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Nanodisc self-assembly is thermodynamically reversible and controllable.
- Source :
-
Soft matter [Soft Matter] 2020 Jun 24; Vol. 16 (24), pp. 5615-5623. - Publication Year :
- 2020
-
Abstract
- Many highly ordered complex systems form by the spontaneous self-assembly of simpler subunits. An important biophysical tool that relies on self-assembly is the Nanodisc system, which finds extensive use as native-like environments for studying membrane proteins. Nanodiscs are self-assembled from detergent-solubilized mixtures of phospholipids and engineered helical proteins called membrane scaffold proteins (MSPs). Detergent removal results in the formation of nanoscale bilayers stabilized by two MSP "belts." Despite their numerous applications in biology, and contributions from many laboratories world-wide, little is known about the self-assembly process such as when the bilayer forms or when the MSP associates with lipids. We use fluorescence and optical spectroscopy to probe self-assembly at various equilibria defined by the detergent concentration. We show that the bilayer begins forming below the critical micellar concentration of the detergent (10 mM), and the association of MSP and lipids begins at lower detergent levels, showing a dependence on the concentrations of MSP and lipids. Following the dissolution process by adding detergent to purified Nanodiscs demonstrates that the self-assembly is reversible. Our data demonstrate that Nanodisc self-assembly is experimentally accessible, and that controlling the detergent concentration allows exquisite control over the self-assembly reaction. This improved understanding of self-assembly could lead to better functional incorporation of hitherto intractable membrane target proteins.
- Subjects :
- 2-Naphthylamine analogs & derivatives
2-Naphthylamine chemistry
Anisotropy
Fluorescent Dyes chemistry
Laurates chemistry
Phospholipids chemistry
Spectrum Analysis
Thermodynamics
Tyrosine chemistry
Detergents chemistry
Lipid Bilayers chemistry
Membrane Proteins chemistry
Nanostructures chemistry
Sodium Cholate chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-6848
- Volume :
- 16
- Issue :
- 24
- Database :
- MEDLINE
- Journal :
- Soft matter
- Publication Type :
- Academic Journal
- Accession number :
- 32524103
- Full Text :
- https://doi.org/10.1039/d0sm00336k