Sürdürülebilir Kalkınma Amaçları
Yazarlar
- Topal, Fevzi(5)
- Supuran, Claudiu T.(4)
- Topal, Meryem(4)
- Gülçin, Ilhami(3)
- Gulcin, Ilhami(2)
- Keskin, Ali(2)
- Yapıcı, İsmail(2)
- Çelik, Murat(2)
- Şentürk, Murat(2)
- Afsin Kaya, A.(1)
- Akar, Zeynep(1)
- Aksu, Kadir(1)
- Alver, A.(1)
- Alver, Ahmet(1)
- Alwasel, Saleh H.(1)
- Atmaca, Ufuk(1)
- Aygul, Imdat(1)
- Ayna, Adnan(1)
- Balci, Neslihan(1)
- Capkin A, Aydin(1)
- Danis, Ozkan(1)
- Dastan, Arif(1)
- Demir, S.(1)
- Demir, Selim(1)
- Durdagi, Serdar(1)
- Ekhteiari Salmas, Ramin(1)
- Fidan, Evren(1)
- Fidan, Sami(1)
- Gezegen, Hayreddin(1)
- Gocer, Hulya(1)
- Goksu, Süleyman(1)
- Guney, Murat(1)
- Göksu, Haydar(1)
- Gülin, Ihami(1)
- Gültekin, Mehmet S.(1)
- Gülçin, İlhami(1)
- Hakan, Oguzhan(1)
- Karahalil, Fatma Yaylaci(1)
- Karkucak, M.(1)
- Kavgaci, Halil(1)
Yayınlar
- MakaleYalnız künye2026Phytochemical profiling, biological activities, and molecular docking analysis of Dorycnium pentaphyllum subsp. haussknechtii
Ayna, Adnan; Hakan, Oguzhan; Yapıcı, İsmail; İzol, Ebubekir; Yılmaz, Mustafa Abdullah; Necip, Adem; Yapar, Yakup
BACKGROUND: In the current study, the biological activity fingerprint of Dorycnium pentaphyllum subsp. haussknechtii was investigated by an interdisciplinary approach through analysis of its phytochemical content, antioxidant capacity, enzyme inhibitory potential and molecular docking. RESULTS: The analysis of the phytochemical content by liquid chromatography–tandem mass spectrometry was characterized by the presence of flavan-3-ols, such as epicatechin, epigallocatechin, and catechin, as well as quercetin-derived flavonoids such as isoquercitrin. Analysis of the antioxidant capacity by 2,2-diphenyl-1-picrylhydrazyl, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), ferric reducing antioxidant power, Fe3+–Fe2+ reducing and cupric reducing antioxidant capacity methods indicated the strong antioxidant capacity of the plant extract. In addition, the plant extract was able to modulate biological enzyme activity effectively, with IC50 values of 111.78 μg mL−1 for acetylcholinesterase, 22.07 μg mL−1 for butyrylcholinesterase, 1.39 μg mL−1 for α-glucosidase, 7.34 μg mL−1 for carbonic anhydrase I, and 17.41 μg mL−1 for carbonic anhydrase II. To have a better understanding of the molecular mechanism for the plant extract's properties, the major phenolic compounds present in the plant extract were investigated for molecular docking with their respective enzymes. As such, the results revealed a strong binding affinity and conformational stability, with strong hydrogen bonding and π–π interactions. CONCLUSION: Generally, the properties revealed by the plant extract indicate that the phenolic content, strong antioxidant properties, and enzyme inhibition activity of D. pentaphyllum subsp. haussknechtii have shown great potential for being a useful natural source for therapeutic lead compounds.
- MakaleAçık Erişim2026Synthesis, Characterization, Biological Properties, and Sensor Applications of Novel Thiosemicarbazone Derivatives
Gezegen, Hayreddin; Özbek, Oguz; Topal, Meryem; Şahin, Hatice; Koçyiğit, Ümit M.
In this study, novel thiosemicarbazone derivative molecules (5a–j) were synthesized. The characterization of the synthesized molecules was carried out using 1H–, 13C–NMR, FT–IR, and Q–TOF spectroscopic techniques. Then, the inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The hCA I II, and AChE were efficiently inhibited by synthesized thiosemicarbazone derivatives, with Ki values in the range of 0.293–1.666 µM for hCA I, 0.298–1.332 µM for hCA II, and 52.51–138.63 µM for AChE, respectively. Finally, the sensor properties of the synthesized thiosemicarbazone derivatives were investigated. The newly synthesized thiosemicarbazone derivative molecules exhibited high selectivity towards Pb2+ ions. The sensor prepared with 5a from these molecules had a Nernstian behavior of 28.8 ± 1.5 mV/decade and a low detection limit of 2.86 × 10−6 M in a wide concentration range of 1.0 × 10−1–1.0 × 10−5 M. The newly proposed sensor also had a wide pH working range (5.0–10.0), a very fast response time (5 s), and good reproducibility. The newly fabricated sensors were used as indicator electrodes for the potentiometric titration of Pb2+ ions with ethylenediaminetetraacetic acid (EDTA) and were successfully applied for the determination of Pb2+ ion content in different water samples.
