In previous studies, we have systematically investigated the membrane insertion and structural effects of several natural AMPs, including LL-37, indolicidin, magainin II, aurein, and cecropin A, across a wide range of physiologically relevant peptide-to-lipid (PL) ratios . We found variations in how these peptides inserted into membranes: aurein exhibited transmembrane-like insertion, whereas LL-37's insertion was concentration dependent, integrating only into the outer leaflet at low PL ratios (1:100) and more deeply at higher PL ratios (1:50), nearing the solubilization limit. Most AMPs studied only inserted between the head and tail groups in the outer leaflet, aligning with Wimley's interfacial activity model . Indolicidin, a bovine AMP, is particularly interesting due to its unstructured nature, maintaining this lack of structure even upon membrane insertion, as shown by circular dichroism (CD) . Using SAXS and SANS, we demonstrated that even at high PL ratios up to 1:10, indolicidin remains in the interfacial region of the outer leaflet, exerting minimal structural impact on the membrane . Neutron reflectometry (NR) on supported lipid bilayers confirmed indolicidin's translocation to the inner leaflet only at very high concentrations approaching 1:1 PL ratios, resulting in detergent-like membrane solubilization . Consequently, it is unlikely that indolicidin forms ordered transmembrane pores, yet its ability to permeabilize membranes at lower concentrations is evidenced in dye leakage assays with both cell cultures and vesicles . This suggests that pore formation is not required and raises questions about the mechanism of membrane permeabilization.