ArticleACS chemical biology2026
Fragment-Based Discovery of Fenamic Acids as Pan-Species Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain.
Article in ACS chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Targeting the N-terminal phosphatase domain of soluble epoxide hydrolase (sEH) could potentially represent a pharmacological strategy for treatment of cardiometabolic diseases. However, development of chemical tools to investigate the therapeutic potential of sEH phosphatase (sEH-P) inhibition has proven challenging due to varying activities between different species isoforms and lack of selectivity toward the C-terminal hydrolase domain, which exhibits the epoxide hydrolase activity (sEH-H). Herein, we describe the fragment-based discovery of FZ581 (49), an sEH-P inhibitor against human, rat, and mouse isoforms. In vivo studies with this compound in mice and rats demonstrated a significant increase of main sEH-P substrate levels without affecting plasma levels of sEH-H substrates. Altogether, we provide a pan-species sEH-P inhibitor to study the pharmacotherapeutic potential of sEH-P inhibition.
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