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Article

Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis

1
Department of Immunology, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
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Department of Structural Infection Biology, Center for Structural Systems Biology (CSSB), Helmholtz-Center for Infection Research (HZI), Notkestrasse 85, 22607 Hamburg, Germany
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Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
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Hagler Institute for Advanced Study at Texas A&M University, College Station, TX 7843, USA
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Max Planck Institute for Biophysical Chemistry, Am Faßberg 11, 37077 Göttingen, Germany
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Nuffield Department of Clinical Medicine, Ludwig Institute for Cancer Research, University of Oxford, Oxford OX3 7DQ, UK
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Faculty of Mathematics, Informatics and Natural Sciences, University of Hamburg, Rothenbaumchaussee 19, 20148 Hamburg, Germany
*
Authors to whom correspondence should be addressed.
Biosensors 2021, 11(3), 60; https://doi.org/10.3390/bios11030060
Received: 26 January 2021 / Revised: 16 February 2021 / Accepted: 19 February 2021 / Published: 24 February 2021
(This article belongs to the Section Biosensor and Bioelectronic Devices)
The aryl hydrocarbon receptor (AhR) is a highly conserved cellular sensor of a variety of environmental pollutants and dietary-, cell- and microbiota-derived metabolites with important roles in fundamental biological processes. Deregulation of the AhR pathway is implicated in several diseases, including autoimmune diseases and cancer, rendering AhR a promising target for drug development and host-directed therapy. The pharmacological intervention of AhR processes requires detailed information about the ligand binding properties to allow specific targeting of a particular signaling process without affecting the remaining. Here, we present a novel microscale thermophoresis-based approach to monitoring the binding of purified recombinant human AhR to its natural ligands in a cell-free system. This approach facilitates a precise identification and characterization of unknown AhR ligands and represents a screening strategy for the discovery of potential selective AhR modulators. View Full-Text
Keywords: AhR; recombinant expression; ligand binding; MST; high-throughput screening AhR; recombinant expression; ligand binding; MST; high-throughput screening
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MDPI and ACS Style

Stinn, A.; Furkert, J.; Kaufmann, S.H.E.; Moura-Alves, P.; Kolbe, M. Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis. Biosensors 2021, 11, 60. https://doi.org/10.3390/bios11030060

AMA Style

Stinn A, Furkert J, Kaufmann SHE, Moura-Alves P, Kolbe M. Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis. Biosensors. 2021; 11(3):60. https://doi.org/10.3390/bios11030060

Chicago/Turabian Style

Stinn, Anne, Jens Furkert, Stefan H.E. Kaufmann, Pedro Moura-Alves, and Michael Kolbe. 2021. "Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis" Biosensors 11, no. 3: 60. https://doi.org/10.3390/bios11030060

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