Given the importance of maintaining chemical and electrical segregation, it is not surprising that the main suggested mechanism of antimicrobial peptides (AMPs) involves the permeabilization of the membrane to ions and larger solutes . AMPs are a class of surface-active peptides with potent and broad scope activity. Both natural and, eventually, de novo designed AMPs display a large degree of variation in terms of size and secondary structure, and widely share only two features: they are amphiphilic and cationic. Abundant in both hydrophobic and basic residues, these molecules have a natural propensity to interact with the cellular membrane. Moreover, their selectivity in preferentially targeting negatively charged bacterial membranes over zwitterionic mammalian membranes is often attributed to their cationic charge. This selectivity is reflected in the fact that natural AMPs are often referred to as host defense peptides, as they were originally discovered as part of the innate immune system in a wide variety of organisms, including humans. This intriguing combination of broad-spectrum activity, inherent selectivity, and limited susceptibility to resistance has made AMPs the focal point of extensive research efforts. The ultimate goal of which is to develop AMP-based antibiotics capable of countering the rapidly escalating threat of antimicrobial resistance, predicted to become a leading cause of mortality in the near future . Despite extensive research, AMPs have scarcely entered clinical use, with only a few exceptions like Colistin . This can mainly be attributed to the susceptibility of AMPs to serum proteases, and to their cytotoxicity at elevated concentrations. However, efforts to address these limitations are likely hampered by the persistent limited understanding and lack of consensus regarding the molecular modes of action of AMPs.