Olfr70 Inhibitors

Chemical inhibitors of Olfr70 can employ a variety of mechanisms to prevent the normal function of the protein. Benzaldehyde and cinnamaldehyde act as competitive antagonists, which means they bind to the receptor sites where natural activators would, without triggering the cascades that lead to cellular responses. By occupying these sites, they block the activators from binding and thus inhibit the function of Olfr70. Similarly, eugenol and citronellal can also inhibit Olfr70 by binding to its receptor sites, acting as a barrier to activation by the natural ligands. These substances essentially mimic the shape and electronic properties of the natural ligand without initiating the same response, leading to a decrease in Olfr70 activity.

Further inhibitory effects can be seen with chemicals like methyl anthranilate and alpha-terpineol, which serve as inverse agonists and competitive inhibitors, respectively. Methyl anthranilate decreases the activity of Olfr70 by binding to the receptor and stabilizing it in an inactive form, while alpha-terpineol competes with activators for the binding site, therefore inhibiting the receptor's activation. Thiolane and menthol can enact allosteric inhibition, which involves binding to a different site on Olfr70 than the active site, causing a conformational change to the protein structure that results in decreased receptor activity. Lastly, zinc gluconate and copper sulfate interact with metal ion binding sites on Olfr70 that are crucial for the protein's conformation and function. By binding to these sites, they can inhibit the activation of the receptor, effectively reducing its ability to respond to its natural ligands. Capsaicin and allyl isothiocyanate, on the other hand, bind to the ligand-binding domain of Olfr70, with allyl isothiocyanate forming a covalent bond that leads to irreversible inhibition, providing robust blockage of receptor function.