Determinación de la actividad inhibitoria de la fracción alcaloidal de Phaedranassa cuencana, sobre las enzimas acetilcolinesterasa y butirilcolinesterasa.

Abstract

The objective of this research was to determine the inhibitory activity on the enzymes acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE), by the alkaloidal fraction of Phaedranassa cuencana (Amaryllidaceae). The alkaloidal extract of the dry bulb of P. cuencana was obtained from a maceration with methanol, and the subsequent use of organic solvents (ethyl ether and ethyl acetate), in addition to pH changes, reaching a yield of 0.137%. Subsequently, the alkaloids were separated and identified by gas chromatography coupled with mass spectrometry (GC-MS). GC-MS showed a total of 7 alkaloids, including lycorine with 56.68%, followed by galantamine 18.90%, and 7.25% sanguinine. And in smaller abundance lycorine and galantamine-type alkaloids. The inhibitory activity of AChE and BuChE was evaluated through Ellman’s method with modifications using as the reference compound the alkaloid galantamine. Enzymatic inhibition of P. cuencana was determined presenting IC50 values 1.12 ±0.05 µg/mL for AChE, result very close to the reference compound galantamine, which has an IC50= 0.3 ±0.02 µg/mL. On the other hand, the inhibition that was presented for BuChE, was IC50= 21.53 ±1.64 µg/mL, observing that it presents lower activity than galantamine IC50= 5.00 ±0.36 µg/mL. It was known to note with the results that, although its inhibitory activity is lower that the reference compound, it shows a high inhibitory activity of both acetylcholinesterase and Butyrylcholinesterase. P. cuencana according to the results are exposed, is considered a plant species with high potential for the treatment of Alzheimer’s disease, therefore it is recommended phytochemical, pharmacological, and toxicological studies of it.