Every cell is protected by a semipermeable membrane. Peptides with the right properties, for example Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore-forming antibacterial peptides or toxins.

• Klíčová slova
• antibiotics, fluorescent probes, membrane structure, membrane transport, molecular biophysics, none, structural biology,
• MeSH
• biologické modely MeSH
• buněčná membrána chemie   metabolismus   MeSH
• hydrofobní a hydrofilní interakce MeSH
• kationické antimikrobiální peptidy chemie   metabolismus   MeSH
• konformace proteinů * MeSH
• metoda Monte Carlo MeSH
• molekulární modely MeSH
• poriny chemie   metabolismus   MeSH
• vztahy mezi strukturou a aktivitou MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• kationické antimikrobiální peptidy MeSH
• poriny MeSH