Native Mass Spectrometry Characterization of Intact Nanodisc Lipoprotein Complexes

We describe here the analysis of nanodisc complexes by using native mass spectrometry (MS) to characterize their molecular weight (MW) and polydispersity. Nanodiscs are nanoscale lipid bilayers that offer a platform for solubilizing membrane proteins. Unlike detergent micelles, nanodiscs are native-...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2012-11, Vol.84 (21), p.8957-8960
Main Authors: Marty, Michael T, Zhang, Hao, Cui, Weidong, Blankenship, Robert E, Gross, Michael L, Sligar, Stephen G
Format: Article
Language:English
Subjects:
Analytical chemistry
BASIC BIOLOGICAL SCIENCES
Chemistry
detergents
dissociation
Exact sciences and technology
gases
lipid bilayers
Lipid Bilayers - chemistry
Lipids
Lipoproteins
Lipoproteins - chemistry
Mass Spectrometry
membrane proteins
Membranes
micelles
Models, Molecular
Molecular Conformation
Molecular Weight
Molecules
Nanostructures - chemistry
Proteins
scaffolding proteins
SOLAR ENERGY
solubilization
Spectrometric and optical methods
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Summary:We describe here the analysis of nanodisc complexes by using native mass spectrometry (MS) to characterize their molecular weight (MW) and polydispersity. Nanodiscs are nanoscale lipid bilayers that offer a platform for solubilizing membrane proteins. Unlike detergent micelles, nanodiscs are native-like lipid bilayers that are well-defined and potentially monodisperse. Their mass spectra allow peak assignment based on differences in the mass of a single lipid per complex. Resultant masses agree closely with predicted values and demonstrate conclusively the narrow dispersity of lipid molecules in the nanodisc. Fragmentation with collisionally activated dissociation (CAD) or electron-capture dissociation (ECD) shows loss of a small number of lipids and eventual collapse of the nanodisc with release of the scaffold protein. These results provide a foundation for future studies utilizing nanodiscs as a platform for launching membrane proteins into the gas phase.
ISSN:0003-2700
1520-6882
1520-6882
DOI:10.1021/ac302663f