Article 2025 · 1 citations

Naringenin, Helichrysin A: Characterization, isolation, molecular docking studies and enzyme inhibitory profiles for carbonic anhydrase, acetylcholinesterase, and<i> α</i>-glycosidase

Guven, Leyla, Erturk, Adem, Gulcin, Ilhami

Abstract

In the current study, Naringenin and Helichrysin A purified and characterized from Helichrysum plicatum subsp. pseudoplicatum. The inhibitory effects of isolated Naringenin and Helichrysin A were tested against human carbonic anhydrase I (hCA I) and II isoenzymes (hCA II), alpha-glycosidase (alpha-gly) and acetylcholinesterase (AChE). Naringenin and Helichrysin A's Ki values were found to respectively 51.99 +/- 2.78 and 75.75 +/- 13.66 nM against hCA I, 36.16 +/- 2.02 and 96.81 +/- 12.46 nM against hCA II, 0.74 +/- 0.04 and 1.27 +/- 0.16 nM against AChE, 8.34 +/- 1.61 and 9.58 +/- 1.90 nM against alpha-gly. As a result, the inhibitory effects of the isolated compounds against each metabolic enzyme examined were demonstrated. Moreover, in the molecular docking study of Helichrysin A, it was observed that the three enzymes had the lowest binding free energy and maximum binding affinity. Helichrysin A and Naringenin show promise as treatments for conditions including epilepsy, leukemia, diabetes mellitus, glaucoma, and Alzheimer's disease.

Keywords

Enzyme inhibition Helichrysin A Molecular docking Naringenin ITALICUM FLOWER

WoS Categories

Pharmacology & Pharmacy

Sustainable Development Goals

Good Health and Well-being

Citation

Journal: JOURNAL OF RESEARCH IN PHARMACY
Year: 2025
Volume: 29
Issue: 3
Pages: 1198-1208
ISSN: 2630-6344
DOI: 10.12991/jrespharm.1694383
WoS UID: WOS:001538397700014

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