In situ captured antibacterial action of membrane-incising peptide lamellae

The study uses electron microscopy to study the formation of supramolecular structures of lysine-rich heterochiral β3-peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. The phosphate-induced conformational change on these lamellins leads to the formation of striped lamellae, which can incise the cell envelope of Gram-negative bacteria, providing a mechanistic link for membrane-targeting agents.