Antimicrobial peptides (AMPs) are recognized as promising safe alternatives to antibiotics for its low drug-resistance. Brevilaterin B, a newly discovered antimicrobial lipopeptide produced by Brevibacillus laterosporus S62-9, exhibits efficient antibacterial activity on Listeria monocytogenes with a minimum inhibitory concentration of 1μgmL-1. The present research aimed to investigate the antibacterial mechanism of brevilaterin B against Listeria monocytogenes. Brevilaterin B caused membrane depolarization and the breakup of the cytomembrane as measured by 3,3-dipropylthiadicarbocyanine iodide and transmission electron microscopy, respectively. Using 1,2-dipalmitoyl-sn-glycero-3-phosphocholine and 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (7:3) as a model membrane, results proved that brevilaterin B could bind to liposomes, integrate into the lipid bilayer, and consequently increase the permeability of liposomes to calcein. The secondary structure of brevilaterin B also changed from an unstructured coil to a mainly β-sheet conformation as measured by circular dichroism. Brevilaterin B exhibits antibacterial activity by a membrane interaction mechanism, which provides a theoretical basis for using brevilaterin B as a promising natural and effective antimicrobial agent against pathogenic bacteria. KEY POINTS: • Brevilaterin B exhibited antibacterial activity against Listeria monocytogenes. • Brevilaterin B exhibited membrane interaction mechanism. • Brevilaterin B showed conformational change when interacted with liposome.
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