Surfactant effects on protein structure examined by electrospray ionization mass spectrometry
Open accessAbstract
Electrospray ionization mass spectrometry (ESI‐MS) has proven to be a useful tool for examining noncovalent complexes between proteins and a variety of ligands. It has also been used to distinguish between denatured and refolded forms of proteins. Surfactants are frequently employed to enhance solubilization or to modify the tertiary or quaternary structure of proteins, but are usually considered incompatible with mass spectrometry. A broad range of ionic, nonionic, and zwitterionic surfactants was examined to characterize their effects on ESI‐MS and on protein structure under ESI‐MS conditions. Solution conditions studied include 4% acetic acid/50% acetonitrile/46% H 2 O and 100% aqueous. Of the surfactants examined, the nonionic saccharides, such as n‐dodecyl‐β‐D‐gluco‐pyranoside, at 0.1% to 0.01% (w/v) concentrations, performed best, with limited interference from chemical background and adduct formation. Under the experimental conditions used, ESI‐MS performance in the presence of surfactants was found to be unrelated to critical micelle concentration. It is demonstrated that surfactants can affect both the tertiary and quaternary structures of proteins under conditions used for ESI‐MS. However, several of the surfactants caused significant shifts in the charge‐state distributions, which appeared to be independent of conformational effects. These observations suggest that surfactants, used in conjunction with ESI‐MS, can be useful for protein structure studies, if care is used in the interpretation of the results.
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Most salts and conventional surfactants are incompatible with MS and must be removed before downstream analysis.
“However, most salts and conventional surfactants are generally incompatible with MS analysis and must be removed before downstream analysis [22].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [22]
Precipitation is often required with surfactants because surfactants inhibit MS signal by outcompeting proteins or forming harmful adducts.
“In particular, precipitation is often required when using surfactants, which are often employed during cell lysis to solubilize hydrophobic membrane proteins, because they significantly inhibit MS signal by outcompeting proteins for ionization or by forming harmful adducts [24,25].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [24]
A clear 1% solution of Azo has a Krafft temperature of 24.5 °C, as reported in prior work.
“Kraft temperature (a clear 1% surfactant solution) was previously reported at 24.5 °C7.”
From A photocleavable surfactant for top-down proteomics (2019) · cites this paper as [7]
Conventional ionic surfactants are incompatible with mass spectrometry because they greatly suppress protein MS signal.
“Unfortunately, conventional ionic surfactants are not compatible with MS because they greatly suppress protein MS signal6, 7.”
From A photocleavable surfactant for top-down proteomics (2019) · cites this paper as [7]
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- Authors
- Loo, R. R. O., Dales, N., & Andrews, P. C.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Andrews, P. C.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 1994-11
- Volume
- 3
- Issue
- 11
- Pages
- 1975-1983
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC2142636
- OpenAlex
- W1996316908
- Cited by
- 184
- References
- 35
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 7 · 2023: 8 · 2022: 7 · 2021: 10 · 2020: 11 · 2019: 5 · 2018: 7 · 2017: 7 · 2016: 11 · 2015: 9 · 2014: 4 · 2013: 6 · 2012: 3
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Protein Science (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- surfactants, protein structure, electrospray ionization mass spectrometry, nonionic surfactants, protein tertiary structure, quaternary structure, charge state distribution, critical micelle concentration, protein denaturation, adduct formation
- MeSH terms
- Cytochrome c Group, Detergents, Micelles, Muramidase, Myoglobin, Protein Binding, Protein Conformation, Protein Denaturation, Mass Spectrometry, Surface-Active Agents, Ubiquitins, Protein Structure, Tertiary
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