Maurotoxin
Maurotoxin (abbreviated MTX) is a peptide toxin from the venom of the Tunisian chactoid scorpion Scorpio maurus palmatus, from which it was first isolated and from which the chemical gets its name. It acts by blocking several types of voltage-gated potassium channel.
Chemistry
Maurotoxin is a peptide of 34 amino acids cross-linked by four disulfide bridges, with an atypical pattern of organization compared with other scorpion toxins; this unusual pairing of cysteine residues may be mediated by the presence of adjacent prolines. The peptide contains an alpha helix linked by two disulfide bridges to a two-stranded antiparallel beta sheet.
Target
Scorpion toxins constitute the largest group of potassium (K+) channel blockers and are useful pharmacological probes to investigate ion channels and their functions.
Maurotoxin (MTX) blocks various K+ -channels:
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