An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins.
Helfinger, Lukas R
Journal of the American Chemical Society
MetadataShow full item record
Chien, C. H., Helfinger, L. R., Bostock, M., Solt, A., Tan, Y. L., & Nietlispach, D. (2017). An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins.. Journal of the American Chemical Society, 139 (42), 14829-14832. https://doi.org/10.1021/jacs.7b06730
Based on the saposin-A (SapA) scaffold protein we demonstrate the suitability of a size-adaptable phospholipid membrane-mimetic system for solution NMR studies of membrane proteins under close-to-native conditions. The Salipro nanoparticle size can be tuned over a wide pH range by adjusting the saposin-to-lipid stoichiometry enabling maintenance of sufficiently high amounts of phospholipid in the Salipro nanoparticle to mimic a realistic membrane environment while controlling the overall size to enable solution NMR for a range of membrane proteins. Three representative membrane proteins including one G-protein-coupled receptor (GPCR) were successfully incorporated into SapA-dimyristoylphosphatidylcholine (DMPC) nanoparticles and studied by solution NMR spectroscopy.
Saposins, Phospholipids, Dimyristoylphosphatidylcholine, Membrane Proteins, Receptors, G-Protein-Coupled, Membranes, Artificial, Magnetic Resonance Spectroscopy, Biomimetics, Hydrogen-Ion Concentration, Nanoparticles
External DOI: https://doi.org/10.1021/jacs.7b06730
This record's URL: https://www.repository.cam.ac.uk/handle/1810/276383
Attribution 4.0 International
Licence URL: http://creativecommons.org/licenses/by/4.0/
Recommended or similar items
The following licence files are associated with this item: