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In vitro and pharmacophore insights into CYP3A enzymes.

The cytochrome P450 3A ( CYP3A) enzymes have a major role in the metabolism of drugs in humans. Their wide substrate specificity and induction by a vast array of structurally diverse compounds presents the possibility of metabolic drug-drug interactions. Understanding the enzymes themselves is crucial. Over the past decade, this has occurred mostly with in vitro studies, although more recent approaches incorporate computational models to predict CYP inhibition and substrate potential. The three-dimensional displacement, or pharmacophore, of chemical features in space that are derived from inhibition data have produced pharmacophores for CYP3A4, CYP3A5 and CYP3A7, and provide new insights into ligand binding for each enzyme.[1]

References

  1. In vitro and pharmacophore insights into CYP3A enzymes. Ekins, S., Stresser, D.M., Williams, J.A. Trends Pharmacol. Sci. (2003) [Pubmed]
 
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