Design and Synthesis of Novel PAS-linked Quinone Methide Precursors as Potential Resurrectors and Reactivators of Organophosphorus-aged and Organophosphorus-inhibited Acetylcholinesterase

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2025-05

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The Ohio State University

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Abstract

Organophosphorus (OP) compounds account for more than 3 million annual hospitalizations and more than 220,000 annual deaths. OP compounds covalently inhibit acetylcholinesterase (AChE), a cholinergic enzyme responsible for the hydrolysis of acetylcholine (ACh). The inhibition of AChE by an OP compound prevents the enzyme from hydrolyzing ACh, resulting in an accumulation of ACh in the synaptic cleft. The overstimulation of post-synaptic neurons by the accumulated ACh produces cholinergic crisis, which may result in death if left untreated. Fortunately, current therapeutics exist which can return OP-inhibited AChE to its native state. However, after inhibition, OP-inhibited AChE may also undergo a spontaneous O-dealkylation event to produce OP-aged AChE. There are currently no approved therapeutics capable of recovering OP-aged AChE. Previous work in our lab has identified a class of novel compounds, quinone methide precursors (QMPs), that can recover OP-inhibited and OP-aged AChE. Herein, we describe the development of novel QMP therapeutics that were designed to increase binding affinity via binding to residues of the peripheral anionic site (PAS) of AChE. These compounds demonstrate reactivation of several OP-inhibited structures, including pesticides and phosphoramidates. These novel QMP therapeutics further demonstrate resurrection of methylphosphonate-aged AChE. The design, synthesis, and in vitro biochemical screening of these novel potential therapeutics will be presented in hopes of identifying a broad-scope medical countermeasure capable of combatting OP exposure.

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Organophosphorus Compounds, Acetylcholinesterase (AChE), Organic Synthesis, Structure Activity Relationship (SAR), Biochemical Screening

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