An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins.
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Authors
Helfinger, Lukas R
Solt, Andras
Publication Date
2017-10-10Journal Title
Journal of the American Chemical Society
ISSN
0002-7863
Volume
139
Issue
42
Pages
14829-14832
Language
eng
Type
Article
This Version
VoR
Physical Medium
Print-Electronic
Metadata
Show full item recordCitation
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
Abstract
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.
Keywords
Saposins, Phospholipids, Dimyristoylphosphatidylcholine, Membrane Proteins, Receptors, G-Protein-Coupled, Membranes, Artificial, Magnetic Resonance Spectroscopy, Biomimetics, Hydrogen-Ion Concentration, Nanoparticles
Sponsorship
BBSRC (BB/K01983X/1)
MRC (MR/L014254/1)
Identifiers
External DOI: https://doi.org/10.1021/jacs.7b06730
This record's URL: https://www.repository.cam.ac.uk/handle/1810/276383
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