Nanodisc

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Synthetic model membrane system

title: "Nanodisc" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["membrane-biology"] description: "Synthetic model membrane system" topic_path: "science/biology" source: "https://en.wikipedia.org/wiki/Nanodisc" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Synthetic model membrane system ::

::figure[src="https://upload.wikimedia.org/wikipedia/commons/2/28/NanodiscWith7TMMembraneProtein.jpg" caption="Schematic illustration of a MSP nanodisc with a [[7-transmembrane]] protein embedded. Diameter is about 10 nm. Picture from Sligar Lab" alt="Schematic illustration of a nanodisc with a 7-transmembrane protein embedded."] ::

A nanodisc is a synthetic model membrane system which assists in the study of membrane proteins. Nanodiscs are discoidal proteins in which a lipid bilayer is surrounded by molecules that are amphipathic molecules including proteins, peptides, and synthetic polymers. It is composed of a lipid bilayer of phospholipids with the hydrophobic edge screened by two amphipathic proteins. These proteins are called membrane scaffolding proteins (MSP) and align in double belt formation. Nanodiscs are structurally very similar to discoidal high-density lipoproteins (HDL) and the MSPs are modified versions of apolipoprotein A1 (apoA1), the main constituent in HDL. Nanodiscs are useful in the study of membrane proteins because they can solubilise and stabilise membrane proteins and represent a more native environment than liposomes, detergent micelles, bicelles and amphipols.

The art of making nanodiscs has progressed past using only the MSPs and lipids to make particles, leading to alternative strategies like peptide nanodiscs that use simpler proteins and synthetic nanodiscs that do not need any proteins for stabilization.

MSP nanodisc

The original nanodisc was produced by apoA1-derived MSPs from 2002.

Peptide nanodisc

In peptide nanodiscs, the lipid bilayer is screened by amphipathic peptides instead of two MSPs. Peptide nanodiscs are structurally similar to MSP nanodiscs and the peptides also align in a double belt. They can stabilise membrane proteins, but have higher polydispersity and are structurally less stable than MSP nanodiscs. Recent studies, however, showed that dimerization and polymerization of the peptides make them more stable.

Synthetic/Native nanodisc

Another way to mimic the native lipid membrane are synthetic polymers. Styrene-maleic acid co-polymers (SMAs) called SMALPs or Lipodisq and Diisobutylene-maleic acid (DIBMA) are such synthetic polymers (DIBMALPs). They can solubilize membrane proteins directly from cells or raw extract. They also have been used to study the lipid composition of several organisms. It was discovered that all synthetic polymers which contained a styrene and maleic acid group can solubilize proteins. These SMA nanoparticles have also been tested as possible drug delivery vehicle and for the study of folding, post-translational modifications and lipid interactions of membrane proteins by native mass spectrometry. They are now routinely used to solve membrane protein structures for cryo-EM, such as the aerolysin pore-forming toxins (2.1Å resolution), where some lipid density was modelled and key interactions relevant for the understanding of pore formation mechanism, its correct positioning and anchoring in the membrane were elucidated.

References

References

  1. (1 October 2015). "Dissecting the Structure of Membrane Proteins". [[Gen. Eng. Biotechnol. News.
  2. (April 2021). "Temperature- and composition-dependent conformational transitions of amphipathic peptide–phospholipid nanodiscs". Journal of Colloid and Interface Science.
  3. (March 2004). "Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size". Journal of the American Chemical Society.
  4. (November 2010). "Engineering extended membrane scaffold proteins for self-assembly of soluble nanoscale lipid bilayers". Protein Engineering, Design & Selection.
  5. (July 2019). "From polymer chemistry to structural biology: The development of SMA and related amphipathic polymers for membrane protein extraction and solubilisation". Chemistry and Physics of Lipids.
  6. (June 2009). "Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer". Journal of the American Chemical Society.
  7. (December 2017). "Formation of Lipid-Bilayer Nanodiscs by Diisobutylene/Maleic Acid (DIBMA) Copolymer". Langmuir.
  8. (November 2020). "Lipid nanoparticle technologies for the study of G protein-coupled receptors in lipid environments". Biophysical Reviews.
  9. (February 2021). "Lipidomic and in-gel analysis of maleic acid co-polymer nanodiscs reveals differences in composition of solubilized membranes". Communications Biology.
  10. (August 2019). "Lipodisqs for eukaryote lipidomics with retention of viability: Sensitivity and resistance to Leucobacter infection linked to C.elegans cuticle composition". Chemistry and Physics of Lipids.
  11. "Diisobutylene-maleic acid (DIBMA)".
  12. (April 2020). "Physicochemical Characterization, Toxicity and ''In Vivo'' Biodistribution Studies of a Discoidal, Lipid-Based Drug Delivery Vehicle: Lipodisq Nanoparticles Containing Doxorubicin". Journal of Biomedical Nanotechnology.
  13. (March 2021). "Detergent-free Lipodisq Nanoparticles Facilitate High-Resolution Mass Spectrometry of Folded Integral Membrane Proteins". Nano Letters.
  14. (12 February 2025). "Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment". Journal of the American Chemical Society.

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membrane-biology