Analgesic Compound from Sea Anemone Heteractis crispa Is the First Polypeptide Inhibitor of Vanilloid Receptor 1 (TRPV1)

摘要: Venomous animals from distinct phyla such as spiders, scorpions, snakes, cone snails, or sea anemones produce small toxic proteins interacting with a variety of cell targets. Their bites often cause pain. One the ways pain generation is activation TRPV1 channels. Screening 30 different venoms spiders and for modulation activity revealed inhibitors in tropical anemone Heteractis crispa venom. Several separation steps resulted isolation an inhibiting compound. This 56-residue-long polypeptide named APHC1 that has Bos taurus trypsin inhibitor (BPTI)/Kunitz-type fold, mostly represented by serine protease ion channel blockers. acted partial antagonist capsaicin-induced currents (32 ± 9% inhibition) half-maximal effective concentration (EC50) 54 4 nm. In vivo, 0.1 mg/kg dose significantly prolonged tail-flick latency reduced acute Therefore, our results can make important contribution to research into molecular mechanisms help solve problem overactivity this receptor during number pathological processes organism.