The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

Natural products from food and plant sources have been used for medicinal usage for ages. Also, natural products with therapeutic significance are compounds derived from animals, plants, or any microorganism. In this study, chrysin, carvacrol, hesperidin, zingerone, and naringin as natural phenols s...

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Bibliographic Details
Published in:Journal of biochemical and molecular toxicology 2017-12, Vol.31 (12), p.n/a
Main Authors: Taslimi, Parham, Caglayan, Cuneyt, Gulcin, İlhami
Format: Article
Language:English
Subjects:
acetylcholinesterase
Acetylcholinesterase - chemistry
alpha-Glucosidases - chemistry
Anticonvulsants - chemistry
butyrylcholinesterase
Butyrylcholinesterase - chemistry
carbonic anhydrase
Carbonic Anhydrase Inhibitors - chemistry
Carbonic Anhydrases - chemistry
Cholinesterase Inhibitors - chemistry
Enzyme Assays
Humans
Hypoglycemic Agents - chemistry
Phenolic compounds
α‐glycosidase
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Summary:Natural products from food and plant sources have been used for medicinal usage for ages. Also, natural products with therapeutic significance are compounds derived from animals, plants, or any microorganism. In this study, chrysin, carvacrol, hesperidin, zingerone, and naringin as natural phenols showed excellent inhibitory effects against human (h) carbonic anhydrase (CA) isoforms I and II (hCA I and II), α‐glucosidase (α‐Gly), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). These phenolic compounds were tested for the inhibition of α‐glycosidase, hCA I, hCA II, AChE, and BChE enzymes and demonstrated efficient inhibition profiles with Ki values in the range of 3.70 ± 0.92–79.66 ± 20.81 nM against hCA I, 2.98 ± 0.33–84.88 ± 40.32 nM against hCA II, 4.93 ± 2.01–593.60 ± 134.74 nM against α‐Gly, 0.52 ± 0.18–46.80 ± 17.15 nM against AChE, and 1.25 ± 0.22–32.08 ± 2.68 against BChE.
ISSN:1095-6670
1099-0461
DOI:10.1002/jbt.21995