Bromo-dragonfly, a potent and long-acting hallucinogen linked to severe vasoconstriction and fatal intoxications, was not metabolized in human liver microsomes, cytosol, or recombinant enzyme systems, unlike its analogue 2C-B-fly, which underwent monohydroxylation and N-acetylation via CYP2D6 and MAO-A. Bromo-dragonfly competitively inhibited monoamine oxidase A (MAO-A) with a Ki of 0.352 μM, and its IC50 suggested clinically relevant MAO-A inhibition, though further data are needed to assess its impact on serotonin levels in the body. Protein binding and pharmacokinetic parameters were also investigated.
The NBOMe compounds, potent serotonin 5-HT2A receptor agonists used recreationally for their hallucinogenic effects, are metabolized primarily by specific cytochrome P450 enzymes. For 25I-NBOMe, CYP3A4 is the major enzyme involved; for 25I-NBOH, CYP2D6 is the major enzyme. 25I-NBOH also undergoes direct glucuronidation, which may reduce the impact of CYP2D6 genetic variation. The intrinsic clearance values were 70.1 mL/min/kg for 25I-NBOMe and 118.7 mL/min/kg for 25I-NBOH. Users of 25I-NBOMe may face drug-drug interactions if taken with a strong CYP3A4 inhibitor. Metabolites included hydroxylation, O-demethylation, N-dealkylation, and dehydrogenation products.