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.
Original language | English |
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Pages (from-to) | 1199-1203 |
Number of pages | 5 |
Journal | Bulletin of the Korean Chemical Society |
Volume | 37 |
Issue number | 8 |
DOIs | |
State | Published - 1 Aug 2016 |
Keywords
- Amphipathic helices
- Antimicrobial peptides
- Hemolytic activity
- Stapled peptides
- α-helix