Abstract
The cyclic β-sheet antimicrobial peptide tachyplesin I (T-SS) was found to show 280-fold higher affinity for lipopolysaccharides (LPS) compared with acidic phospholipids, whereas the linear α-helical peptide F5W-magainin 2 (MG2) could not discriminate between LPS and acidic phospholipids. The recognition site was the lipid A moiety and the cyclic structure was crucial to this specific binding. The cyclic structure also endowed the peptide with very rapid outer membrane (OM) permeabilization.
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