An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins

被引:31
作者
Chien, Chih-Ta Henry [1 ]
Helfinger, Lukas R. [1 ]
Bostock, Mark J. [1 ]
Solt, Andras [1 ]
Tan, Yi Lei [1 ]
Nietlispach, Daniel [1 ]
机构
[1] Univ Cambridge, Dept Biochem, 80 Tennis Court Rd, Cambridge CB2 1GA, England
基金
英国生物技术与生命科学研究理事会;
关键词
BETA(2)-ADRENERGIC RECEPTOR; NANODISCS; SPECTROSCOPY; ENVIRONMENT; BICELLES; DYNAMICS; SAPOSIN; LIPIDS;
D O I
10.1021/jacs.7b06730
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:14829 / 14832
页数:4
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