Gympietides are a peptide family of neurotoxins that target pain receptors and permanently change and inactivate voltage-gated sodium channels in sensory neurons to produce long-lasting pain. The highly stable nature of these peptides means that they can repeatedly stimulate these sensory neurons, prolonging the pain. [1] Their 3D molecular structure makes Gympietides similar to spider or cone snail toxins. [2] [3]
The species Dendrocnide moroides produces gympietides. These toxins give D. moroides its notoriously painful toxic stings, which can last for a few hours. [4] Dendrocnide excelsa also produces gympietides. [2]
They get their name after the species of plant Dendrocnide moroides , commonly known as gympie-gympie. [4]
All known gympietides have a very similar primary structure. The tertiary structure of Excelsatoxin A was determined via NMR spectroscopy, showing a cystine-knot structure. The other members of the family are predicted to have very similar 3D structures. [2]
>sp|P0DQP4|NTXA_DENMD Moroidotoxin A IPRCDSPLCSLFRIGLCGDKCFCVPLPIVGICVPSV>sp|P0DQP3|NTXA_DENEC Excelsatoxin A LPRCDSPFCSLFRIGLCGDKCTCVPLPIFGLCVPDV>tr|A0A7G9XV74|A0A7G9XV74_DENEC Excelsatoxin B LPRCDSPFCSLFRMGLCGDKCICVPLPIFGICVPNVThey could have potential therapeutic use in pain relief by providing a scaffold. [3] [ clarification needed ]
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