Abstract
The “catastrophic threat” of antibiotic resistance has prompted research into biological methods of combating bacterial infection. One such pervasive strategy employs cationic antimicrobial peptides, CAMPs. These peptides use their structure to target and disrupt bacterial membranes. They specifically attach to PG (phosphatidylglycerol) and CL (cardiolipin) rich membranes, a common, anionic lipid of the outer bacterial leaflet. Most have shown broad spectrum activity, adequate potency, and minimal resistance. Considering these peptides have been active against pathogens for millions of years and have not developed any broad resistance, they are of particular interest to study. We have characterized the 3D structure, activity, and behavior of NA-CATH, a 34 amino acid CAMP from the Naja Atra snake. NMR studies reveal a single straight amphipathic α-helix with a disordered tail. Using one and two phase liposomes, we have found that lipid composition and the presence of phase separation affect the activity and behavior of NA-CATH. Fluorescence leakage and requenching assays indicate that the presence of phase separation increases leakage activity and the anionic lipid locale affects the leakage mechanism.
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