For detergent-like peptides such as -lysin, Pokorny et al. demonstrated that cholesterol-rich raft domains resist peptide activity, while liquid-disordered POPC-rich domains are vulnerable to attack . Paradoxically, cholesterol abundance can enhance hemolytic activity by creating smaller, disordered domains where peptides preferentially aggregate . Cholesterol is capable of inducing some degree of resistance against membrane-active AMPs but becomes less effective in laterally heterogeneous membranes . Liquid-disordered domains are especially susceptible to . The literature consistently shows that toroidal pore-forming ↵-helical peptides are hindered by cholesterol-induced acyl chain ordering and lipid compression. In contrast, cholesterol's role in detergent-like peptide activity appears more variable, depending on its local concentration and the degree of lateral heterogeneity.