Document Type

Oral Presentation

Location

Oxford Conference Center

Event Website

https://oxfordicsb.org/

Start Date

23-4-2026 11:10 AM

End Date

23-4-2026 11:30 AM

Description

The Amaryllidaceae family is well known for its rich diversity of alkaloids, including lycorine- and galantamine-type structures with potent cholinesterase inhibitory properties. In this study, we investigated the phytochemical composition and cholinesterase inhibitory activity of alkaloids isolated from Narcissus poeticus L., a species native to the botanically rich Auvergne region of France. Phytochemical analysis and bioguided fractionation of bulb extracts led to the identification of three known alkaloids, pseudolycorine, norgalantamine, and 2-O-(3’-hydroxybutanoyl)-lycorine, as well as a newly characterized tetrahydroquinoline derivative, poeticine A. The inhibitory activities of these compounds against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) were assessed using both a standard 96-well microplate assay and a HPTLC bioautography method. HPTLC bioautography enabled direct visualization of enzyme inhibition on chromatographic plates using an enzyme-selective fluorescent probe and provided semi-quantitative IC₅₀. Poeticine A displayed moderate inhibition, with IC₅₀ values of 23 μM for AChE and 118 μM for BChE whereas norgalantamine exhibited strong inhibition, with IC₅₀ values of 0.47 μM for AChE and 21 μM for BChE. These results were in agreement with the observation using HPTLC. These results highlight the relevance of Narcissus poeticus alkaloids as cholinesterase inhibitors and demonstrate the reliability of HPTLC bioautography as a complementary tool for rapid activity-guided screening and fractionation.

This work has been financed by Region Auvergne Rhône Alpes, by ISITE program.

Comments

Maël Gainche is an Associate Professor specializing in natural products chemistry. He graduated as a chemical engineer from SIGMA Clermont in 2017 and obtained the same year a Master’s degree in Organic Synthesis and Biocatalysis from the Clermont Auvergne University. He completed his PhD in Phytochemistry in the same University in 2020, where his research focused on the characterization of bioactive metabolites from local natural sources. Following his doctoral work, he served as a Teaching and Research Assistant (ATER) at the Strasbourg University Faculty of Pharmacy from 2020 to 2021 in the pharmacognosy department, contributing to research on natural antibacterial compounds from plants and fungus. Since 2021, Maël Gainche has been a Contract Post-Doc in natural products chemistry within the Clermont Auvergne INP group. His current research focus on phytochemistry and the development of innovative HPTLC-based bioautography methods to explore the biological potential of plant and fungal metabolites. He is committed to advancing analytical tools to support natural products research and to improving the integration of chemical profiling and bioactivity-guided analysis. He was also elected as president of the newly Francophone Chapter of the HPTLC Association in June 2025.

Publication Date

April 2026

Accessibility Status

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Apr 23rd, 11:10 AM Apr 23rd, 11:30 AM

Alkaloid profiling of Narcissus poeticus L. bulbs and their inhibitory activity of cholinesterases

Oxford Conference Center

The Amaryllidaceae family is well known for its rich diversity of alkaloids, including lycorine- and galantamine-type structures with potent cholinesterase inhibitory properties. In this study, we investigated the phytochemical composition and cholinesterase inhibitory activity of alkaloids isolated from Narcissus poeticus L., a species native to the botanically rich Auvergne region of France. Phytochemical analysis and bioguided fractionation of bulb extracts led to the identification of three known alkaloids, pseudolycorine, norgalantamine, and 2-O-(3’-hydroxybutanoyl)-lycorine, as well as a newly characterized tetrahydroquinoline derivative, poeticine A. The inhibitory activities of these compounds against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) were assessed using both a standard 96-well microplate assay and a HPTLC bioautography method. HPTLC bioautography enabled direct visualization of enzyme inhibition on chromatographic plates using an enzyme-selective fluorescent probe and provided semi-quantitative IC₅₀. Poeticine A displayed moderate inhibition, with IC₅₀ values of 23 μM for AChE and 118 μM for BChE whereas norgalantamine exhibited strong inhibition, with IC₅₀ values of 0.47 μM for AChE and 21 μM for BChE. These results were in agreement with the observation using HPTLC. These results highlight the relevance of Narcissus poeticus alkaloids as cholinesterase inhibitors and demonstrate the reliability of HPTLC bioautography as a complementary tool for rapid activity-guided screening and fractionation.

This work has been financed by Region Auvergne Rhône Alpes, by ISITE program.

https://egrove.olemiss.edu/icsb/2026_ICSB/Schedule/33