ArticleThe Analyst2015
New supercharging reagents produce highly charged protein ions in native mass spectrometry.
Article in The Analyst, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Native Mass Spectrometry of Soluble Proteins with Sodium Chloride Enabled by a Dendritic Detergent.ACS measurement science au · 2026Article
- Dynamic Additive Scanning for Precise Control in Electrospray Ionization Mass Spectrometry.ACS measurement science au · 2026Article
- Studying Membrane Protein-Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes.Journal of the American Society for Mass Spectrometry · 2023Article
- Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer.Nature methods · 2023Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Current perspectives on supercharging reagents in electrospray ionization mass spectrometry.RSC advances · 2021Review
- Structural Characterization of Carbonic Anhydrase-Arylsulfonamide Complexes Using Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2021Article
- Charge Manipulation Using Solution and Gas-Phase Chemistry to Facilitate Analysis of Highly Heterogeneous Protein Complexes in Native Mass Spectrometry.Analytical chemistry · 2021Article
- Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020Article
- Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins.Nature methods · 2020Article
- Overcharging Effect in Electrospray Ionization Mass Spectra of Daunomycin-Tuftsin Bioconjugates.Molecules (Basel, Switzerland) · 2019Article
- Chemical Additives Enable Native Mass Spectrometry Measurement of Membrane Protein Oligomeric State within Intact Nanodiscs.Journal of the American Chemical Society · 2019Article
- Resolving the Discrepancies Between Empirical and Rayleigh Charge Limiting Models for Globular Proteins.Journal of the American Society for Mass Spectrometry · 2018Article
- Enhancing Sensitivity of Liquid Chromatography-Mass Spectrometry of Peptides and Proteins Using Supercharging Agents.International journal of mass spectrometry · 2018Article
- Protein-Glass Surface Interactions and Ion Desalting in Electrospray Ionization with Submicron Emitters.Journal of the American Society for Mass Spectrometry · 2018Article
- Preliminary investigation of deoxyoligonucleotide binding to ribonuclease A using mass spectrometry: An attempt to develop a lab experience for undergraduates.F1000Research · 2018Article
- Real-time HD Exchange Kinetics of Proteins from Buffered Aqueous Solution with Electrothermal Supercharging and Top-Down Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- High-Resolution Live-Cell Imaging and Analysis by Laser Desorption/Ionization Droplet Delivery Mass Spectrometry.Analytical chemistry · 2016Article
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3 authors.
Funding
Abstract
The effectiveness of two new supercharging reagents for producing highly charged ions by electrospray ionization (ESI) from aqueous solutions in which proteins have native structures and reactivities were investigated. In aqueous solution, 2-thiophenone and 4-hydroxymethyl-1,3-dioxolan-2-one (HD) at a concentration of 2% by volume can increase the average charge of cytochrome c and myoglobin by up to 163%, resulting in even higher charge states than those that are produced from water/methanol/acid solutions in which these proteins are denatured. The greatest extent of supercharging occurs in pure water, but these supercharging reagents are also highly effective in aqueous solutions containing 200 mM ammonium acetate buffer commonly used in native mass spectrometry (MS). These reagents are less effective supercharging reagents than m-nitrobenzyl alcohol (m-NBA) and propylene carbonate (PC) when ions are formed from water/methanol/acid. The extent to which loss of the heme group from myoglobin occurs is related to the extent of supercharging. Results from guanidine melts of cytochrome c monitored with tryptophan fluorescence show that the supercharging reagents PC, sulfolane and HD are effective chemical denaturants in solution. These results provide additional evidence for the role of protein structural changes in the electrospray droplet as the primary mechanism for supercharging with these reagents in native MS. These results also demonstrate that for at least some proteins, the formation of highly charged ions from native MS is no longer a significant barrier for obtaining structural information using conventional tandem MS methods.
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