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Biophys J, February 1998, p. 857-868, Vol. 74, No. 2
*Département de Chimie, Centre de Recherche en Sciences et Ingénierie des Macromolécules, Université Laval, Québec, Québec G1K 7P4, Canada, and #Centre de Recherche Paul Pascal, CNRS, 33600 Pessac, France
31P two-dimensional exchange solid-state NMR
spectroscopy was used to measure the lateral diffusion,
DL, in the fluid phase of
dipalmitoylphosphatidylcholine (DPPC) in the presence and absence of
melittin. The use of a spherical solid support with a radius of
320 ± 20 nm, on which lipids and peptides are adsorbed together, and a novel way of analyzing the two-dimensional exchange patterns afforded a narrow distribution of DL
centered at a value of (8.8 ± 0.5) × 10
8
cm2/s for the pure lipid system and a large distribution of
DL spanning 1 × 10
8 to
10 × 10
8 cm2/s for the lipids in the
presence of melittin. In addition, the determination of
DL for nonsupported DPPC multilamellar
vesicles (MLVs) suggests that the support does not slow down the lipid diffusion and that the radii of the bilayers vary from 300 to 800 nm.
Finally, the DPPC-melittin complex is stabilized at the surface of the
silica beads in the gel phase, opening the way to further study of the
interaction between melittin and DPPC.
Biophys J, February 1998, p. 857-868, Vol. 74, No. 2
© 1998 by the Biophysical Society 0006-3495/98/02/857/12 $2.00
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