Influence of the arrangement and secondary structure of melittin peptides on the formation and stability of toroidal pores

► Simulated symmetrically and asymmetrically arranged melittins in a POPC bilayer pore. ► For the first time observed creation of the fully toroidal pore in symmetric arrangement. ► Observed that helicity is not a prerequisite for the toroidal pore creation. ► Investigated the role of melittin charge distribution promoting toroidal pore creation. ► Proposed that the symmetrical arrangement of melittin peptides is more favorable for the toroidal pore creation.