While the investigated AMPs clearly facilitate ion-transport through the DMPC/PG membranes, with dimyristoyl (DM) (saturated, 14-C) tails, it would appear that the AMP induced permeabilization is dependent on the bilayer thickness. This dependency is clearly seen when we compare the results of DM membranes, particularly those presented in figure , to the TR-SAXS data of DSPC/PG and POPC/PG membranes presented in figures 6A and 6B respectively. While there is again a clear and time-dependent deformation observed for the DSPC/PG membrane in the absence of peptide, it is not as dramatic as for the thinner membranes. This is expected, as the membrane is in this case comprised of lipids with distearoyl (saturated, 18-C) tails, and is much stiffer. What is more surprising is that this deformation is unaffected by peptide addition, as can be seen in figure . Model analysis of the vesicles in Tris, with and without peptide (shown in the inset of figure ), reveal that the peptide inserts in the outer leaflet as before. Despite the peptides inserting, it appears that they are not able to permeabilize the membrane, at least not quickly enough to alleviate the osmotic pressure and prevent deformation. This is interesting, considering that only the length of the lipid tails are different compared to the previous LUVs. The lipid head groups and their proportion to each other, and hence the membrane charge, remain the same as before.