The aryl hydrocarbon receptor (AhR) is a cellular sensor that interacts with a plethora of molecules in the environment to mediate a response. For example, the AhR senses molecules produced by bacteria infecting the body and influences the body’s immune response.
The AhR is fundamental in several biological processes and its deregulation is associated with disease, including cancer and autoimmune diseases. For this reason, the AhR is an attractive target for therapeutic drugs. However, with so many different molecules interacting with this receptor, it is important to understand the binding properties of all these interactions to allow specific pharmacological targeting of one without affecting the other interactions.
Dr Pedro Moura Alves, working with colleagues from Germany, has developed a new method for identifying and characterising the human AhR’s interactions. Published in the journal Biosensors, their approach uses a technique called microscale thermophoresis, which overcomes many of the disadvantages with existing technologies to allow a faster and more robust investigation of these binding events. Key to their innovation is the development of a new system for generating larger amounts of stable, purified human AhR protein by fusing the AhR to a protein tag and co-expressing the AhR in complex with its interacting partner ARNT.
This new method will not only allow the further investigation and discovery of AhR interactors for biomedical research but also has the potential to underpin future screens for drugs that can be used to treat AhR-associated diseases.