Translocation of a Channel-Forming Antimicrobial Peptide, Magainin 2, across Lipid Bilayers by Forming a Pore

• Published in: Biochemistry (Easton) Vol. 34; no. 19; pp. 6521 - 6526
• Main Authors: Matsuzaki, Katsumi, Murase, Osamu, Fujii, Nobutaka, Miyajima, Koichiro
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 16.05.1995
• Subjects: Amino Acid Sequence; Animals; Anti-Bacterial Agents - chemistry; Antimicrobial Cationic Peptides; Biological Transport; Cell Membrane Permeability; Energy Transfer; Freshwater; Ion Channels - chemistry; Lipid Bilayers - chemistry; Magainins; Membrane Proteins - chemistry; Molecular Sequence Data; Xenopus laevis; Xenopus Proteins
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00019a033

A channel-forming antimicrobial peptide, magainin 2, has been shown to translocate across phospholipid bilayers by forming a pore comprising multimeric peptides. The translocation was demonstrated by four sets of experiments by use of resonance energy transfer from tryptophan introduced into the peptide to a dansyl chromophore incorporated into the lipid membrane. The translocation was coupled to pore formation, as detected by the dye efflux from the lipid vesicles; about 30% of the total peptide molecules translocated into the inner leaflets over 10 min, while 80% of the dye molecules leaked out at a lipid to peptide ratio of 57. This novel model can explain the problems debated so far, i.e., the peptide forms an ion channel whereas the magainin helix essentially lies parallel to the membrane surface. Channel (pore) formation in the vesicles is a transient process observable mainly during the early stage of the peptide membrane interactions.