Reactivation of immobilized acetylcholinesterase-tabun complex by methoxime and its homologues

Drug Chem Toxicol. 2007;30(2):97-103. doi: 10.1080/01480540601186614.

Abstract

Using an immobilized acetylcholinesterase-tabun enzyme-inhibitor complex, the reactivation efficacy of a homologous series of bispyridinium reactivators with increasing length of the alkylene chain between the pyridinium rings has been studied. The number of the alkylene groups in the chain ranged from one to six. N,N'-Monomethylenebis(4-pyridiniumaldoxime) dibromide (MMB-4) and N,N'-trimethylenebis(4-pyridiniumaldoxime) dibromide (TMB-4) are the most efficient reactivators of the series.

MeSH terms

  • Acetylcholinesterase / drug effects*
  • Acetylcholinesterase / metabolism
  • Animals
  • Chemical Warfare Agents / toxicity
  • Cholinesterase Inhibitors / toxicity
  • Cholinesterase Reactivators / pharmacology*
  • Enzymes, Immobilized
  • Organophosphates / toxicity
  • Oximes / pharmacology*
  • Pyridinium Compounds / pharmacology*
  • Structure-Activity Relationship
  • Swine

Substances

  • Chemical Warfare Agents
  • Cholinesterase Inhibitors
  • Cholinesterase Reactivators
  • Enzymes, Immobilized
  • Organophosphates
  • Oximes
  • Pyridinium Compounds
  • N,N'-monomethylenebis(pyridiniumaldoxime)
  • Acetylcholinesterase
  • tabun