NMR is commonly used for the structural characterisation (both the chemical characterisation and the three dimensional structure), but it is also a very efficient spectroscopy for the analysis of the interactions between molecular assemblies. These studies can give information both at the thermodynamic level and at the kinetic level. These properties allow us to propose the use of small unilamellar vesicles (SUVs) as a possible membrane model for the study of the interaction of peptides or proteins with a phospholipid bilayer. Such a model can be used in complement with the work in micellar media by NMR experiments in liquid conditions. Although very often used the micellar media are not always the best membrane model and SUVs can constitute an interesting alternative.
Numerous new improvements for solid-state NMR studies have been developed for peptides deeply inserted inside the membrane bilayer. These new methods are not efficient in case of very dynamical character of the peptide-lipid interaction. By contrast, when the association-dissociation kinetic rates are fast enough SUVs permit to obtain good quality NMR spectra of interacting peptides. In these conditions three dimensional structure of peptides interacting with SUVs have already been obtained in a lipidic environment.
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