Gympietides
Family of pain-causing neurotoxins
From Wikipedia, the free encyclopedia
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]
Name
They get their name after the species of plant Dendrocnide moroides, commonly known as gympie-gympie.[4]
Structure
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
LPRCDSPFCSLFRMGLCGDKCICVPLPIFGICVPNV
Medicine
They could have potential therapeutic use in pain relief by providing a scaffold.[3][clarification needed]