It acts as a cell-penetrating peptide (CPP); it binds with high affinity and specificity to skeletal ryanodine receptor 1 (RYR1) of the sarcoplasmic reticulum, thereby triggering calcium release from intracellular Ca2+ stores.

[1] On the basis of its amino acid structure, vejocalcin belongs to the family of scorpion calcin toxins, a group of selective, high-affinity membrane-permeable ligands of RyRs.

However, comparisons among different calcins show that, for each peptide, there appears to be no correlation between DM, binding affinity and subconductance state attributes.

[1][5] Like most calcins, vejocalcin shows a fast association rate, as well as a reversible effect, due to free dissociation from the binding site.

[1] Mechanistically, vejocalcin is thought to promote this action by increasing the “openness” of the channel in a long-lasting, reversible and transient manner.

High concentrations of vejocalcin drive incomplete, submaximal depletion of Ca2+ load through the process of calcium-induced calcium release (CICR) from intracellular Ca2+ stores.

[1] While the effects of vejocalcin have not yet been studied, in vivo toxicity testing of hemicalcin has shown that the peptide induces neurotoxic symptoms in mice, followed by death.