MARTINEZ, Denis; DECOSSAS, Marion; KOWAL, Julia; FREY, Lukas; STAHLBERG, Henning; DUFOURC, Erick J.; RIEK, Roland; HABENSTEIN, Birgit; BIBOW, Stefan; LOQUET, Antoine

doi:10.1002/cphc.201700450

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MARTINEZ, Denis

Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

DECOSSAS, Marion
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

KOWAL, Julia

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Chemphyschem : a European journal of chemical physics and physical chemistry. 2017-06, vol. 18, n° 2, p. 2651-2657

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Nanodiscs offer a very promising tool to incorporate membrane proteins into native-like lipid bilayers and an alternative to liposomes to maintain protein functions and protein-lipid interactions in a soluble nanoscale object. The activity of the incorporated membrane protein appears to be correlated to its dynamics in the lipid bilayer and by protein-lipid interactions. These two parameters depend on the lipid internal dynamics surrounded by the lipid-encircling discoidal scaffold protein that might differ from more unrestricted lipid bilayers observed in vesicles or cellular extracts. A solid-state NMR spectroscopy investigation of lipid internal dynamics and thermotropism in nanodiscs is reported. The gel-to-fluid phase transition is almost abolished for nanodiscs, which maintain lipid fluid properties for a large temperature range. The addition of cholesterol allows fine-tuning of the internal bilayer dynamics by increasing chain ordering. Increased site-specific order parameters along the acyl chain reflect a higher internal ordering in nanodiscs compared with liposomes at room temperature; this is induced by the scaffold protein, which restricts lipid diffusion in the nanodisc area.< Réduire

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Lipid Internal Dynamics Probed in Nanodiscs

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