期刊
BIOSENSORS-BASEL
卷 11, 期 3, 页码 -出版社
MDPI
DOI: 10.3390/bios11030060
关键词
AhR; recombinant expression; ligand binding; MST; high-throughput screening
资金
- Max Planck Society
- International Max Planck Research School for Infectious Diseases and Immunology (IMPRS-IDI)
- iNEXT - Horizon 2020 programme of the European Union [653706]
The AhR is a highly conserved cellular sensor with important roles in various diseases, making it a promising target for drug development. Understanding the ligand binding properties is crucial for precise pharmacological interventions and targeted therapies.
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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