Antimicrobial Peptide Toroidal Pore Formation

This simulator renders a patch of lipid bilayer as two instanced leaflets of lipid headgroups and lets you drive antimicrobial-peptide membrane disruption through its real physical mechanism: the toroidal pore. Raise the peptide-to-lipid ratio and enough amphipathic peptides insert to reorganize the surrounding lipids into a continuous curved rim connecting the outer and inner leaflets, rather than the flat wall of a simple channel. The pore radius evolves under a genuine line-tension-vs-peptide-tension energy balance with thermal noise, so pore nucleation is a stochastic barrier-crossing event — small fluctuations reseal, but once peptide coverage lowers the critical radius far enough, a fluctuation runs away into full membrane rupture, exactly as in real dye-leakage and patch-clamp assays of peptides like magainin and LL-37.