In the present work, we have addressed this by utilizing the recent advances in synchrotron X-ray scattering to combine structural characterization of the peptide-membrane interactions with simultaneous characterization of the flux of monoatomic ions through the lipid membrane. Static SAXS of equilibrated samples revealed that while peptide-free vesicles are significantly deformed by the osmotic pressure resulting from increase in the external NaCl concentration, prior incubation with AMPs facilitate equilibration of the external and internal salt concentrations. This negates the osmotic pressure and prevents deformation even at very high initial salt gradients. Concurrent with the salt equilibration, these results revealed that the peptides indolicidin and LL-37 inserted only peripherally with minimal structural changes to the membrane and without any observable solubilization, which is in excellent agreement with numerous previous studies . Crucially, the peptide partitioning into the membrane also did not change with increasing salt-gradients. TR-SAXS allowed us to track the salt equilibration in real time, with millisecond temporal-resolution.