Towards high-throughput identification of endocrine disrupting compounds with mass spectrometry

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Author(s) Bovet, Cédric, Plet, Benoit, Ruff, Marc, Eiler, Sylvia, Granger, Florence, Panagiotidis, Andreas, Wenzel, Ryan, Nazabal, Alexis, Moras, Dino, Zenobi, Renato
Publication Type Journal Items, Publication Status: Published
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Title Towards high-throughput identification of endocrine disrupting compounds with mass spectrometry
Author(s) Bovet, Cédric
Plet, Benoit
Ruff, Marc
Eiler, Sylvia
Granger, Florence
Panagiotidis, Andreas
Wenzel, Ryan
Nazabal, Alexis
Moras, Dino
Zenobi, Renato
Journal or Series Title Toxicology in vitro
Volume Number 23
Issue Number 4
Start Page 704
End Page 709
ISSN 0887-2333
Publisher Pergamon Press
Publication Place Oxford
Publication Date 2009
Keyword(s) Mass spectrometry
Endocrine disrupting compounds
Automated sample preparation
Abstract High-mass matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) combined with chemical cross-linking has the ability to monitor the ligand-dependent dimerization of the human estrogen receptor alpha ligand binding domain (hER alpha LBD) in solution. Because only ER ligands enhance the homodimer abundance, we evaluated the ability of this label-free approach for identifying endocrine disrupting compounds (EDCs) in a high-throughput manner. This was achieved by combining an automated liquid handler with an automated MS acquisition procedure, which allowed a five-fold gain in operator time compared to a fully manual approach. To detect ligand binding with enough confidence, the receptor has to be incubated with at least a 10 mu M concentration of the test compound. Based on the increase of the measured homodimer intensity, eight compounds with a relative binding affinity (RBA, relative to the natural hormone estradiol) >7% were identified as ER ligands among the 28 chemicals tested. Two other compounds, quercetin and 4-tert-amylphenol, were also identified as ER ligands, although their RBAs have been reported to be only 0.01% and 0.000055%, respectively. This suggests that these two ligands have a higher affinity for hER alpha LBD than reported in the literature. The high-mass MALDI approach thus allows identifying high affinity EDCs in an efficient way.
DOI 10.1016/j.tiv.2009.02.004
Additional Notes Received 13 June 2008, Accepted 6 February 2009, Available online 20 February 2009
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 03430
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NEBIS System Number 000036642
Source Database ID PP-49609
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  author = "Bovet, C{\'{e}}dric and Plet, Benoit and Ruff, Marc and Eiler, Sylvia and Granger, Florence and Panagiotidis, Andreas and Wenzel, Ryan and Nazabal, Alexis and Moras, Dino and Zenobi, Renato",
  title = "{T}owards high-throughput identification of endocrine disrupting compounds with mass spectrometry",
  journal = "Toxicology in vitro",
  year = 2009,
  volume = "23",
  number = "4",
  pages = "704--709",

E-Citations record created: Tue, 04 May 2010, 12:04:37 CET