Recent advances in nanodisc technology for membrane protein studies (2012-2017)

被引:64
|
作者
Rouck, John E. [1 ,2 ]
Krapf, John E. [1 ,2 ]
Roy, Jahnabi [3 ]
Huff, Hannah C. [3 ]
Das, Aditi [1 ,2 ,4 ]
机构
[1] Univ Illinois, Dept Comparat Biosci, Dept Biochem, Beckman Inst Adv Sci,Div Nutr Sci,Neurosci Progra, Urbana, IL USA
[2] Univ Illinois, Dept Bioengn, Urbana, IL 61802 USA
[3] Univ Illinois, Dept Chem, Urbana, IL USA
[4] Univ Illinois, Dept Comparat Biosci, Div Nutr Sci, Neurosci Program, Urbana, IL USA
关键词
electron microscopy; ESI; FRET; isotope labeling; lipid bilayer; MALDI; membrane protein; nanodisc; NMR; SPR; LIPID-BILAYER NANODISCS; NEUROTRANSMITTER-SODIUM SYMPORTER; CELL-DIVISION ZIPA; CRYO-EM STRUCTURE; SOLID-STATE NMR; PHOSPHOLIPID-BILAYER; MASS-SPECTROMETRY; SUBSTRATE-BINDING; X-RAY; FUNCTIONAL RECONSTITUTION;
D O I
10.1002/1873-3468.12706
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Historically, the main barrier to membrane protein investigations has been the tendency of membrane proteins to aggregate (due to their hydrophobic nature), in aqueous solution as well as on surfaces. The introduction of biomembrane mimetics has since stimulated momentum in the field. One such mimetic, the nanodisc (ND) system, has proved to be an exceptional system for solubilizing membrane proteins. Herein, we critically evaluate the advantages and imperfections of employing nanodiscs in biophysical and biochemical studies. Specifically, we examine the techniques that have been modified to study membrane proteins in nanodiscs. Techniques discussed here include fluorescence microscopy, solution-state/solid-state nuclear magnetic resonance, electron microscopy, small-angle X-ray scattering, and several mass spectroscopy methods. Newer techniques such as SPR, charge-sensitive optical detection, and scintillation proximity assays are also reviewed. Lastly, we cover how nanodiscs are advancing nanotechnology through nanoplasmonic biosensing, lipoprotein-nanoplatelets, and sortase-mediated labeling of nanodiscs.
引用
收藏
页码:2057 / 2088
页数:32
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