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The interactions of amphipathic α-helical peptides with lipid bilayers provide a model of the interactions of membrane proteins with their environment, as well as insights into the modes of action of biologically important peptides. Recent results have shown that antimicrobial peptides, such as magainin, may act by stabilising the formation of toroidal pores within lipid bilayers. In contrast, the influenza fusion peptide promotes nonbilayer lipid phases. Complex pore-forming bacterial toxins, such as colicins, unfold at the bilayer surface, yielding a dynamic structure containing both bilayer-inserted and bilayer-surface helices. Recent improvements in methods for computer simulations have enabled them to play an important role in helping elucidate the nature of peptide-bilayer interactions.

Original publication




Journal article


Current Opinion in Colloid and Interface Science

Publication Date





518 - 524