The phospholipid packing arrangement in small bilayer vesicles as revealed by proton magnetic resonance studies at 500 MHz.

Proton magnetic resonance spectra of saturated phospholipids in small unilamellar vesicles has been recorded at 500 MHz on a Bruker WM500 spectrometer. The additional spectral dispersion reveals new structure in the acyl chain resonances. At temperatures near the thermal phase transition, the chain methylene and methyl peaks are split, both showing a broad and a relatively sharp component. Magnetization transfer experiments together with studies in the presence of manganese ions inside or outside the vesicles indicate that the sharp component is to be assigned to the protons from the acyl chains in the inner half of the bilayer and the broad component to chains in the outer monolayer. These experiments demonstrate unambiguously that the extreme surface curvature intrinsic to small unilamellar vesicles induces a profound asymmetry in the packing arrangement of the hydrocarbon chains in the two leaflets of the bilayer and causes the two monolayers to exist in markedly different motional states.