors of acetylcholinesterase (AChE), the enzyme responsible for the hydrolysis of acetylcholine and, consequently, the termination of the transmission of nerve impulses. The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. In this sense, the oximes are compounds capable of removing the nerve agent and reactivate the enzyme. Here, we have applied amethodology involving theoretical docking and Quantum Mechanics/Molecular Mechanics, using the softwares Molegro(R) and Spartan(R), to evaluate the kinetic constants of reactivation and the interactions of the oxime BI-6 with AChE inhibited by differentorganophosphorus compounds in comparison to in vitro data. Results confirm that this method is suitable for the prediction of kinetic and thermodynamic parameters of oximes, which may be useful in the design and selection of new and more

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Journal of biomolecular structure and dynamics

ISSN

0739-1102

e-ISSN

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Svazek periodika

33

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

2048-2058

Kód UT WoS článku

000358144400016

EID výsledku v databázi Scopus

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