In the article we present today we are going to address the topic of Charybdotoxin, a topic that has aroused the interest of many people throughout history. Charybdotoxin is a complex and fascinating topic that covers a wide range of aspects and has repercussions in various areas of society. Over the years, Charybdotoxin has been the subject of numerous studies, debates and controversies, which has contributed to enriching our understanding of this topic. In this article, we propose to explore different facets related to Charybdotoxin, from its origin to its impact today, offering a comprehensive vision and diverse perspectives that allow the reader to delve into this exciting topic.
Charybdotoxin | |||||||
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Identifiers | |||||||
Organism | |||||||
Symbol | ChTX | ||||||
Alt. symbols | ChTX-Lq1, ChTx-a | ||||||
CAS number | 95751-30-7 | ||||||
PDB | 2crd More structures | ||||||
UniProt | P13487 | ||||||
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Charybdotoxin (ChTX) is a 37 amino acid neurotoxin from the venom of the scorpion Leiurus quinquestriatus hebraeus (deathstalker) that blocks calcium-activated potassium channels. This blockade causes hyperexcitability of the nervous system. It is a close homologue of agitoxin and both toxins come from Leiurus quinquestriatus hebraeus. It is named after Charybdis, a sea monster from Greek myth.
The Charybdotoxin family of scorpion toxins is a group of small peptides that has many family members, such as the pandinotoxin, derived from the venom of scorpion Pandinus imperator.
Scorpions such as the deathstalker paralyze their prey by injecting a potent mix of peptide toxins. Charybdotoxin, a 37 amino acid, 4 kDa neurotoxin with the molecular formula C176H277N57O55S7, is one of the peptide toxins that can be extracted from the venom of the scorpion. Its structure is very similar to that of margatoxin. Charybdotoxin contains three disulfide bridges.
Charybdotoxin occludes the pore of calcium-activated voltage-gated shaker K+ channels by binding to one of four independent, overlapping binding sites. It binds both to the open and the closed states. In addition, the block is enhanced as the ionic strength is lowered. This block occurs as the Asn 30 on the CTX interacts with the Asp 381 on the K+ channel. The blockade of K+ channels by the charybdotoxin peptide causes neuronal hyperexcitability. Mutations of the Lys31Gln and the Asn30Gln had the effect of lessening the CTX block of the pore on the shaker channel.
Anti-scorpion venom serum (AScVS) is an effective and safe method of therapy in severe scorpion envenoming syndrome. Compared with other therapies like alpha blockers it has a relatively short recovery period (10 vs 16–42 hours).