Applications of Phospholipid Bilayer Nanodiscs in the Study of Membranes and Membrane Proteins

Abhinav Nath, William M. Atkins, Stephen G. Sligar

Biochemistry · 2007 · 437 citations · 81 references

Concepts

TL;DR

Phospholipid bilayer Nanodiscs, derived from high‑density lipoprotein particles, provide a monodisperse, stable, nativelike membrane model that overcomes the insolubility and polydispersity issues of traditional liposomes and detergent micelles. These proteins are simultaneously monomerized, solubilized, and incorporated into the well‑defined membrane environment provided by Nanodiscs. Nanodiscs have been employed to study diverse membrane proteins such as cytochrome P450s, GPCRs, and bacterial chemoreceptors, and they also offer insights into membrane thermodynamics, biophysics, and small‑molecule binding.

Abstract

Phospholipid bilayer Nanodiscs are novel model membranes derived from high-density lipoprotein particles and have proven to be useful in studies of membrane proteins. Membrane protein enzymology has been hampered by the inherent insolubility of membrane proteins in aqueous environments and has necessitated the use of model membranes such as liposomes and detergent-stabilized micelles. Current model membranes display a polydisperse particle size distribution and can suffer from problems of inconsistency and instability. It is also unclear how well they mimic biological lipid bilayers. In contrast, Nanodiscs, the particle size of which is constrained by a coat of scaffold proteins, are relatively monodisperse, stable model membranes with a "nativelike" lipid bilayer. Nanodiscs have already been used to study a variety of membrane proteins, including cytochrome P450s, seven-transmembrane proteins, and bacterial chemoreceptors. These proteins are simultaneously monomerized, solubilized, and incorporated into the well-defined membrane environment provided by Nanodiscs. Nanodiscs may also provide useful insights into the thermodynamics and biophysics of biological membranes and binding of small molecules to membranes.

References

81