Antimicrobial peptides (AMPs) can kill pathogens via the formation of permeable membrane pores. However, matching peptide properties with their ability to form pores remains elusive. In particular, the proline/glycine kink in helical AMPs was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence leakage experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The precise position of the proline/glycine kink in the sequence further controls the formation of specific toroidal pore structure: U- or hourglass-shaped. Moreover, we demonstrate that two helical peptides can form a stable kink-like connection with similar behavior as one long helical peptide with kink. The provided molecular-level insight can be utilized for rational design or modification of antibacterial peptides or toxins to alter their ability to form membrane pores.