Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy.
Bechinger B, Zasloff M, Opella SJ.
???displayArticle.abstract??? Magainin 2 is a 23-residue peptide that forms an amphipathic alpha-helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One- and two-dimensional solid-state 15N NMR spectra of specifically 15N-labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is alpha-helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.
Bechinger,
Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy.
1991, Pubmed,
Xenbase
Bechinger,
Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy.
1991,
Pubmed
,
Xenbase Bechinger,
Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation.
1992,
Pubmed
,
Xenbase Bessalle,
All-D-magainin: chirality, antimicrobial activity and proteolytic resistance.
1990,
Pubmed
,
Xenbase Bevins,
Peptides from frog skin.
1990,
Pubmed
,
Xenbase Boman,
Antibacterial peptides: key components needed in immunity.
1991,
Pubmed Chen,
Synthetic magainin analogues with improved antimicrobial activity.
1988,
Pubmed
,
Xenbase Duclohier,
Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers.
1989,
Pubmed
,
Xenbase Durell,
Modeling the ion channel structure of cecropin.
1992,
Pubmed Jackson,
Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy.
1992,
Pubmed
,
Xenbase Kaiser,
Peptides with affinity for membranes.
1987,
Pubmed Lear,
Synthetic amphiphilic peptide models for protein ion channels.
1988,
Pubmed Marion,
A two-dimensional NMR study of the antimicrobial peptide magainin 2.
1988,
Pubmed
,
Xenbase Matsuzaki,
Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers.
1991,
Pubmed
,
Xenbase McDonnell,
fd coat protein structure in membrane environments.
1993,
Pubmed Milik,
Insertion of peptide chains into lipid membranes: an off-lattice Monte Carlo dynamics model.
1993,
Pubmed
,
Xenbase Mulvey,
High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein.
1989,
Pubmed Oiki,
Channel protein engineering: synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers.
1988,
Pubmed Opella,
Protein structure by solid-state NMR spectroscopy.
1987,
Pubmed Reid,
An electrophysiological and spectroscopic study of the properties and structure of biological calcium channels. Investigations of a model ion channel.
1992,
Pubmed Shon,
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
1991,
Pubmed Smith,
High-resolution solid-state NMR of proteins.
1988,
Pubmed Smith,
Solid-state NMR approaches for studying membrane protein structure.
1992,
Pubmed Urrutia,
Spontaneous polymerization of the antibiotic peptide magainin 2.
1989,
Pubmed
,
Xenbase Waugh,
Uncoupling of local field spectra in nuclear magnetic resonance: determination of atomic positions in solids.
1976,
Pubmed Westerhoff,
Magainins and the disruption of membrane-linked free-energy transduction.
1989,
Pubmed
,
Xenbase Zasloff,
Antimicrobial activity of synthetic magainin peptides and several analogues.
1988,
Pubmed
,
Xenbase
