Scyllatoxin

Sources

Scyllatoxin is one of the components of the venom of the Israeli scorpion ‘Leiurus quinquestriatus hebraeus’. It consists of only 0.02% of the total protein in crude venom.

Chemistry

Leiurotoxin I is a 31-residue peptide (sequence AFCNLRMCQLSCRSLGLLGKCIGDKCECVKH-NH2), with a helix and a short antiparallel β-sheet. This toxin is stabilized by disulfide bonds: Cys8-Cys26 and Cys12-Cys28 is bound to the β-sheet, while Cys3-Cys21 is bound to an N-terminal segment preceding the helix. Leiurotoxin adopts the ά/β motif. Especially the positively charged residues (Arg6 and Arg13, which are located in the ά helix) are important for the expression of toxin biological activities and for its receptor affinity.

Target

Scyllatoxin is a blocker of small-conductance Ca2+– activated K+ channels at 10−13–10−11 M concentrations in various cell types. This toxin shows similarity in its physiological activity and binding specificity to apamin, but both toxins show no structural similarity.

Mode of action

Scyllatoxin blocks the slow after-hyperpolarization that follows an action potential in some nerve cells.

Toxicity

Scyllatoxin induces spontaneous contractions in guinea pig taenia coli muscle cells that have been relaxed with epinephrine.

References

References

1. (September 2002). "Role of disulfide bonds in folding and activity of leiurotoxin I: just two disulfides suffice". Biochemistry.
2. (August 1996). "Synthesis and characterization of leiurotoxin I analogs lacking one disulfide bridge: evidence that disulfide pairing 3-21 is not required for full toxin activity". Biochemistry.
3. (June 1997). "Characterization of a new family of toxin-like peptides from the venom of the scorpion ''Leiurus quinquestriatus hebraeus''. 1H-NMR structure of leiuropeptide II". The Journal of Peptide Research.
4. (July 1988). "Purification and characterization of a unique, potent inhibitor of apamin binding from ''Leiurus quinquestriatus hebraeus'' venom". J. Biol. Chem..
5. (January 1992). "Scyllatoxin, a blocker of Ca²⁺-activated K⁺ channels: structure-function relationships and brain localization of the binding sites". Biochemistry.