journal article·2021-06-08

Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs

Nicolai Tidemand Johansen, Alessandra Luchini, Frederik Grønbæk Tidemand, Simone Orioli, Anne Martel, Lionel Porcar, Lise Arleth, Martin Cramer Pedersen

Langmuir· Volume 37· Issue 22
Publisher page

Abstract

Nanodiscs based on membrane scaffold proteins (MSPs) and phospholipids are used as membrane mimics to stabilize membrane proteins in solution for structural and functional studies. Combining small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), and time-resolved small-angle neutron scattering (TR-SANS), we characterized the structure and lipid bilayer properties of five different nanodiscs made with dimyristoylphosphatidylcholine and different MSPs varying in size, charge, and circularization. Our SAXS modeling showed that the structural parameters of the embedded lipids are all similar, irrespective of the MSP properties. DSC showed that the lipid packing is not homogeneous in the nanodiscs and that a 20 Å wide boundary layer of lipids with perturbed packing is located close to the MSP, while the packing of central lipids is tighter than in large unilamellar vesicles. Finally, TR-SANS showed that lipid exchange rates in nanodiscs decrease with increasing nanodisc size and are lower for the nanodiscs made with supercharged MSPs compared to conventional nanodiscs. Altogether, the results provide a thorough biophysical understanding of the nanodisc as a model membrane system, which is important in order to carry out and interpret experiments on membrane proteins embedded in such systems.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Lipid Membrane Structure and Behavior · Supramolecular Self-Assembly in Materials · RNA Interference and Gene Delivery

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Structural Biophysics Group, Niels Bohr Institute, University of Copenhagen, 2100 Copenhagen E, Denmark

Structural Biology and NMR Laboratory and Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, 2200 Copenhagen N, Denmark

Institut Laue Langevin, 38000 Grenoble, France

Funding

Lundbeckfonden

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