Scorpine
Scorpine is a protein of 75 amino acids and three disulfide bridges isolated from the venom of the scorpion Pandinus imperator. The peptide shows limited structural similarities with defensins and cecropins in its terminal sequences. Scorpine has antibacterial activity and is a potent inhibitor of the ookinete and gamete stages of Plasmodium berghei development (Conde et al, 2000).
Zhu and Tytgat (2004) have identified Opiscorpine-1, Opiscorpine-2, Opiscorpine-3, Opiscorpine-4 as scorpine homologs (named opiscorpines) in the venom gland of the African scorpion Opistophthalmus carinatus.
Heteroscorpine-1
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