CEITEC – Central European Institute of Technology, Masaryk University, Kamenice, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice, Czech Republic
Ivo Kabelka
CEITEC – Central European Institute of Technology, Masaryk University, Kamenice, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice, Czech Republic
Tereza Králová
CEITEC – Central European Institute of Technology, Masaryk University, Kamenice, Czech Republic
Lukáš Sukeník
CEITEC – Central European Institute of Technology, Masaryk University, Kamenice, Czech Republic; Department of Condensed Matter Physics, Faculty of Science, Masaryk University, Kotlářská, Czech Republic
Šárka Pokorná
J. Heyrovsky Institute of Physical Chemistry, Czech Academy of Sciences, Prague, Czech Republic
CEITEC – Central European Institute of Technology, Masaryk University, Kamenice, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice, Czech Republic; Department of Condensed Matter Physics, Faculty of Science, Masaryk University, Kotlářská, Czech Republic
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.