Nanodisc self-assembly is thermodynamically reversible and controllable.

Soft Matter
Tyler Camp, Stephen G Sligar

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 dem...Continue Reading

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Citations

Nov 10, 2020·Protein Science : a Publication of the Protein Society·Stephen G Sligar, Ilia G Denisov

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Methods Mentioned

BETA
X-ray
optical spectroscopy
ISS
NMR
second
electron
nuclear magnetic resonance

Software Mentioned

VINCI

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