It prevents inactivation of voltage gated sodium channels and therefore blocks synaptic transmission in the central nervous system.

[1] Catterall et al. hypothesized that some polypeptide neurotoxins modify voltage-gated channels function via a "voltage-sensor trapping" mechanism.

[2][6] Normally, the region of the channel where neurotoxin receptor site 3 is undergoes a conformational change of an outward movement to lead to inactivation.

This combination resulted in the sodium channels activating at very negative potentials and deactivating very slowly, a phenomenon commonly seen in excitable tissues.

It is similar in structure to a transmembrane signal peptide, which implies that it will anchor at the membrane by burying the hydrophobic core within the bilayer.

[10] Specifically, the positively charged arginine and the non-polar alanine residues were both shown to be essential for poneratoxin potency.

[2] See figure, where the hydrophobic (red) and hydrophilic (blue) regions of poneratoxin and the lipid bilayer align, demonstrating that the structure is evolved to insert into the membrane, which will promote interaction with the voltage gated sodium channels.

[citation needed] Toxicity assays have found that the LT50 of poneratoxin, delivered via injections of genetically engineered viruses, to S. frugiperda larvae, was at 131 hours post-injection.