date: 2021-03-04T05:36:35Z
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pdf:docinfo:title: Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis
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Keywords: AhR; recombinant expression; ligand binding; MST; high-throughput screening
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subject: 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.
dc:creator: Anne Stinn, Jens Furkert, Stefan H. E. Kaufmann, Pedro Moura-Alves and Michael Kolbe
dcterms:created: 2021-03-04T02:56:43Z
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title: Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis
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pdf:docinfo:keywords: AhR; recombinant expression; ligand binding; MST; high-throughput screening
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dc:title: Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis
modified: 2021-03-04T05:36:35Z
cp:subject: 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.
pdf:docinfo:subject: 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.
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pdf:docinfo:creator: Anne Stinn, Jens Furkert, Stefan H. E. Kaufmann, Pedro Moura-Alves and Michael Kolbe
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creator: Anne Stinn, Jens Furkert, Stefan H. E. Kaufmann, Pedro Moura-Alves and Michael Kolbe
meta:author: Anne Stinn, Jens Furkert, Stefan H. E. Kaufmann, Pedro Moura-Alves and Michael Kolbe
dc:subject: AhR; recombinant expression; ligand binding; MST; high-throughput screening
meta:creation-date: 2021-03-04T02:56:43Z
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meta:keyword: AhR; recombinant expression; ligand binding; MST; high-throughput screening
Author: Anne Stinn, Jens Furkert, Stefan H. E. Kaufmann, Pedro Moura-Alves and Michael Kolbe
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