kaliseptine has been shown to reduce ion current through the k1.2 k channel during depolarization. since it has affinity for the dtx receptor domain, kaliseptine may act on the channel in a similar manner as the agonist dtx. whether kaliseptine exerts its action by hindering conformational changes of the k1.2 channel, is not certain. evidence was provided that dtx binds in close proximity to the external mouth of the channel, leading to occlusion of the pore. it is not certain whether this partial occlusion fully explains the inhibiting effect. the exact mechanism by which kaliseptine alters k1.2 function is still debated. kaliseptine is thought to act in conjunction with other neurotoxins present in the snakelocks anemone venom, altogether prolonging the action potential.