CYP2D26 Inhibitors

Chemical inhibitors of CYP2D26 include a range of compounds that interact with the enzyme to impede its metabolic function. Quinidine, a known CYP2D26 inhibitor, competitively binds to the active site of the enzyme, which is crucial for the metabolism of various substrates, thus preventing those substrates from being metabolized. Similarly, fluoxetine and paroxetine exhibit their inhibitory effects by occupying the active site of CYP2D26, which leads to a reduction in the enzyme's activity. This competitive inhibition is a common mechanism by which these drugs block the metabolic capabilities of CYP2D26, ensuring that the substrates normally metabolized by CYP2D26 are left unprocessed.

Other inhibitors, such as ajmalicine and amiodarone, directly bind to CYP2D26, which results in a blockade of the enzyme's active site. This binding precludes the access and processing of the enzyme's natural substrates, effectively inhibiting the function of CYP2D26. Haloperidol and ritonavir also adhere to this mode of inhibition by directly interacting with CYP2D26's active site, which diminishes the enzyme's ability to carry out its normal metabolic reactions. Compounds like diphenhydramine, chlorpheniramine, bupropion, sertraline, and methadone are additional examples of chemicals that inhibit CYP2D26 through direct binding to the active site. This direct interaction hampers the conversion of substrates by CYP2D26, showcasing a consistent strategy among various chemical inhibitors to reduce the metabolic throughput of this enzyme. Each of these chemicals binds in a manner that competes with the natural substrates of CYP2D26, ensuring that the enzyme's activity is hindered and the substrates remain unaltered.