Cytochrome (CYP) P450 enzymes are a superfamily of heme-containing proteins found in all living organisms.  The main function of these enzymes during detoxification is to catalyze the oxidation of organic substances through monooxygenation reactions. CYP450 enzymes are also involved in the bioactivation of environmental procarcinogens, leading to the production of carcinogenic species.Previous studies have shown that a number of aromatic acetylenes and flavonoids act as inhibitors of P450 enzymes. We have previously shown that ethynylcoumarin derivatives, which have structural similarities to proparglyflavone analogs, can cause inactivation of certain P450 enzymes such as P450s 1A1, 1A2, 2B6, and 2B1.For this project, we have focused our efforts on the design and synthesis of a group of flavonoids with an ethynyl moiety at different locations on the ring system. These target compounds will be used in a structure-activity relationship study.

Ethynyl flavones as inhibitors of human cytochrome P450 enzymes

245th National Meeting (2013)

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