ArticleCell biology and toxicology2026
Mechanism of palytoxin-induced ferroptosis in HaCaT cells via targeting TrxR1.
Article in Cell biology and toxicology, 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
PLTX (Palytoxin) is a fatty-chain polyether marine biotoxin originally produced by benthic dinoflagellates, particularly Ostreopsis ovata and Ostreopsis siamensis. Via the marine food web, PLTX bioaccumulates in numerous organisms such as corals and shellfish, and ranks among the most lethal non-proteinaceous natural compounds described to date. Thus far, its toxicological mechanism remains unclear, and no specific clinical antidote is available. In this study, we employed a limited proteolysis‑based chemical proteomics approach (Lip‑SMap) to analyze the protection of protease cleavage sites conferred by PLTX binding. Combined with DIA (data‑independent acquisition) mass spectrometry in HaCaT (human immortalized keratinocyte) cells, we identified TrxR1 (thioredoxin reductase 1) as an intracellular direct target of PLTX. Molecular docking simulations revealed that PLTX forms stable hydrogen bonds with the active‑site residues Q230 and N234 of TrxR1. BLI (Biolayer interferometry) further confirmed a moderate‑to‑high affinity interaction between them (KD = 5.415 × 10
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