Anthopleurin can bind to the extracellular site of voltage-gated sodium channels.

The voltage-gated sodium channels cause persistent sodium current into the cell, which generates the action potential.

In order for excitability and conduction to occur, voltage-gated sodium channels must be activated.

It affects voltage-gated sodium ion channels leading to an increased duration of its opening.

It affects the gating of voltage-gated sodium channels and calcium channels.

Like other α-scorpion toxins kurtoxin was also found to interact with voltage-gated sodium channels.

This depolarization opens some voltage-gated sodium channels, but not enough to generate an action potential.

Tetrodotoxin binds to what is known as site 1 of the fast voltage-gated sodium channel.

The mechanism of toxicity is through the blockage of fast voltage-gated sodium channels.

It acts on the voltage-gated sodium channels of nerve cells, preventing normal cellular function and leading to paralysis.