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Hairpin structure stability plays a role in the activity of two antimicrobial peptides

Many naturally occurring antimicrobial peptides (AMPs) are amphipathic with a β‐hairpin conformation stabilized by cross‐strand disulfides across the associated β‐strands. Here, we show that the disulfides are not essential. Other structuring means such as better β‐turns and noncovalent cross‐strand interactions can, with proper design, replace the disulfides with no loss in antimicrobial activity. Our results also demonstrate that the hairpin turn region may play a role in membrane recognition for at least one member of this class, since a homodimeric turnless β‐sheet analog showed no antimicrobial activity. We also examined the effects of N‐terminal fatty acid adducts on AMPs. Surprisingly, the large hydrophobic carboxylic moieties examined completely eliminated the antimicrobial activity of previously active β‐hairpin peptides.