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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Lipid Internal Dynamics Probed in Nanodiscs.

Denis Martinez¹, Marion Decossas¹, Julia Kowal²

¹CBMN, CNRS., University of Bordeaux, IECB, All. Geoffroy Saint-Hilaire, 34600, Pessac, France.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry

|June 3, 2017

Summary

This summary is machine-generated.

Nanodiscs maintain lipid fluidity across a wide temperature range, unlike liposomes. Scaffold proteins in nanodiscs increase lipid ordering and restrict diffusion, impacting membrane protein dynamics.

Keywords:

NMR spectroscopy lipids membranes nanostructures solid-state structures

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Area of Science:

Biophysics
Structural Biology
Membrane Protein Research

Background:

Nanodiscs are soluble nanoscale discoidal particles that encapsulate lipid bilayers, serving as an alternative to liposomes for studying membrane proteins.
Membrane protein activity is linked to lipid bilayer dynamics and protein-lipid interactions, which can be influenced by the nanodisc's scaffold protein.

Purpose of the Study:

To investigate lipid internal dynamics and thermotropism within nanodiscs using solid-state NMR spectroscopy.
To compare lipid behavior in nanodiscs with that in liposomes and understand the influence of the scaffold protein.

Main Methods:

Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
Lipid internal dynamics and thermotropic properties of nanodiscs were analyzed.

Main Results:

The gel-to-fluid phase transition of lipids in nanodiscs is largely abolished, maintaining fluidity over a broad temperature range.
Cholesterol addition modulates internal bilayer dynamics, increasing lipid chain ordering.
The scaffold protein induces higher site-specific order parameters in nanodiscs compared to liposomes, restricting lipid diffusion.

Conclusions:

Nanodiscs provide a stable, fluid lipid environment for membrane proteins, with dynamics distinct from liposomes.
The scaffold protein plays a crucial role in modulating lipid ordering and dynamics within nanodiscs.
These findings are vital for understanding how nanodisc properties affect incorporated membrane protein function.