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Towards High-Throughput Identification of Endocrine Disrupting Compounds With Mass Spectrometry

Towards High-Throughput Identification of Endocrine Disrupting Compounds With Mass Spectrometry

Cédric Bovet, Benoit Plet, Marc Ruff, Sylvia Eiler, Florence Granger, Andreas Panagiotidis, Ryan Wenzel, Alexis Nazabal, Dino Moras, Renato Zenobi

Toxicol In Vitro. 2009 Jun;23(4):704-9.

PMID: 19233257

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 (hERalpha 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 microM 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 hERalpha LBD than reported in the literature. The high-mass MALDI approach thus allows identifying high affinity EDCs in an efficient way.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP80466	4-tert-Amylphenol		80-46-6	Price

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