The toxin is an amphipathic peptide consisting of a large hydrophobic patch which is surrounded by a ring of six polar lysine residues.

The toxin contains three intramolecular disulfide bonds that contribute to the formation of its inhibitor cystine knot (ICK).

It can insert itself into the membrane by binding to anionic and cationic groups based on hydrophobic and electrostatic interactions.

[6] GsMTx-4 mainly targets mechanosensitive channels from the Piezo[8] and TRP[9] families, such as Piezo1[8] and TRPC6[9] which are generally bilayer tension-sensitive.

[6][12] Rather than directly binding to the gating structures like other ICK peptides do,[4] GsMTx4 makes the mechanosensitive channels less sensitive to mechanical tension of the bilayer membrane.

GsMTx-4 might play a role in the treatment of volume-activated arrhythmias or muscular dystrophy; it potentially has good therapeutic properties because it is well tolerated following injection in mice, it is non-immunogenic, biologically stable, does not directly interact with MSCs, and has a long pharmacokinetic lifetime.