New eLife: Effect of helical kink in antimicrobial peptides on membrane pore formation
We used computer simulations and fluorescence experiments to show that a kink in amphipathic helices affects the formation of leaky transmembrane 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 which in turns controlls its size and effectivness in leakage. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. TWe expect that the provided molecular-level insight will be utilized for design and modification of pore-forming antibacterial peptides or toxins.
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