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• MakaleYalnız künye2025Scopus SJRQ3/r/gumushane/13533
  Inhibition 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.

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  İncele
• MakaleAçık Erişim2025Scopus SJRQ1/r/gumushane/12426
  Evaluation of Antioxidant and Enzyme Inhibition Properties of Siran Propolis: Correlations With Phenolic Content Determined by LC–MS/MS

  Balci, Neslihan; Aslan, Kubra; Erturk, Adem; Gulcin, Ilhami

  This study evaluates the antioxidant activity, enzyme inhibition potential, and phenolic composition of ethanolic Siran propolis extract. Antioxidant capacity was measured using reducing power (CUPRAC, FRAP, and Fe3+-reducing) and radical scavenging (DPPH·, ABTS·+, and DMPD·+) assays. The extract showed strong reducing ability, surpassing standard antioxidants in CUPRAC and FRAP assays, correlating with high ferulic acid (40.40 mg/g) and p-coumaric acid (88.60 mg/g) levels identified by LC–MS/MS. While it demonstrated notable DPPH· scavenging (IC50: 30.14 μg/mL), ABTS·+ activity was weaker (IC50: 272.44 μg/mL). Enzyme inhibition assays indicated effective inhibition of α-glycosidase, AChE (IC50: 2.15 μg/mL), hCA I, and hCA II. Notably, AChE inhibition was stronger than the standard tacrine inhibitor (IC50: 8.82 μg/mL), suggesting neuroprotective potential. The observed bioactivities are attributed to synergistic effects of phenolic acids and flavonoids, including quercetin, luteolin, taxifolin, and resveratrol. These findings highlight Siran propolis as a promising natural antioxidant and enzyme inhibitor source with potential therapeutic applications and food formulations.

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  AtıfScopus12·WoS12·OpenAlex11

  İncele
• MakaleAçık Erişim2025Scopus SJRQ2/r/gumushane/12209
  Novel Sulfonylhydrazones With Sulfonate Ester Framework: Promising Dual Inhibitors of AChE and hCAs

  Öztürk, Cansu; Balci, Neslihan; Aslan, Osman Nuri; Kalay, Erbay

  Alzheimer's disease (AD) is a progressive neurodegenerative disorder that affects millions of individuals worldwide. Treatment strategies for AD vary depending on cognitive and behavioral symptoms, with cholinergic replacement therapy using acetylcholinesterase (AChE) inhibitors being one of the primary approaches. Recent studies have also identified human carbonic anhydrases (hCAs) as significant therapeutic targets for AD, offering new opportunities for the development of innovative treatments. Carbonic anhydrase inhibitors have been shown to prevent early mitochondrial damage and inhibit H2O2 production, thereby reducing amyloid plaque formation. Building on the promising potential of hydrazones particularly sulfonyl hydrazones as anticholinesterase agents, we synthesized 12 novel chlorine-substituted sulfonyl hydrazone compounds containing aryl sulfonate ester groups. These compounds were evaluated for their inhibitory effects on AChE, hCA I, and hCA II enzymes. The synthesized compounds exhibited low nanomolar inhibitory activity, with Ki values ranging from 9.58 ± 2.22 to 104.04 ± 23.82 nM for AChE, 9.12 ± 2.21 to 477.63 ± 218.52 nM for hCA I, and 17.54 ± 7.74 to 564.62 ± 213.98 nM for hCA II. Notably, compound 6 showed strong inhibitory activity against hCA I (Ki = 9.12 ± 2.21 nM; acetazolamide (AZA) = 26.54 ± 3.11 nM) and hCA II (Ki = 17.54 ± 7.74 nM; AZA = 21.73 ± 2.42 nM), whereas compound 4 exhibited superior AChE inhibition (Ki = 9.58 ± 2.22 nM; TAC = 23.12 ± 2.05 nM). The chemical structures of the synthesized compounds were characterized using advanced spectroscopic techniques, including FT-IR, 1H-NMR, and 13C-NMR spectroscopy.

