Charybdotoxin

Charybdotoxin (ChTX), a 37 amino acid neurotoxin derived from the venom of the scorpion Leiurus quinquestriatus hebraeus (deathstalker), blocks calcium-activated potassium channels.

The neurological system becomes hyperexcited as a result of this blockage. Agitoxin and toxins are a close homologue originated from Leiurus quinquestriatus hebraeus, which was named after the sea monster Charybdis in Greek mythology. The ChTX family of scorpion toxins consists of a large number of small peptides that has many family members such as pandinotoxin. It contains three disulfide bridges and its structure is very similar to margatoxin. ChTX binds to one of four independent, overlapping binding sites to occludes the pore of voltage-gated shaker K⁺ channels that are triggered by calcium. Both the open and the closed states were binded to it. Furthermore, when the ionic strength decreases, the block improves. As the Asn³⁰ on the ChTX interacts with the Asp³⁸¹ on the K⁺ channel, this block happens. Neuronal hyperexcitability is brought on by the ChTX peptide’s blocking of K⁺ channels.