Abstract
To improve the antimicrobial activity of the hydrocarbon‐stapled amphipathic heptapeptide helix identified from our previous study, we prepared a series of its dimeric analogs using several different linkers. All of these dimers showed a significant increase in antimicrobial activity although their hemolytic activity was also largely increased. One particular analog bearing a proline linker displayed notably low hemolytic activity compared to others, indicating that the conformational characteristics of the linker play a key role in disassociating undesirable hemolytic activity from antimicrobial activity in this series of antimicrobial peptides. We believe that this analog can serve as a stepping stone for further development of novel antimicrobial agents to combat antibiotic‐resistance.
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