Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 141, Issue 2, Pages 1054-1061Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b11529
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Funding
- American Cancer Society Institutional Research [IRG-16-124-37-IRG]
- Bisgrove Scholar Award from Science Foundation Arizona
- American Society for Mass Spectrometry Research Award
- National Institute of General Medical Sciences [R01 GM127579, R35 GM128624]
- National Institutes of Health [R01 GM127579, R35 GM128624]
- National Science Foundation - Environmental Protection Agency, as part of the Networks for Sustainable Molecular Design and Synthesis Program [CHE-1339597]
- National Institute of Allergy and Infectious Diseases [R21-AI125804-02]
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Membrane proteins play critical biochemical roles but remain challenging to study. Recently, native or nondenaturing mass spectrometry (MS) has made great strides in characterizing membrane protein interactions. However, conventional native MS relies on detergent micelles, which may disrupt natural interactions. Lipoprotein nanodiscs provide a platform to present membrane proteins for native MS within a lipid bilayer environment, but previous native MS of membrane proteins in nanodiscs has been limited by the intermediate stability of nanodiscs. It is difficult to eject membrane proteins from nanodiscs for native MS but also difficult to retain intact nanodisc complexes with membrane proteins inside. Here, we employed chemical reagents that modulate the charge acquired during electrospray ionization (ESI). By modulating ESI conditions, we could either eject the membrane protein complex with few bound lipids or capture the intact membrane protein nanodisc complex-allowing measurement of the membrane protein oligomeric state within an intact lipid bilayer environment. The dramatic differences in the stability of nanodiscs under different ESI conditions opens new applications for native MS of nanodiscs.
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