This complementary behavior between Magainin-2 and PGLa appears to be essential for their cooperative pore-forming activity. Structural studies, including MD simulations and NMR experiments , indicate that PGLa can form toroidal pores, but only when associated with Magainin-2. This interaction is mediated by the C-terminal segments of both peptides. The association of two almost perfectly helical peptides via the slightly flexible terminal region of Magainin-2 allows to form a dimer that mimics the behavior of helix-kink-helix peptides, known to induce toroidal pores . The cooperative pore formation highlights how synergistic interactions between different peptides can modulate their mechanisms of action.