@article{b6b4b93d77304410af852174d777df3d,
title = "Nanodiscs: A toolkit for membrane protein science",
abstract = "Membrane proteins are involved in numerous vital biological processes, including transport, signal transduction and the enzymes in a variety of metabolic pathways. Integral membrane proteins account for up to 30% of the human proteome and they make up more than half of all currently marketed therapeutic targets. Unfortunately, membrane proteins are inherently recalcitrant to study using the normal toolkit available to scientists, and one is most often left with the challenge of finding inhibitors, activators and specific antibodies using a denatured or detergent solubilized aggregate. The Nanodisc platform circumvents these challenges by providing a self-assembled system that renders typically insoluble, yet biologically and pharmacologically significant, targets such as receptors, transporters, enzymes, and viral antigens soluble in aqueous media in a native-like bilayer environment that maintain a target's functional activity. By providing a bilayer surface of defined composition and structure, Nanodiscs have found great utility in the study of cellular signaling complexes that assemble on a membrane surface. Nanodiscs provide a nanometer scale vehicle for the in vivo delivery of amphipathic drugs, therapeutic lipids, tethered nucleic acids, imaging agents and active protein complexes. This means for generating nanoscale lipid bilayers has spawned the successful use of numerous other polymer and peptide amphipathic systems. This review, in celebration of the Anfinsen Award, summarizes some recent results and provides an inroad into the current and historical literature.",
keywords = "Nanodisc, lipid bilayer, membrane protein, signaling complex",
author = "Sligar, {Stephen G.} and Denisov, {Ilia G.}",
note = "Funding Information: Our work has been supported uninterrupted for over four decades through the National Institutes of Health General Medical Sciences. Receipt of a MIRA award GM118145 allowed exploring a breadth of scientific inquiry in different systems where Nanodisc technology could lead to major advances in the understanding of membrane protein structure and function. The research described and referenced herein is the product of an incredibly talented group of graduate students, technicians, post-doctoral associates and senior research scientists. Our current group includes members that have been with the laboratory for more than 20 years. Finally, the highly collaborative and supportive research environment and colleagues at the University of Illinois Chemistry and Biochemistry departments has encouraged expansion into new arenas of scientific inquiry. All are gratefully acknowledged. Funding Information: Our work has been supported uninterrupted for over four decades through the National Institutes of Health General Medical Sciences. Receipt of a MIRA award GM118145 allowed exploring a breadth of scientific inquiry in different systems where Nanodisc technology could lead to major advances in the understanding of membrane protein structure and function. The research described and referenced herein is the product of an incredibly talented group of graduate students, technicians, post‐doctoral associates and senior research scientists. Our current group includes members that have been with the laboratory for more than 20 years. Finally, the highly collaborative and supportive research environment and colleagues at the University of Illinois Chemistry and Biochemistry departments has encouraged expansion into new arenas of scientific inquiry. All are gratefully acknowledged. Publisher Copyright: {\textcopyright} 2020 The Protein Society",
year = "2021",
month = feb,
doi = "10.1002/pro.3994",
language = "English (US)",
volume = "30",
pages = "297--315",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "2",
}