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  AtıfScopus12·WoS11·OpenAlex9

  İncele
• MakaleAçık Erişim2025/r/gumushane/11585
  Inhibition Effect of Diosmin Flavanoid on Some Metabolic Enzymes and Investigation of Antioxidant Properties

  Balci, Neslihan

  Diosmin is a natural flavonoid obtained by dehydrating flavanone glycoside hesperidin. This study evaluated the inhibition effects of diosmin flavonoid on human carbonic anhydrases (hCA I and hCA II) and acetylcholinesterase (AChE) enzymes, which are linked to various health issues, and compared the results with standard drugs. The antioxidant potential was assessed using five assays, namely DPPH, ABTS, FRAP, CUPRAC and Fe3+ reducing assays. The results determined that diosmin didn’t exhibit strong antioxidant activity. Additionally, the inhibition effects of diosmin on hCA I, hCA II, and AChE enzymes were examined. It effectively inhibited hCA I and hCA II enzymes with Ki values of 3.84±0.63 nM and 15.64±1.90 nM, respectively (Table 1). For comparison, the Ki values of the standard drug AZA were 1.44 ± 0.32 nM for hCA I and 3.66 ± 0.25 nM for hCA II. On the other hand, diosmin effectively inhibited AChE enzymes with Ki values of 9.31±2.40 nM. The Ki values of the standard drug Tacrine was 6.22±1.95 nM for AChE. These findings suggest that diosmin may serve as a selective enzyme inhibitor, particularly for hCA I, but has limited antioxidant capacity. Diosmin exhibited relatively weak antioxidant activity compared to standard antioxidants.

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  İncele
• MakaleYalnız künye2024Scopus SJRQ2/r/gumushane/11970
  Sulfonamide derivatives with benzothiazole scaffold: Synthesis and carbonic anhydrase I–II inhibition properties

  Öztürk, Cansu; Kalay, Erbay; Gerni, Serpil; Balci, Neslihan; Tokali, Feyzi Sinan; Aslan, Osman Nuri; Polat, Emrah

  The secondary sulfonamide derivatives containing benzothiazole scaffold (1–10) were synthesized to determine their inhibition properties on two physiologically essential human carbonic anhydrases isoforms (hCAs, EC, 4.2.1.1), hCA I, and hCA II. The inhibitory effects of the compounds on hCA I and hCA II isoenzymes were investigated by comparing their IC50 and Ki values. The Ki values of compounds (1–10) against hCA I and hCA II are in the range of 0.052 ± 0.022–0.971 ± 0.280 and 0.025 ± 0.010–0.682 ± 0.335, respectively. Some of these inhibited the enzyme more effectively than the standard drug, acetazolamide. In particular, compounds 5 and 4 were found to be most effective on hCA I and hCA II.

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  AtıfScopus13·WoS11·OpenAlex13

  İncele
• MakaleAçık Erişim2023Scopus SJRQ3/r/gumushane/14512
  Schiff Base Synthesis with a New Reliable Method and Investigation of Their Inhibition Effects on Glutathione S-Transferase and Cholinesterase Enzymes

  Balcı, Neslihan; Çelik, Hülya; Türkan, Fikret; Çelebioğlu, Neslihan; Çelik, Tuba; Bursal, Ercan

  The principle purpose of this study is to synthesize some Schiff base derivatives with a new microwave irradiation technique and investigate their enzyme inhibition effects. Related Schiff base compounds (1 a–1 h) were synthesized from 4-fluoro aniline and some substituted benzaldehyde derivatives (3 a–3 h). The chemical structures of Schiff bases were elucidated by various spectroscopic methods (1H NMR, 13C NMR). The inhibitory effects of the synthesized compounds against acetylcholinesterase, butyrylcholinesterase and glutathione S-transferase were investigated. The in vitro enzyme study determined the best enzyme inhibitors for AChE, BChE, and GST enzymes as 3 h, 3 b, and 3 e compounds, respectively. The results were compared with the standard drugs tacrine for cholinesterase and ethacrynic acid for GST enzymes. Molecular docking results demonstrated the low binding energy values between −5.8 kcal/mol and −8.7 kcal/mol with hydrogen bonding, hydrophilic, and hydrophobic interactions at the active catalytic sites of the enzymes.

  AtıfScopus14·WoS10·OpenAlex15

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