Melittin-induced changes in lipid multilayers. A solid-state NMR study.
Solid-state 1H, 13C, 14N, and 31P NMR spectroscopy was used to study the effects of the bee venom peptide, melittin, on aligned multilayers of dimyristoyl-, dilauryl- and ditetradecyl-phosphatidylcholines above the gel to liquid-crystalline transition temperature, Tc. Both 31P spectra from the lipid headgroups and 1H resonances from the lipid acyl chain methylene groups indicate that the peptide does not affect the mosaic spread of the lipid molecules at lipid:peptide molar ratios of 10:1, or higher. None of the samples prepared above Tc showed any evidence of the formation of hexagonal or isotropic phases. Melittin-induced changes in the chemical shift anisotropy of the headgroup phosphate and the lipid carbonyl groups, and in the choline 14N quadrupole splittings, show that the peptide has effects on the headgroup order and on the molecular organization in the sections of the acyl chains nearest to the bilayer surface. The spin-lattice relaxation time for the lipid acyl chain methylene protons was found to increase and the rotating-frame longitudinal relaxation time to markedly decrease with the addition of melittin, suggesting that motions on the nanosecond time scale are restricted, whereas the slower, collective motions are enhanced in the presence of the peptide.
Smith
R
R
Biochemistry Department, University of Queensland, Australia.
Separovic
F
F
Bennett
F C
FC
Cornell
B A
BA
D000595:Amino Acid Sequence; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D005782:Gels; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008555:Melitten; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010713:Phosphatidylcholines / Q000737:chemistry*; D013329:Structure-Activity Relationship
D005782:Gels; D010713:Phosphatidylcholines; C015153:1,2-dilauroylphosphatidylcholine; D008555:Melitten; D004134:Dimyristoylphosphatidylcholine