title: Phospholipid packing and conformation in small vesicles revealed by two-dimensional 1H nuclear magnetic resonance cross-relaxation spectroscopy.
abstract: Two-dimensional 1H-NMR spectroscopy has been used to examine cross-relaxation in sonicated phospholipid vesicle systems. The observed pattern of proton cross-relaxation reveals several important features of these vesicle systems. For example, cross-relaxation rates on each monolayer of the vesicle system can be resolved and reflect the expected geometric packing constraints of the vesicle system. Small but significant magnetization-exchange is also seen to develop between the headgroup N-methyl resonance and the terminal methyl resonance. Spectra taken with deuterated lipids indicate that this exchange is not mediated by spin-diffusion down the length of the alkyl chains. Since spin-diffusion is the only process that is expected to facilitate magnetization-exchange over distances of 15-20 A, a close proximity of headgroup and terminal methyl protons in a fraction of the membrane lipid is indicated by these results. This could occur by events such as lipid interdigitation or alkyl chain bends that terminate lipid alkyl chain ends near the membrane surface.
mesh_terms: D008081:Liposomes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D008968:Molecular Conformation; D010713:Phosphatidylcholines; D011663:Pulmonary Surfactants
chemical_list: D008081:Liposomes; D010713:Phosphatidylcholines; D011663:Pulmonary Surfactants