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- MakaleYalnız künye2025Inhibition Effect of Cordyceps sinensis (C. sinensis) Mycelium on Some Metabolic Enzymes and Investigation of Antioxidant Properties
Balcı, Neslihan
Cordyceps sinensis (CS), a traditional medicinal fungus, is a rich source of bioactive metabolites with pharmacological potential. This study investigated the inhibitory effects of CS mycelium on human carbonic anhydrase isoenzymes I and II (hCA I and hCA II) and acetylcholinesterase (AChE), as well as its antioxidant properties. Enzyme inhibition was assessed using spectrophotometric methods, whereas antioxidant capacity was evaluated by DPPH, ABTS, CUPRAC, FRAP, and Fe3⁺-reducing assays. LC-MS/MS analysis identified key secondary metabolites, including apigenin, apigenin-7-glucoside, (+)-taxifolin, dihydrokaempferol, p-coumaric acid, salicylic acid, and L-theanine, with apigenin as the major constituent. CS strongly inhibited hCA I (IC50 = 1.11 µg/mL) and hCA II (IC50 = 1.77 µg/mL), exceeding the potency of acetazolamide, and also showed relevant AChE inhibition (IC50 = 8.00 µg/mL), comparable to tacrine. Antioxidant assays revealed moderate DPPH activity but strong ABTS and CUPRAC reducing capacities, indicating the structural contributions of flavonoids and phenolic acids. These findings suggest that CS possess dual bioactivity through enzyme inhibition and antioxidant effects, highlighting its therapeutic potential against neurodegenerative and oxidative stress–related diseases.
- MakaleAçık Erişim2019The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes
Topal, Meryem
Sesamol (1,3-benzodioxol-5-ol) is found in the oilseed product, sesame. In our study, the inhibitory effects of sesamol compound on acetylcholinesterase and α-glycosidase enzymes were evaluated. Another aim of this study was to compare the inhibitory effects of sesamol to acarbose for α-glycosidase enzyme and tacrine for acetylcholinesterase (AChE). Sesamol exhibited non-competitive inhibition for both metabolic enzymes. IC50 values for AChE and α-glycosidase enzymes were calculated as 86.63 nM and 99.00 nM, respectively. On the other hand, Ki values were calculated as 46.68 nM and 75.33 nM for AChE and α-glycosidase enzymes, respectively. According to the obtained results showed effective inhibition at low concentrations.