ArticleProtein science : a publication of the Protein Society2007
Estrogen receptor-ligand complexes measured by chip-based nanoelectrospray mass spectrometry: an approach for the screening of endocrine disruptors.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 44 citations in OpenAlex.
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- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Influence of Linkage Stereochemistry and Protecting Groups on Glycosidic Bond Stability of Sodium Cationized Glycosyl Phosphates.Journal of the American Society for Mass Spectrometry · 2017Article
- Structure-Based Understanding of Binding Affinity and Mode of Estrogen Receptor α Agonists and Antagonists.PloS one · 2017Article
- Native Mass Spectrometry in Fragment-Based Drug Discovery.Molecules (Basel, Switzerland) · 2016Review
- Mass spectrometric analysis of protein-ligand interactions.Biophysics and physicobiology · 2016Article
- Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.Journal of the American Society for Mass Spectrometry · 2016Article
- Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: a systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors.Journal of the American Society for Mass Spectrometry · 2012Article
- Integrating mass spectrometry of intact protein complexes into structural proteomics.Proteomics · 2012Review
- Studying protein-protein affinity and immobilized ligand-protein affinity interactions using MS-based methods.Analytical and bioanalytical chemistry · 2011Review
- Protein-protein binding affinities in solution determined by electrospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Detection of nucleic acid-nuclear hormone receptor complexes with mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Probing the hydrophobic effect of noncovalent complexes by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- CE50: quantifying collision induced dissociation energy for small molecule characterization and identification.Journal of the American Society for Mass Spectrometry · 2009Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present report, a method based on chip-based nanoelectrospray mass spectrometry (nanoESI-MS) is described to detect noncovalent ligand binding to the human estrogen receptor alpha ligand-binding domain (hERalpha LBD). This system represents an important environmental interest, because a wide variety of molecules, known as endocrine disruptors, can bind to the estrogen receptor (ER) and induce adverse health effects in wildlife and humans. Using proper experimental conditions, the nanoESI-MS approach allowed for the detection of specific ligand interactions with hERalpha LBD. The relative gas-phase stability of selected hERalpha LBD-ligand complexes did not mirror the binding affinity in solution, a result that demonstrates the prominent role of hydrophobic contacts for stabilizing ER-ligand complexes in solution. The best approach to evaluate relative solution-binding affinity by nanoESI-MS was to perform competitive binding experiments with 17beta-estradiol (E2) used as a reference ligand. Among the ligands tested, the relative binding affinity for hERalpha LBD measured by nanoESI-MS was 4-hydroxtamoxifen approximately diethylstilbestrol > E2 >> genistein >> bisphenol A, consistent with the order of the binding affinities in solution. The limited reproducibility of the bound to free protein ratio measured by nanoESI-MS for this system only allowed the binding constants (K(d)) to be estimated (low nanomolar range for E2). The specificity of nanoESI-MS combined with its speed (1 min/ligand), low sample consumption (90 pmol protein/ligand), and its sensitivity for ligand (30 ng/mL) demonstrates that this technique is a promising method for screening suspected endocrine disrupting compounds and to qualitatively evaluate their binding affinity.
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