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

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), α-glycosidase (α-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 α-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.