There appear to have been multiple evolutionary recruitments of defensins to be toxin proteins used in the venoms of animals. and act via a completely different mechanism to their antimicrobial relatives, from binding directly to ion channels to disrupting nerve signals. Examples include the crotamine toxin in snake venom, many scorpion toxins, some sea anemone toxins, and one of the toxins in platypus venom. Indeed, an insect defensin has been experimentally converted into a toxin by deletion of a small loop that otherwise sterically hindered interactions with the ion channels.