Musilek_2010_ChemMedChem_5_247

Reference

Title : Monooxime-monocarbamoyl Bispyridinium Xylene-Linked Reactivators of Acetylcholinesterase-Synthesis, In vitro and Toxicity Evaluation, and Docking Studies - Musilek_2010_ChemMedChem_5_247
Author(s) : Musilek K , Holas O , Misik J , Pohanka M , Novotny L , Dohnal V , Opletalova V , Kuca K
Ref : ChemMedChem , 5 :247 , 2010
Abstract : Acetylcholinesterase (AChE) reactivators are crucial antidotes to organophosphate intoxication. A new series of 26 monooxime-monocarbamoyl xylene-linked bispyridinium compounds was prepared and tested in vitro, along with known reactivators (pralidoxime, HI-6, obidoxime, trimedoxime, methoxime, K107, K108 and K203), on a model of tabun- and paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte AChE. Although their ability to reactivate tabun-inhibited AChE did not exceed that of the previously known compounds, some newly prepared compounds showed promising reactivation of pesticide-inhibited AChE. The acute toxicity of the novel compounds was also determined. Docking studies using tabun-inhibited AChE were performed for three compounds of interest. The structure-activity relationship (SAR) study confirmed the apparent influence of the xylene linkage and carbamoyl moiety on the reactivation ability and toxicity of the agents.
ESTHER : Musilek_2010_ChemMedChem_5_247
PubMedSearch : Musilek_2010_ChemMedChem_5_247
PubMedID: 20058292

Related information

Reactivator K203

Citations formats

Musilek K, Holas O, Misik J, Pohanka M, Novotny L, Dohnal V, Opletalova V, Kuca K (2010)
Monooxime-monocarbamoyl Bispyridinium Xylene-Linked Reactivators of Acetylcholinesterase-Synthesis, In vitro and Toxicity Evaluation, and Docking Studies
ChemMedChem 5 :247

Musilek K, Holas O, Misik J, Pohanka M, Novotny L, Dohnal V, Opletalova V, Kuca K (2010)
ChemMedChem 5 :247

Array
(
    [id] => 55180
    [paper] => Musilek_2010_ChemMedChem_5_247
    [author] => Musilek K || Holas O || Misik J || Pohanka M || Novotny L || Dohnal V || Opletalova V || Kuca K
    [year] => 2010
    [title] => Monooxime-monocarbamoyl Bispyridinium Xylene-Linked Reactivators of Acetylcholinesterase-Synthesis, In vitro and Toxicity Evaluation, and Docking Studies
    [journal] => ChemMedChem
    [volume] => 5
    [page] => 247
    [medline] => 20058292
    [abstract] => Musilek_2010_ChemMedChem_5_247
    [kin_reference] => 
    [mutation] => 
    [kinetic_parameter] => 
    [inhibitor] => 
    [kin_value] => 
    [substrate] => 
    [gene_locus] => Array
        (
        )

    [family] => 
    [interact_gene_locus] => 
    [xenobiotic_sensitivity] => 
    [news] => 
    [likid_reference] => 
    [lip_reference] => 
    [gene_locus_frgt] => 
    [structure] => 
    [comment] => 
    [chemical] => 
    [arpigny_jaeger] => 
    [reactivator] => K203
    [disease] => 
    [enzyme] => 
    [risk_factor] => 
    [tissue] => 
    [sub_tissue] => 
    [activity] => 
    [specific_activity] => 
    [disease_by_interaction] => 
    [abstract_text] => Array
        (
            [id] => 155353
            [longtext] => Musilek_2010_ChemMedChem_5_247
            [content] => Acetylcholinesterase (AChE) reactivators are crucial antidotes to organophosphate intoxication. A new series of 26 monooxime-monocarbamoyl xylene-linked bispyridinium compounds was prepared and tested in vitro, along with known reactivators (pralidoxime, HI-6, obidoxime, trimedoxime, methoxime, K107, K108 and K203), on a model of tabun- and paraoxon-, methylparaoxon- and DFP-inhibited human erythrocyte AChE. Although their ability to reactivate tabun-inhibited AChE did not exceed that of the previously known compounds, some newly prepared compounds showed promising reactivation of pesticide-inhibited AChE. The acute toxicity of the novel compounds was also determined. Docking studies using tabun-inhibited AChE were performed for three compounds of interest. The structure-activity relationship (SAR) study confirmed the apparent influence of the xylene linkage and carbamoyl moiety on the reactivation ability and toxicity of the agents.
        )

)