CYP2C9 Inhibitors

Valproic acid sodium salt demonstrates notable interactions with CYP2C9, primarily through hydrogen bonding and ionic interactions that stabilize its binding to the enzyme. This compound's unique stereochemistry facilitates specific conformational changes in CYP2C9, impacting its metabolic activity. The kinetics of the reaction are influenced by the compound's solubility and polarity, which affect diffusion rates and substrate accessibility, ultimately modulating the enzyme's overall function.

Competitively inhibits CYP2C9, reducing the metabolism of drugs that are CYP2C9 substrates.

Apigenin exhibits a distinctive role as a modulator of CYP2C9 activity, characterized by its ability to form π-π stacking interactions with aromatic residues within the enzyme's active site. This interaction alters the enzyme's conformation, enhancing substrate affinity. Additionally, apigenin's lipophilicity influences its partitioning in biological membranes, affecting the enzyme's accessibility to various substrates and potentially altering metabolic pathways. Its unique structural features contribute to the modulation of CYP2C9's catalytic efficiency.

(R)-Omeprazole Sodium Salt acts as a selective inhibitor of CYP2C9, showcasing unique interactions with the enzyme's heme group. Its chiral structure facilitates specific binding, leading to altered electron transfer dynamics. This compound's hydrophobic regions enhance its interaction with lipid membranes, influencing the enzyme's localization and substrate interaction. The distinct stereochemistry of (R)-Omeprazole Sodium Salt plays a crucial role in modulating CYP2C9's metabolic pathways and reaction kinetics.

Warfarin Sodium is a potent modulator of CYP2C9, exhibiting unique binding characteristics that influence its metabolic profile. Its planar structure allows for effective π-π stacking interactions with the enzyme, enhancing substrate specificity. The compound's electron-withdrawing groups facilitate resonance stabilization, impacting reaction kinetics. Additionally, Warfarin's lipophilicity promotes membrane permeability, potentially altering enzyme localization and activity in various biological contexts.

Myricetin acts as a selective inhibitor of CYP2C9, showcasing distinct molecular interactions that modulate enzymatic activity. Its flavonoid structure enables hydrogen bonding and hydrophobic interactions with the enzyme's active site, influencing substrate affinity. The compound's antioxidant properties may also affect redox states within the enzyme, altering its catalytic efficiency. Furthermore, Myricetin's diverse conformational flexibility allows for dynamic binding, potentially impacting metabolic pathways.

Fluconazole functions as a potent inhibitor of CYP2C9, characterized by its unique ability to form stable complexes with the enzyme. Its triazole ring facilitates specific interactions with heme iron, disrupting the enzyme's catalytic cycle. This compound exhibits a distinct binding affinity, which can alter the kinetics of substrate metabolism. Additionally, Fluconazole's solubility properties enhance its interaction dynamics, influencing the overall metabolic landscape.

Benzbromarone acts as a selective inhibitor of CYP2C9, distinguished by its unique structural features that promote strong interactions with the enzyme's active site. Its bromobenzene moiety enhances hydrophobic interactions, while the presence of a carbonyl group facilitates hydrogen bonding. This compound exhibits a notable impact on the enzyme's conformational dynamics, leading to altered substrate specificity and reaction rates. Its lipophilic nature further influences its metabolic pathways, contributing to its distinct pharmacokinetic profile.

Binds non-selectively to various CYP enzymes, including CYP2C9, and inhibits their function.

Baicalein is a flavonoid that exhibits selective inhibition of CYP2C9 through specific interactions with the enzyme's active site. Its unique hydroxyl groups enhance hydrogen bonding, while the aromatic rings contribute to π-π stacking interactions, stabilizing the enzyme-inhibitor complex. This compound influences the enzyme's kinetic parameters, altering substrate affinity and turnover rates. Additionally, its solubility characteristics may affect its distribution and interaction with other metabolic pathways.