Researchers from the Laboratory of Protein Structure at the International Institute of Molecular and Cell Biology in Warsaw, led by Prof. Marcin Nowotny, used the KRIOS cryoelectron microscope located at the SOLARIS National Synchrotron Radiation Centre to study the human TRPM8 protein.
The structure they obtained will enable a better understanding of the binding mechanism of small-molecule compounds affecting the activity of this ion channel. It will facilitate the design of new small-molecule compounds that can be used as therapeutics to treat numerous diseases associated with TRPM8 protein, such as neuropathic pain, irritable bowel syndrome, oropharyngeal dysphagia, chronic cough, and hypertension. As an example, in collaboration with scientists from Italy led by Dr. Carmine Talarico of Dompé Farmaceutici SpA, they have performed modeling of the binding of icilin, a small-molecule compound showing 200 times stronger TRPM8 channel activation than menthol.
Read more on SOLARIS website
Image: Structure of human cold receptor TRPM8
Credit: Mariusz Czarnocki-Cieciura