Ibogaine and the inhibition of acetylcholinesterase.
Journal of ethnopharmacology – February 15, 2012
Source: PubMed
Summary
Ibogaine, a compound explored for addiction treatment, was tested for its interaction with acetylcholinesterase, an enzyme vital for nerve function. Researchers confirmed ibogaine does inhibit this enzyme, but only at very high concentrations. This inhibition is physiologically negligible, indicating it doesn't explain ibogaine's observed effects in the body or pose a significant toxicological concern.
Abstract
Ibogaine is a psychoactive monoterpine indole alkaloid extracted from the root bark of Tabernanthe iboga Baill. that is used globally in medical and nonmedical settings to treat drug and alcohol addiction, and is of interest as an ethnopharmacological prototype for experimental investigation and pharmaceutical development. The question of whether ibogaine inhibits acetylcholinesterase (AChE) is of pharmacological and toxicological significance. AChE activity was evaluated utilizing reaction with Ellman's reagent with physostigmine as a control. Ibogaine inhibited AChE with an IC(50) of 520±40 μM. Ibogaine's inhibition of AChE is physiologically negligible, and does not appear to account for observations of functional effects in animals and humans that might otherwise suggest the possible involvement of pathways linked to muscarinic acetylcholine transmission.