Melittin-induced changes in lipid multilayers. A solid-state NMR study

Smith R., Separovic F., Bennett F.C. and Cornell B.A. (1992) Melittin-induced changes in lipid multilayers. A solid-state NMR study. Biophysical Journal, 63 2: 469-474. doi:10.1016/S0006-3495(92)81623-5

Author Smith R.
Separovic F.
Bennett F.C.
Cornell B.A.
Title Melittin-induced changes in lipid multilayers. A solid-state NMR study
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
Publication date 1992-01-01
Sub-type Article (original research)
DOI 10.1016/S0006-3495(92)81623-5
Open Access Status Not yet assessed
Volume 63
Issue 2
Start page 469
End page 474
Total pages 6
Language eng
Subject 1304 Biophysics
Abstract 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
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Citation counts: TR Web of Science Citation Count  Cited 44 times in Thomson Reuters Web of Science Article | Citations
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