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.
Biophys J
2003 May 01;845:3052-60. doi: 10.1016/S0006-3495(03)70031-9.
Show Gene links
Show Anatomy links
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.
Hallock KJ
,
Lee DK
,
Ramamoorthy A
.
???displayArticle.abstract???
In this work, we present the first characterization of the cell lysing mechanism of MSI-78, an antimicrobial peptide. MSI-78 is an amphipathic alpha-helical peptide designed by Genaera Corporation as a synthetic analog to peptides from the magainin family. (31)P-NMR of mechanically aligned samples and differential scanning calorimetry (DSC) were used to study peptide-containing lipid bilayers. DSC showed that MSI-78 increased the fluid lamellar to inverted hexagonal phase transition temperature of 1,2-dipalmitoleoyl-phosphatidylethanolamine indicating the peptide induces positive curvature strain in lipid bilayers. (31)P-NMR of lipid bilayers composed of MSI-78 and 1-palmitoyl-2-oleoyl-phosphatidylethanolamine demonstrated that the peptide inhibited the fluid lamellar to inverted hexagonal phase transition of 1-palmitoyl-2-oleoyl-phosphatidylethanolamine, supporting the DSC results, and the peptide did not induce the formation of nonlamellar phases, even at very high peptide concentrations (15 mol %). (31)P-NMR of samples containing 1-palmitoyl-2-oleoyl-phosphatidylcholine and MSI-78 revealed that MSI-78 induces significant changes in the bilayer structure, particularly at high peptide concentrations. At lower concentrations (1-5%), the peptide altered the morphology of the bilayer in a way consistent with the formation of a toroidal pore. Higher concentrations of peptide (10-15%) led to the formation of a mixture of normal hexagonal phase and lamellar phase lipids. This work shows that MSI-78 induces significant changes in lipid bilayers via positive curvature strain and presents a model consistent with both the observed spectral changes and previously published work.
Andreu,
Animal antimicrobial peptides: an overview.
1998, Pubmed
Andreu,
Animal antimicrobial peptides: an overview.
1998,
Pubmed
Bechinger,
Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy.
1993,
Pubmed
,
Xenbase
Dathe,
Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.
1999,
Pubmed
,
Xenbase
Epand,
Modulation of membrane curvature by peptides.
2000,
Pubmed
Fenske,
Phosphorus-31 two-dimensional solid-state exchange NMR. Application to model membrane and biological systems.
1991,
Pubmed
García-Olmedo,
Plant defense peptides.
1998,
Pubmed
Gasset,
Influence of cholesterol on gramicidin-induced HII phase formation in phosphatidylcholine model membranes.
1988,
Pubmed
Hallock,
An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies.
2002,
Pubmed
Keller,
Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures.
1996,
Pubmed
Killian,
Importance of hydration for gramicidin-induced hexagonal HII phase formation in dioleoylphosphatidylcholine model membranes.
1985,
Pubmed
Liu,
A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane alpha-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes.
2001,
Pubmed
Maloy,
Structure-activity studies on magainins and other host defense peptides.
1995,
Pubmed
Matsuzaki,
Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria.
1997,
Pubmed
,
Xenbase
Matsuzaki,
Relationship of membrane curvature to the formation of pores by magainin 2.
1998,
Pubmed
,
Xenbase
Matsuzaki,
Magainins as paradigm for the mode of action of pore forming polypeptides.
1998,
Pubmed
,
Xenbase
Moll,
Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D.
1990,
Pubmed
Oren,
Mode of action of linear amphipathic alpha-helical antimicrobial peptides.
1998,
Pubmed
Siegel,
The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion.
1999,
Pubmed
Thayer,
Phosphorus-31 nuclear magnetic resonance spectra characteristic of hexagonal and isotropic phospholipid phases generated from phosphatidylethanolamine in the bilayer phase.
1981,
Pubmed
Vogel,
Thermal unbinding of highly oriented phospholipid membranes.
2000,
Pubmed
Wieprecht,
Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure.
1999,
Pubmed
,
Xenbase
Wieprecht,
Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides.
1997,
Pubmed
Wieprecht,
Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects.
2000,
Pubmed
,
Xenbase
Zasloff,
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
1987,
Pubmed
,
Xenbase
