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androctonin

Androctonin is an antimicrobial peptide of 25 amino acids (RSVCRQIKICRRRGGCYYKCTNRPY) isolated from the hemolymph of unchallenged scorpions of the species Androctonus australis. Androctonin contains two disulfide bridges. It shows marked sequence homology to tachyplesins and polyphemusins from horseshoe crabs and gomesin from spiders. The peptide is non-hemolytic and is active against Gram-positive bacteria and Gram-negative bacteria and fungi (Ehret-Sabatier et al, 1996). The peptide acts by altering membrane permeability (Hetru et al, 2000).

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