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Oxime-mediated in vitro reactivation kinetic analysis of organophosphates-inhibited human and electric eel acetylcholinesterase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F16%3A50004737" target="_blank" >RIV/62690094:18470/16:50004737 - isvavai.cz</a>

  • Alternative codes found

    RIV/00179906:_____/16:10330362

  • Result on the web

    <a href="http://www.tandfonline.com/doi/abs/10.3109/15376516.2016.1143070?journalCode=itxm20" target="_blank" >http://www.tandfonline.com/doi/abs/10.3109/15376516.2016.1143070?journalCode=itxm20</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3109/15376516.2016.1143070" target="_blank" >10.3109/15376516.2016.1143070</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Oxime-mediated in vitro reactivation kinetic analysis of organophosphates-inhibited human and electric eel acetylcholinesterase

  • Original language description

    Organophosphate (OP)-based pesticides and nerve agents are highly toxic compounds which interrupt the catalytic mechanism of acetylcholinesterase (AChE) by phosphorylating the hydroxyl moiety of serine residue. The inhibited enzyme can be reactivated by the nucleophilic action of oxime reactivators. To analyze the effect of different AChE sources on reactivation efficacy of reactivators, several in vivo studies have carried out using variety of AChE sources like pig, rat and monkey. Investigations on species differences provide a better insight for the development of new reactivators. Hence, present study was mainly targeted on comparative analysis of the reactivation of electric eel and human AChE inhibited by different OP. A series of butene-linked bis-pyridinium mono oximes which vary in functional groups present at the second pyridinium ring have been examined against sarin, VX, tabun and ethyl-paraoxon-poisoned AChE. In case of tabun-inhibited AChEs, tested oximes were better than reference oximes. For VX-poisoned human AChE, reactivator K251 (k(r2);1.51mM(-1)min(-1)) showed good reactivation efficacy with standard oximes. Studies stipulated that butene-linked oximes consisting of different functional moieties are good reactivators and found to have better efficacy to reactivate nerve agent-inhibited human AChE in comparison to eel AChE.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FR - Pharmacology and apothecary chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/LH13009" target="_blank" >LH13009: The research of modified cholinesterase reactivators for organophosphorus pesticide poisoning treatment</a><br>

  • Continuities

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

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Toxicology mechanisms and methods

  • ISSN

    1537-6516

  • e-ISSN

  • Volume of the periodical

    26

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    319-326

  • UT code for WoS article

    000380053100002

  • EID of the result in the Scopus database