The study used an electric‑based test to see how the human antimicrobial peptide LL‑37 sticks to different membrane‑like fats. It barely affects a common cell‑membrane fat (DOPC), slightly affects a negatively‑charged fat (DOPG) and a bacterial component (lipid A), and strongly affects a pure lipid A layer, confirming LL‑37’s ability to disrupt bacterial membranes.

LL-37 is an alpha-helical antimicrobial peptide of human origin. It is a 37 residue cathelicidin peptide. This paper explores the use of electrochemical methods to investigate the interaction of LL-37 with phospholipid and lipid A monolayers on a mercury drop electrode. Experiments were carried out in Dulbecco's phosphate buffered saline at pH approximately 7.6. The capacity-potential curves of the coated electrode in the presence and absence of LL-37 were measured using out-of-phase ac voltammetry. The frequency dependence of the complex impedance of the coated electrode in the presence and absence of LL-37 was estimated at -0.4 V versus Ag/AgCl 3.5 mol dm(-3) KCl. The monolayer permeability to ions was studied by following the reduction of Tl(I) to Tl(Hg) at the coated electrode. LL-37 shows no significant interaction with DOPC. However, LL-37 shows a small interaction with DOPG and lipid A within a DOPC monolayer where the monolayer permeability is marginally increased and the zero frequency capacitance (ZFC) is marginally decreased in both cases. LL-37 shows a significant interaction with a lipid A monolayer thereby decreasing the ZFC by 30%. The results concur with the known membrane active properties of LL-37 and establish this electrochemical approach as a key technique for screening peptides.