Increased organophosphate scavenging in a butyrylcholinesterase mutant

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

Research output: Contribution to journalArticle

8 Citations (Scopus)

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

Fingerprint

Butyrylcholinesterase
Organophosphates
Scavenging
Cocaine
Hydrolases
Cholinesterase Inhibitors
Paraoxon
Production platforms
Antidotes
Pesticides
Poisoning
Tobacco
Purification

Keywords

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

ASJC Scopus subject areas

  • Toxicology

Cite this

Increased organophosphate scavenging in a butyrylcholinesterase mutant. / Geyer, Brian C.; Woods, Ryan R.; Leket-Mor, Tsafrir.

In: Chemico-Biological Interactions, Vol. 175, No. 1-3, 25.09.2008, p. 376-379.

Research output: Contribution to journalArticle

Geyer, Brian C. ; Woods, Ryan R. ; Leket-Mor, Tsafrir. / Increased organophosphate scavenging in a butyrylcholinesterase mutant. In: Chemico-Biological Interactions. 2008 ; Vol. 175, No. 1-3. pp. 376-379.
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