Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy.
PGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be helical between residues 6 and 21 when associated with detergent micelles by multidimensional solution nuclear magnetic resonance (NMR) spectroscopy. Solid-state NMR experiments on specifically 15N-labeled peptides in oriented phospholipid bilayer samples show that the helix axis is parallel to the plane of the bilayers. 15N solid-state NMR powder pattern line shapes obtained on unoriented samples demonstrate that the amino-terminal residues are highly mobile and that the fluctuations of backbone sites decrease from Ala6 toward the carboxy terminus. The powder pattern observed for 15N-labeled Ala20 is essentially that expected for a rigid site. These findings are similar to those for the 23-residue magainin2 peptide in membrane environments.
Bechinger
B
B
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
Zasloff
M
M
Opella
S J
SJ
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers / Q000737:chemistry*; D008823:Micelles; D008969:Molecular Sequence Data; D009584:Nitrogen; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D010714:Phosphatidylethanolamines / Q000737:chemistry; D010715:Phosphatidylglycerols / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D008823:Micelles; D010455:Peptides; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D012996:Solutions; C057561:1-palmitoyl-2-oleoylphosphatidylethanolamine; C045866:peptide-Gly-Leu-amide; C060037:1-palmitoyl-2-oleoylglycero-3-phosphoglycerol; D009584:Nitrogen