posted on 2019-08-02, 12:03authored byFrancesca Toselli, Marlene Fredenwall, Peder Svensson, Xue-Qing Li, Anders Johansson, Lars Weidolf, Martin A. Hayes
Oxetane-containing
ring systems are increasingly used in medicinal
chemistry programs to modulate druglike properties. We have shown
previously that oxetanes are hydrolyzed to diols by human microsomal
epoxide hydrolase (mEH). Mapping the enzymes that contribute to drug
metabolism is important since an exaggerated dependence on one specific
isoenzyme increases the risk of drug–drug interactions with
co-administered drugs. Herein, we illustrate that mEH-catalyzed hydrolysis
is an important metabolic pathway for a set of more structurally diverse
oxetanes and the degree of hydrolysis is modulated by minor structural
modifications. A homology model based on the Bombyx
mori EH crystal structure was used to rationalize
substrate binding. This study shows that oxetanes can be used as drug
design elements for directing metabolic clearance via mEH, thus potentially
decreasing the dependence on cytochromes P450. Metabolism by mEH should
be assessed early in the design process to understand the complete
metabolic fate of oxetane-containing compounds, and further study
is required to allow accurate pharmacokinetic predictions of its substrates.