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Designing new antimicrobial peptides (AMPs) focuses heavily on the activity of the peptide and less on the elements that stabilize the secondary structure of these peptides. Studies have shown that improving the structure of naturally occurring AMPs can affect activity and so here we explore the relationship between structure and activity of two non‐naturally occurring AMPs. We have used a backbone‐cyclized...
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...
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