Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 42, Pages 14829-14832Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b06730
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Funding
- BBSRC [BB/K01983 X/1]
- BBSRC [BB/K01983X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K01983X/1] Funding Source: researchfish
- Medical Research Council [1509279] Funding Source: researchfish
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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 (MPs) 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 MPs. Three representative MPs, including one G-protein-coupled receptor, were successfully incorporated into SapA-dimyristoylphosphatidylcholine nanoparticles and studied by solution NMR spectroscopy.
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