CYP3A4 Substrates
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Vinblastine Sulfate | 143-67-9 | sc-201447 sc-201447A sc-201447B sc-201447C | 10 mg 50 mg 100 mg 1 g | $109.00 $412.00 $561.00 $2244.00 | 9 | |
Vinblastine Sulfate exhibits notable interactions with CYP3A4, primarily through allosteric modulation rather than direct competition. Its unique polycyclic structure allows for specific π-π stacking and van der Waals forces, influencing enzyme conformation and activity. The compound's kinetic behavior is characterized by a multi-step binding process, which alters the enzyme's substrate specificity and metabolic pathways, shedding light on intricate regulatory mechanisms within the cytochrome P450 system. | ||||||
Verapamil hydrochloride | 152-11-4 | sc-3590 sc-3590A sc-3590B | 100 mg 1 g 5 g | $51.00 $77.00 $153.00 | 22 | |
Verapamil hydrochloride engages with CYP3A4 through a distinct mechanism involving conformational changes rather than simple inhibition. Its unique aromatic and aliphatic regions facilitate hydrophobic interactions and hydrogen bonding, enhancing binding affinity. The compound's kinetic profile reveals a complex interaction pattern, where it modulates enzyme activity by altering the active site dynamics, thereby influencing the metabolic fate of various substrates within the cytochrome P450 family. | ||||||
Vincristine Sulfate | 2068-78-2 | sc-201434 sc-201434A | 5 mg 25 mg | $122.00 $342.00 | 15 | |
Vincristine sulfate exhibits a multifaceted interaction with CYP3A4, characterized by its ability to form stable complexes through π-π stacking and electrostatic interactions. This compound influences the enzyme's catalytic efficiency by altering substrate accessibility and promoting conformational shifts in the active site. Its unique structural features enable selective modulation of CYP3A4 activity, impacting the metabolic pathways of co-administered compounds and contributing to intricate drug-drug interaction profiles. | ||||||
Clarithromycin-N-methyl-d3 | 959119-22-3 | sc-217926 | 5 mg | $379.00 | ||
Clarithromycin-N-methyl-d3 exhibits distinctive interactions with CYP3A4, characterized by its isotopic labeling which enhances the study of metabolic pathways. The compound's unique deuterated structure may influence isotope effects during enzymatic reactions, providing insights into reaction mechanisms. Its ability to modulate enzyme activity through specific binding sites can lead to variations in substrate turnover rates, offering a nuanced understanding of metabolic regulation in biochemical systems. | ||||||
Clarithromycin | 81103-11-9 | sc-205634 sc-205634A | 100 mg 250 mg | $77.00 $122.00 | 1 | |
Clarithromycin interacts with CYP3A4 through a combination of hydrophobic and hydrogen bonding interactions, leading to conformational changes in the enzyme. This compound can act as a competitive inhibitor, affecting the metabolism of various substrates by altering their binding affinity. Its unique stereochemistry allows for selective engagement with the enzyme, influencing reaction kinetics and potentially leading to altered pharmacokinetic profiles of co-administered substances. | ||||||
(R)-(+)-Warfarin | 5543-58-8 | sc-255498 | 5 mg | $627.00 | ||
(R)-(+)-Warfarin demonstrates notable interactions with CYP3A4, primarily through its stereochemistry, which influences binding affinity and selectivity. This enantiomer's unique conformation allows for specific hydrogen bonding and hydrophobic interactions within the enzyme's active site, affecting its metabolic stability. The compound's kinetic profile reveals a complex interplay of competitive inhibition and allosteric modulation, shedding light on the intricacies of drug metabolism and enzyme dynamics. | ||||||