title: Spontaneous polymerization of the antibiotic peptide magainin 2.
abstract: We describe here the ability of the magainin 2 peptide to assemble spontaneously into characteristic 13-nm diameter filaments having a 30 nm periodic helical substructure. Optimal conditions for extensive polymerization into filaments of several hundred microns required low pH and high ionic strength. Polymerization of the magainin 2 peptide may be involved in its recently described in vitro membrane-disrupting and antibiotic activities.
authors.affiliation: Laboratory of Neuro-otolaryngology, NIDCD, Bethesda, MD 20892.
authors.forename: R
authors.initials: R
authors.lastname: Urrutia
authors.forename: R A
authors.initials: RA
authors.lastname: Cruciani
authors.forename: J L
authors.initials: JL
authors.lastname: Barker
authors.forename: B
authors.initials: B
authors.lastname: Kachar
mesh_terms: D000818:Animals; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D006863:Hydrogen-Ion Concentration; D054806:Magainins; D008854:Microscopy, Electron; D008859:Microscopy, Polarization; D009994:Osmolar Concentration; D010455:Peptides; D011108:Polymers; D029867:Xenopus Proteins; D014982:Xenopus laevis
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D010455:Peptides; D011108:Polymers; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus