ArticleChemical research in toxicology2015
Catalytic Soman Scavenging by the Y337A/F338A Acetylcholinesterase Mutant Assisted with Novel Site-Directed Aldoximes.
Article in Chemical research in toxicology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 44 citations in OpenAlex.
- Engineered acetylcholinesterase-loaded dissolvable microneedles mitigate dermal toxicity by targeting trichlorfon binding and metabolic pathway modulation.Materials today. Bio · 2026Article
- From Mechanisms to Materials: Oximate Reactivity and Emerging Strategies for Organophosphate Detoxification.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Review
- Article
- Click-chemistry-derived oxime library reveals efficient reactivators of nerve agent-inhibited butyrylcholinesterase suitable for pseudo-catalytic bioscavenging.Archives of toxicology · 2025Article
- A Phenanthroimidazole-Based Luminophore for Selective and Specific Identification of Sarin Simulant, Diethylchlorophosphate.Journal of fluorescence · 2025Article
- Advancements in bioscavenger mediated detoxification of organophosphorus poisoning.Toxicology research · 2024Review
- Structural and dynamic effects of paraoxon binding to human acetylcholinesterase by X-ray crystallography and inelastic neutron scattering.Structure (London, England : 1993) · 2022Article
- Nanomaterial-Enabled Sensors and Therapeutic Platforms for Reactive Organophosphates.Nanomaterials (Basel, Switzerland) · 2021Review
- Counteracting poisoning with chemical warfare nerve agents.Arhiv za higijenu rada i toksikologiju · 2020Review
- Productive reorientation of a bound oxime reactivator revealed in room temperature X-ray structures of native and VX-inhibited human acetylcholinesterase.The Journal of biological chemistry · 2019Article
- Optimization of Cholinesterase-Based Catalytic Bioscavengers Against Organophosphorus Agents.Frontiers in pharmacology · 2018Article
- Immunopurification of Acetylcholinesterase from Red Blood Cells for Detection of Nerve Agent Exposure.Chemical research in toxicology · 2017Article
- HI-6 assisted catalytic scavenging of VX by acetylcholinesterase choline binding site mutants.Chemico-biological interactions · 2016Article
- Efforts toward treatments against aging of organophosphorus-inhibited acetylcholinesterase.Annals of the New York Academy of Sciences · 2016Review
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Exposure to the nerve agent soman is difficult to treat due to the rapid dealkylation of the soman-acetylcholinesterase (AChE) conjugate known as aging. Oxime antidotes commonly used to reactivate organophosphate inhibited AChE are ineffective against soman, while the efficacy of the recommended nerve agent bioscavenger butyrylcholinesterase is limited by strictly stoichiometric scavenging. To overcome this limitation, we tested ex vivo, in human blood, and in vivo, in soman exposed mice, the capacity of aging-resistant human AChE mutant Y337A/F338A in combination with oxime HI-6 to act as a catalytic bioscavenger of soman. HI-6 was previously shown in vitro to efficiently reactivate this mutant upon soman, as well as VX, cyclosarin, sarin, and paraoxon, inhibition. We here demonstrate that ex vivo, in whole human blood, 1 μM soman was detoxified within 30 min when supplemented with 0.5 μM Y337A/F338A AChE and 100 μM HI-6. This combination was further tested in vivo. Catalytic scavenging of soman in mice improved the therapeutic outcome and resulted in the delayed onset of toxicity symptoms. Furthermore, in a preliminary in vitro screen we identified an even more efficacious oxime than HI-6, in a series of 42 pyridinium aldoximes, and 5 imidazole 2-aldoxime N-propylpyridinium derivatives. One of the later imidazole aldoximes, RS-170B, was a 2-3-fold more effective reactivator of Y337A/F338A AChE than HI-6 due to the smaller imidazole ring, as indicated by computational molecular models, that affords a more productive angle of nucleophilic attack.
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