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

ABSTRACT: Many naturally occurring antimicrobial peptides (AMPs) are amphipathic with a ?-hairpin conformation stabilized by cross-strand disulfides across the associated ?-strands. Here, we show that the disulfides are not essential. Other structuring means such as better ?-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 ?-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 ?-hairpin peptides.

SUBMITTER: Sivanesam K

PROVIDER: S-EPMC5578868 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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

Sivanesam Kalkena K Kier Brandon L BL Whedon Samuel D SD Chatterjee Champak C Andersen Niels H NH

FEBS letters 20161121 24

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 ...[more]

PMID: 27859052

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