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The multiple-tentacle box jellyfish, (Sucharitakul, 2017) and (Horst, 1907), are venomous species found in Thai waters. They are responsible for numerous envenomations through their stinging organelles, nematocysts. These specialized microscopic structures discharge venom, yet detailed knowledge of their types and morphology in these species remains limited.

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Article Synopsis
  • Many marine animals, particularly Cnidarians like jellyfish, can be dangerous to humans and often cause painful burns, especially in tropical waters.
  • Contact with their toxins may lead to acute kidney damage, with varying effects depending on the specific species of Cnidaria involved.
  • Currently, there's one specific antitoxin for Cnidarian-induced burns, but research is ongoing to develop a universal treatment that could neutralize toxins from various Cnidarian species.
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Molecular evolution of ovothiol biosynthesis in animal life reveals diversity of the natural antioxidant ovothiols in Cnidaria.

Free Radic Biol Med

February 2025

Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, 80131, Naples, Italy; Department of Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy. Electronic address:

Sulfoxide synthase OvoA is the key enzyme involved in the biosynthesis of ovothiols (OSHs), secondary metabolites endowed with unique antioxidant properties. Understanding the evolution of such enzymes and the diversity of their metabolites should reveal fundamental mechanisms governing redox signaling and environmental adaptation. "Early-branching" animals such as Cnidaria display unique molecular diversity and symbiotic relationships responsible for the biosynthesis of natural products, however, they have been neglected in previous research on antioxidants and OSHs.

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The aim of this study was to prepare and characterize jellyfish collagen peptide (JCP)-calcium chelates (JCP-Ca) using peptides with different molecular weights. Further analysis revealed that the low-molecular-weight jellyfish collagen peptide (JCP1) had a higher chelation rate. Structural characterization showed that functional groups such as N-H, C[bond, double bond]O, and -COO were involved in the formation of JCP-Ca, which shifted towards a more ordered and regular structure, and smaller-molecular-weight peptides were more likely to form a denser structure.

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Article Synopsis
  • Envenomation from jellyfish can lead to severe skin reactions known as jellyfish dermatitis, whose treatment is complicated by various venom components.
  • The study evaluated Troxerutin (TRX) as a potential treatment using mice models and various assays to analyze its effects on inflammation and oxidative damage caused by jellyfish venom.
  • Results showed that TRX significantly reduced skin toxicity and inflammation by inhibiting key signaling pathways, suggesting it could be an effective new therapy for jellyfish dermatitis.
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