OATP2A1 Inhibitors

Chemical inhibitors of OATP2A1 include a variety of compounds that interact with the protein to prevent its normal function of transporting substrates across cell membranes. Chrysin, a flavonoid, binds to OATP2A1, which can lead to a conformational change or occupy the substrate site, thereby obstructing the access of physiological substrates. Similarly, Rifampicin, an antibiotic, competes with endogenous substrates for binding to OATP2A1, effectively inhibiting the protein's transport activity. Cyclosporin A, an immunosuppressant, also binds to OATP2A1, which prevents the transport of other molecules. This action is mirrored by Bromosulfophthalein and Sulfobromophthalein, both of which competitively inhibit OATP2A1 by occupying its substrate binding sites and thus block the translocation of natural substrates.

Naringin, a flavanone glycoside, interacts with OATP2A1 and disrupts its ability to engage with substrates, while Erythromycin, an antibiotic, behaves similarly by competitively binding to the substrate sites of OATP2A1. Troglitazone, an antidiabetic drug, can interact with the transporter, obstructing the passage of physiological substrates. Nicotinic Acid, also known as Vitamin B3, competes with endogenous substrates for the binding sites of OATP2A1, thus reducing the transport of these substrates. Ivermectin, an antiparasitic agent, can bind to and alter the transporter's conformation, which decreases its ability to move its natural substrates across the cell membrane. Atorvastatin, a cholesterol-lowering agent, specifically binds to OATP2A1 and inhibits the uptake of endogenous substrates. Lastly, Gossypol, a natural compound found in cotton plants, interacts with the substrate recognition sites of OATP2A1, which blocks the standard binding and transport of OATP2A1 substrates. Each of these chemicals acts on OATP2A1 by a direct interaction that leads to the inhibition of the protein's transport function without affecting the expression levels or the overall synthesis of the protein.