The interactions of amphipathic alpha-helical peptides with lipid bila
yers provide a model of the interactions of membrane proteins with the
ir environment, as well as insights into the modes of action of biolog
ically important peptides. Recent results have shown that antimicrobia
l peptides, such as magainin, may act by stabilising the formation of
toroidal pores within lipid bilayers, In contrast, the influenza fusio
n peptide promotes nonbilayer lipid phases. Complex pore-forming bacte
rial toxins, such as colicins, unfold at the bilayer surface, yielding
a dynamic structure containing both bilayer-inserted and bilayer-surf
ace helices, Recent improvements in methods for computer simulations h
ave enabled them to play an important role in helping elucidate the na
ture of peptide-bilayer interactions.