This highlights how the mechanism of action responsible for the bactericidal activity may be very different from the one that causes toxicity in mammalian cells. The cytotoxic effect of BMAP27 was related to its hydrophobic C-terminal domain, consistent with other studies showing how hydrophobicity and aggregation may promote promiscuous membrane activity . This region promotes membrane insertion, in a manner reminiscent of the membrane-penetrating properties of the bee venom toxin Melittin (Figure ). These findings underscore how membrane composition influences the mechanism of action of AMPs and highlights the importance of designing AMPs with selective activity to minimize toxicity toward mammalian cells.