T2R1 Inhibitors

Chemical inhibitors of T2R1 include a range of compounds that interact with the protein's receptor sites to prevent the binding and recognition of bitter compounds. Propylthiouracil can inhibit T2R1 through competitive antagonism, where it binds to receptor sites responsive to thiourea compounds. This binding prevents the usual activation of T2R1 by its characteristic ligands. Phenylthiocarbamide operates on a comparable mechanism, acting as a competitive inhibitor due to its structural likeness to T2R1's natural ligands, thus preventing receptor activation. Probenecid also inhibits T2R1 by interacting with specific recognition sulfonamide sites on the receptor. This interaction obstructs the binding of other bitter tastants. Acesulfame Potassium, a sweetener, can indirectly inhibit T2R1 by binding to the sweet taste receptor sites, which reduces T2R1's ability to detect and respond to bitter compounds. Capsazepine, meanwhile, can inhibit T2R1 by competing with molecules like capsaicin for binding spots on the receptor, blocking the detection of certain bitter tastants. Lastly, Naringin and Gymnemic Acid bind to T2R1's bitter and sweet taste sites, respectively. Naringin does so due to its inherent bitterness, while Gymnemic Acid's sweet receptor site occupation indirectly leads to a decrease in T2R1's interaction with bitter molecules.