Despite limited direct experimental evidence, the formation of structural transmembrane pores, which we may refer to as "structural pores", is a commonly suggested explanation for the permeabilization observed in many natural AMPs. These are typically proposed as "barrel stave" or "toroidal" pores. The "barrel stave" model suggests that peptide monomers insert transversely into the bilayer and assemble like barrel staves to form a defined pore. The "toroidal" model involves cooperative transmembrane peptide interactions that induce highly curved lipid pores. In a comprehensive review by Huang and Charron, the development of these early mechanistic models and structural pores is presented in greater detail . However, in a critical review from 2010, Wimley highlighted limitations in these ordered structures and noted the lack of convincing experimental support . One compelling argument is that dye release is typically gradual, incomplete and requires moderate peptide-to-lipid ratios for most AMPs. This differs from that of peptides like alamethicin and melittin, which are more accurately classified as toxins due to their lack of selectivity towards bacterial membranes . Unlike AMPs, these pore-forming toxins cause complete membrane permeabilization at much lower concentrations . Wimley also demonstrated that, if true structural pores were formed, rapid release would occur on a sub-second timescale, contrasting with the slower, partial release observed experimentally over approximately 100 seconds. As an alternative, Wimley proposed the "interfacial activity" model, where AMPs insert parallel to the bilayer plane, disrupting lipid packing without forming structural pores or solubilizing the membrane . However, this model similarly does not provide a concrete mechanistic model of permeabilization. Furthermore, while there had been some evidence for this interfacial insertion of AMPs and other peptides , at the time dedicated structural studies of the insertion of AMPs into the membrane were still limited.