CYP2C19 Inhibitors

(R)-Omeprazole Sodium Salt exhibits notable interactions with CYP2C19, characterized by its chiral structure that influences stereospecificity in metabolic processes. The compound's polar functional groups enhance solubility and facilitate hydrogen bonding with the enzyme, promoting effective substrate binding. Its unique electronic properties can alter the enzyme's conformation, impacting reaction kinetics and influencing the overall metabolic pathway, resulting in varied biotransformation outcomes.

Isoniazid interacts with CYP2C19 through its unique hydrazine moiety, which can form covalent bonds with enzyme residues, leading to altered enzyme activity. The compound's electron-withdrawing characteristics enhance its reactivity, facilitating specific metabolic pathways. Additionally, its ability to form stable complexes with CYP2C19 can influence the enzyme's conformational dynamics, potentially affecting substrate specificity and the rate of metabolic reactions.

Fluconazole exhibits notable interactions with CYP2C19, primarily through its triazole ring, which can engage in hydrogen bonding with the enzyme's active site. This interaction alters the enzyme's conformation, impacting its catalytic efficiency. The compound's planar structure allows for π-π stacking with aromatic residues, enhancing binding affinity. Furthermore, its unique electron distribution influences the enzyme's redox state, potentially modulating metabolic pathways and reaction kinetics.

This can inhibit CYP2C19, affecting the metabolism of other drugs.

(S)-(+)-N-3-Benzylnirvanol demonstrates intriguing interactions with CYP2C19, characterized by its chiral center that influences stereoselectivity in binding. The presence of the benzylic group facilitates hydrophobic interactions, enhancing affinity for the enzyme's active site. Additionally, the compound's ability to form transient complexes may alter the enzyme's conformational dynamics, affecting substrate access and turnover rates. Its unique spatial arrangement contributes to distinct metabolic pathways, influencing overall enzymatic activity.

Stiripentol exhibits notable interactions with CYP2C19, primarily through its unique structural features that promote specific binding affinities. The compound's functional groups engage in hydrogen bonding and hydrophobic interactions, stabilizing enzyme-substrate complexes. This results in altered reaction kinetics, as Stiripentol can modulate the enzyme's catalytic efficiency. Its distinct stereochemistry further influences metabolic pathways, potentially leading to varied enzymatic outcomes.

Another antidepressant that inhibits CYP2C19 and can alter the metabolism of several drugs.

Omeprazole interacts with CYP2C19 through its distinctive sulfinyl and pyridine moieties, which facilitate selective binding to the enzyme's active site. This interaction alters the enzyme's conformation, impacting substrate accessibility and reaction rates. The compound's lipophilic characteristics enhance membrane permeability, influencing its distribution and metabolism. Additionally, its chiral centers contribute to stereoselective metabolism, resulting in diverse metabolic profiles.

Ticlopidine-d4 exhibits unique interactions with CYP2C19, characterized by its deuterated structure that alters isotopic effects during metabolic processes. This modification can influence reaction kinetics, potentially enhancing the stability of enzyme-substrate complexes. The compound's hydrophobic regions promote interactions with lipid membranes, affecting its bioavailability. Furthermore, its specific stereochemistry may lead to distinct metabolic pathways, resulting in varied enzymatic outcomes.

An over-the-counter agent in research for heartburn and ulcers that inhibits CYP2C19, leading to drug interactions.