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

Chih-Ta Henry Chien | Zendy; Lukas R. Helfinger | Zendy; Mark J. Bostock | Zendy; Andras Solt | Zendy; Yi Lei Tan | Zendy; Daniel Nietlispach | Zendy

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

Author(s) -

Chih-Ta Henry Chien,

Lukas R. Helfinger,

Mark J. Bostock,

Andras Solt,

Yi Lei Tan,

Daniel Nietlispach

Publication year - 2017

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/jacs.7b06730

Subject(s) - chemistry , phospholipid , membrane , nanodisc , membrane protein , nuclear magnetic resonance spectroscopy , nanoparticle , protein–lipid interaction , biophysics , lipid bilayer , stoichiometry , integral membrane protein , nanotechnology , biochemistry , organic chemistry , materials science , biology

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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