Article 2025 · 1 atıf

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

Özet

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.

Anahtar Kelimeler

Enzyme inhibition Helichrysin A Molecular docking Naringenin ITALICUM FLOWER

WoS Kategorileri

Pharmacology & Pharmacy

Sürdürülebilir Kalkınma Amaçları

Sağlık ve Kaliteli Yaşam

Künye

Dergi: JOURNAL OF RESEARCH IN PHARMACY
Yıl: 2025
Cilt: 29
Sayı: 3
Sayfa: 1198-1208
ISSN: 2630-6344
DOI: 10.12991/jrespharm.1694383
WoS UID: WOS:001538397700014

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