Abstract
Centipedes are among the oldest venomous arthropods that use their venom to subdue the prey. The major components of centipede venom are a variety of low-molecular-weight peptide toxins that have evolved to target voltage-gated ion channels to interfere with the central system of prey and produce pain or paralysis for efficient hunting. Peptide toxins usually contain several intramolecular disulfide bonds, which confer chemical, thermal and biological stability. In addition, centipede peptides generally have novel structures and high potency and specificity and therefore hold great promise both as diagnostic tools and in the treatment of human disease. Here, we review the centipede peptide toxins with reported effects on ion channels, including Nav, Kv, Cav and the nonselective cation channel polymodal transient receptor potential vanilloid 1 (TRPV1).
Highlights
The capsaicin receptor transient receptor potential vanilloid 1 (TRPV1) is a nonselective cation channel located in the plasma membrane of nociceptive dorsal root ganglia (DRG) neurons
Peptide toxins act on voltage‐gated ion channels
Centipede peptides can interfere with Nav, Kv, Cav and toxins act on voltage-gated ion channels
Summary
Centipedes, class Chilopoda, emerged approximately 440 million years ago [1] and are among the most ancient carnivorous terrestrial arthropods in soil ecosystems approximately. Scolopendromorpha represents the best known centipedes because they are frequently involved in Scolopendromorpha human accidents [5,6]. Represents the best known centipedes because they are frequently involved in human accidents [5,6]. Centipede venom, containing large amounts of biogenic amines, serotonin, polysaccharides, lipids, peptide toxins and proteins [8], is a highly complex and functionally diverse mixture. Centipede bites produce extremely sharp pain in humans [1,5]. The numerous symptoms further indicate that centipede venom contains highly complex mixtures of diverse peptide toxins
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