Immobilization of Organophosphorus Acid Anhydrolase Mutant Y212F on Silica Nanospheres

Abstract

We have engineered mutants of the wild type organophosphorus acid anhydrolase (OPAA) for activity on G-type chemical nerve agents and observed increased activity on the most-toxic enantiomers. Enzyme stability might be enhanced by attachment of the OPAA to a silicon dioxide nanoparticle. Conjugation of our enzyme mutant was performed by personnel at nanoComposix (San Diego, CA), which is a producer of customized nanoparticles. After conjugation, the activity of the enzymeparticle combination on pinacolyl methyl phosphonofluoridate (GD, soman) was measured and compared with free enzyme. Activity measurements were made to compare a free and immobilized OPAA mutant on the G-agent stimulant diisopropyl fluorophosphates (DFP) and soman.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 2016
Accession Number
AD1018277

Entities

People

  • Mark A. Guelta
  • Melissa M. Dixon
  • Richard Baldwin
  • Steven P. Harvey

Organizations

  • Edgewood Chemical Biological Center

Tags

Communities of Interest

  • Counter WMD
  • Human Systems

DTIC Thesaurus Topics

  • Amino Acids
  • Biological Sciences
  • Chemical Synthesis
  • Chemical Warfare Agents
  • Chemical Weapons
  • Chemistry
  • Department Of Homeland Security
  • Electron Microscopes
  • Electron Microscopy
  • G Agents
  • Materials
  • Molecules
  • Nanoparticles
  • Nerve Agents
  • Particles
  • Poisoning
  • Silicon Dioxide

Readers

  • Analytical Chemistry
  • Nanocomposite Materials Science
  • Neurotoxicology

Technology Areas

  • Biotechnology