LL-37, the active form of the cathelicidin antimicrobial peptide (CAMP), is derived from the proteolytic cleavage of the inactive precursor CAP-18 . LL-37 adopts an amphipathic ↵-helical structure , and at neutral pH, it spontaneously forms oligomers in solution . To understand how LL-37 interacts with bacterial membranes, Zhao et al. employed the GROMOS united-atom force field to model the interactions of LL-37 monomers with simplified, homogeneous membranes composed of POPG (representing bacterial membranes) and POPC (representing mammalian membranes). Their findings demonstrated that LL-37 interacts with both types of membranes, but the interaction with POPC was much weaker, and resulted in partial helix unfolding .