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Significance Antibiotic resistance among clinically relevant bacteria presents an increasing threat and raises the urgent need for new compounds. Antimicrobial peptides and peptide antibiotics are potent membrane-active molecules and valuable prototypes for drug development. In gram-negative infections, killing of bacteria by antimicrobials is accompanied by the release of lipopolysaccharide (LPS), an endotoxin that causes severe hyperinflammation and pathology. We demonstrate how two medically relevant peptides, the cathelicidin LL-32 and polymyxin B, disarm endotoxins by peptide–LPS interaction. Furthermore, our studies reveal a mechanism of peptide-mediated immune control by acting on signaling domains of the immune cell membrane. Our results significantly enhance our understanding of how peptide antibiotics can regulate inflammation and will be important for their development and therapeutic use.

Cathelicidin and PMB neutralize endotoxins by multifactorial mechanisms including LPS interaction and targeting of host cell membranes