Mindscape Collective is now The Consciousness Library. Same library, new name. You may need to sign in again. About the change
Skip to content

Mohamed O. Kamileen

4 papers in the library · 135 citations · publishing 2018-2025

Papers

Biosynthesis of an Anti-Addiction Agent from the Iboga Plant.

Journal of the American Chemical Society August 21, 2019 Scott C. Farrow, Mohamed O. Kamileen, Lorenzo Caputi et al. 69 citations

The plant-derived psychoactive compounds (-)-ibogaine and (-)-voacangine show promise for treating opioid addiction but are difficult to obtain from natural sources. Researchers achieved the complete biosynthesis of (-)-voacangine and its de-esterified form, which converts to (-)-ibogaine upon heating, enabling biocatalytic production. These compounds have the opposite enantiomeric configuration compared to other major alkaloids in their class, offering insight into enantioselective enzymatic formal Diels-Alder reactions.

Cytochrome P450 and O-methyltransferase catalyze the final steps in the biosynthesis of the anti-addictive alkaloid ibogaine from Tabernanthe iboga

Journal of Biological Chemistry July 20, 2018 Scott C. Farrow, Mohamed O. Kamileen, Jessica Meades et al. 55 citations

Two enzymes that complete the biosynthesis of ibogaine, an alkaloid from the iboga plant used traditionally in equatorial Africa and known for alleviating opioid withdrawal, have been identified. Using the first iboga transcriptome generated by next-generation sequencing and homology-guided gene discovery, the researchers found ibogamine 10-hydroxylase (I10H) and noribogaine-10-O-methyltransferase (N10OMT). When expressed in yeast or bacteria and incubated with precursor compounds, both enzymes performed the predicted chemical steps, confirmed by HPLC–MS analysis. Their transcripts were abundant in ibogaine-producing plant tissues. These discoveries and the publicly available transcriptome may help stabilize the ibogaine supply through synthetic biology and support its development as an addiction treatment.

Oxidative Rearrangements of the Alkaloid Intermediate Geissoschizine.

Angewandte Chemie (International ed. in English) June 10, 2025 Mohamed O. Kamileen, Benke Hong, Klaus Gase et al. 11 citations

Three cytochrome P450 enzymes in the medicinal plant Catharanthus roseus transform the central intermediate 19E-geissoschizine into four distinct alkaloid scaffolds: strychnos, sarpagan, akuammiline-type, and mavacurane-type alkaloids. In vitro enzymatic assays and gene silencing demonstrate this oxidative rearrangement. Mutational analysis shows that minimal changes to the active sites of these similar enzymes modulate product specificity. Substrate reactivity and enzyme mutations work synergistically to generate chemical diversity in monoterpene indole alkaloid biosynthesis.

Biosynthesis of an Anti-Addiction Agent from the Iboga Plant

bioRxiv Preprint Server May 26, 2019 Scott C. Farrow, Mohamed O. Kamileen, Lorenzo Caputi et al. preprint

The psychoactive plant compounds (−)-ibogaine and (−)-voacangine show promise for treating opioid addiction but are difficult to obtain from natural sources. Researchers report the complete biosynthesis of (−)-voacangine and its de-esterified form, which can be converted to (−)-ibogaine by heating. This discovery enables production of these compounds through synthetic biology. Notably, these compounds have the opposite enantiomeric configuration compared to other major alkaloids in their class. The identification of the biosynthetic enzymes reveals how nature produces both enantiomeric series of this medically important alkaloid scaffold using closely related enzymes, including those that catalyze enantioselective formal Diels-Alder reactions.