Neurotoxic peptide from Centruroides scorpion venom

Neurotoxic peptides from Centruroides scorpion venoms are a group of small, cystine-stabilized peptides (typically 66 amino acids, four disulfide bridges, molecular mass 7–8 kDa) that are among the primary toxic components causing the severe neurotoxic symptoms of scorpion stings. These peptides, such as Cv1–Cv5 isolated from Centruroides villegasi, are structurally and functionally classified as β-scorpion toxins (β-ScTx), modifying gating of voltage-gated sodium channels in mammals. By binding to and altering the behavior of Na^+ channels, they prolong action potentials and increase neuronal excitability, leading to neuromuscular, autonomic, and potentially lethal systemic effects. They are key antivenom targets, as demonstrated by studies exploring recombinant antibody fragments for neutralization. While their direct clinical application as therapeutic targets is limited to antivenom development, they remain central to the pathophysiology of scorpion envenomation.

Other names

β-scorpion toxin (β-ScTx)Centruroides neurotoxic peptideCv1–Cv5 (for individual peptides)NaScTx (sodium channel toxin)

Modifies gating properties of voltage-gated sodium channels by binding to specific sites, leading to prolonged channel opening and altered neuronal excitability