Understanding how cholesterol influences peptide insertion, using experimental and computational techniques, reveals critical mechanisms behind AMP selectivity. Pardaxin, a peptide with strong bacteriolytic but weak hemolytic activity, using solid-state NMR . Pardaxin's helix-hinge-helix structure enables membrane destabilization and possibly formation of a toroidal pore . However, cholesterol-rich domains resist Pardaxin insertion by increasing acyl chain order and membrane thickness [332], limiting the hydrophobic matching required for pore formation . Cholesterol also inhibits the membrane curvature necessary for pore formation . In the coarse-grained Martini simulations performed by , a DPPC/DLiPC/Cholesterol membrane was used as a model for a strongly phase-separating membrane, along with the four peptides Magainin 2, BP100, MSI-78, and MSI-103. The study observed a depletion of all peptides from the liquid-ordered phase (comprised of DPPC and cholesterol). This phenomenon was attributed to the more favorable lipid-lipid interactions in the liquid-ordered phase in the absence of peptides that compensate for the entropically unfavorable sorting of the peptides. Interestingly, the simulation also revealed that the peptide Magainin 2 formed toroidal pores only in the liquid-disordered region of the membrane.