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
