Increased organophosphate scavenging in a butyrylcholinesterase mutant

Brian C. Geyer, Ryan R. Woods, Tsafrir Leket-Mor

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Nicotiana benthamiana plant lines expressing a reengineered human butyrylcholinesterase (BChE) with enhanced cocaine hydrolase activity were created. Subsequent purification and biochemical analysis revealed that compared to wild-type butyrylcholinesterase, the cocaine hydrolase displayed increased affinity to the organophosphate (OP) pesticides paraoxon (6.84 × 10-10 M vs. 1.11 × 10-8 M) and malaoxon (9.81 × 10-8 M vs. 5.99 × 10-7 M). Furthermore, the cocaine hydrolase retained identical anticholinesterase binding profiles for all other compounds tested. Thus we have demonstrated a potential large-scale production platform for a multivalent antidote for cocaine and anticholinesterase poisoning.

Original languageEnglish (US)
Pages (from-to)376-379
Number of pages4
JournalChemico-Biological Interactions
Volume175
Issue number1-3
DOIs
StatePublished - Sep 25 2008

Keywords

  • Bioscavenger
  • Cocaine hydrloase
  • Molecular pharming
  • Nerve agents
  • Pesticides
  • Transgenic plants

ASJC Scopus subject areas

  • Toxicology

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