- MakaleAçık Erişim2026Green Synthesis and Bioactivities of Silver Nanoparticles Derived from Mercurialis annua L. Extract
Salad, Aisha Mohamud; Akar, Zeynep
Biogenic synthesis using plant materials provides a sustainable alternative to classical nanoparticle fabrication, minimizing chemical hazards and decreasing energy input. In this study, silver nanoparticles (AgNPs) were prepared using an aqueous extract of Mercurialis annua and characterized. Physicochemical properties of the AgNPs were confirmed using ultraviolet–visible spectroscopy (UV–Vis), Fourier transform infrared (FTIR) analysis, X-ray diffraction (XRD), and transmission electron microscopy coupled with energy-dispersive X-ray (TEM–EDX), which collectively indicated crystalline, spherical silver nanoparticles stabilized by extract-derived functional groups. Subsequently, the biological activities of both the nanoparticles and the extract were comparatively evaluated using antioxidant tests, including cupric ion reducing antioxidant capacity (CUPRAC), ferric reducing antioxidant power (FRAP), 2,2-diphenyl-1-picrylhydrazyl (DPPH), total phenolic content (TPC), and total flavonoid content (TFC), as well as enzyme inhibition tests targeting α-glucosidase and carbonic anhydrase. Liquid chromatography-mass spectrometry profiling identified 31 phenolic constituents in the extract, with ferulic, caffeic, salicylic, and 4-hydroxybenzoic acids detected in high abundance. Overall, the biosynthesized AgNPs demonstrated higher antioxidant performance and stronger inhibitory effects on both enzymes compared with the crude extract. These results indicate that M. annua-based AgNPs hold considerable promise sustainable and effective bioactive agents for future biomedical and biotechnological applications.
- MakaleAçık Erişim2026Evaluation of antioxidant and antiproliferative activities of shogaol and its modulatory effects on key metabolic enzymes
Yapıcı, İsmail; Gülçin, İlhami
Phenolic compounds are versatile bioactive molecules, particularly in food applications. In this study, the antioxidant capacity of Shogaol, a member of the phenolic class, was evaluated using several methods. Additionally, its inhibitory effects on human carbonic anhydrase I and II (hCA I and II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), α-glycosidase, and α-amylase enzymes, as well as its antiproliferative effects on A-549 lung cancer, HT-29 colon cancer, MCF-7 and MDA-MB-453 breast cancer cell lines, and the 3T3-L1 mouse fibroblast normal cell line, were investigated. To determine the antioxidant capacity of Shogaol, DPPH and ABTS radical scavenging assays, as well as Cu²⁺, Fe³⁺, and FRAP reduction methods, were employed. Its inhibitory effects on hCA I and II, AChE, BChE, α-glycosidase, and α-amylase enzymes were examined. Furthermore, cell counting was performed using the TBE method, and cell viability was measured with the XTT assay to assess the antiproliferative effects of Shogaol on A-549, HT-29, MCF-7, MDA-MB-453, and 3T3-L1 cell lines. Shogaol demonstrated higher antioxidant capacity than BHA, BHT, and Trolox in the FRAP assay (60 µg/mL), higher than BHT in the DPPH scavenging assay, and higher than Trolox in the ABTS, Cu²⁺, and Fe³⁺ reduction assays. Shogaol also exhibited significant inhibitory effects against hCA I, hCA II, AChE, BChE, and α-glycosidase, with IC₅₀ values of 75.91, 47.04, 37.44, 24.11, and 35.72 nM, respectively. Moreover, Shogaol showed a more potent antiproliferative effect than the standard chemotherapeutic drug Carboplatin in A-549 lung cancer and HT-29 colon cancer cell lines, and greater efficacy than Docetaxel in the MCF-7 breast cancer cell line.
- MakaleAçık Erişim2025Inhibition 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.
- MakaleYalnız künye2021Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes
Topal, Fevzi; Aksu, Kadir; Gulcin, Ilhami; Tümer, Ferhan; Goksu, Süleyman
In this work, the inhibitory effect of some symmetric sulfamides derived from phenethylamines were determined against human carbonic anhydrase (hCA) I, and II isoenzymes, and compared with standard compound acetazolamide. IC50 values were obtained from the Enzyme activity (%)-[Symmetric sulfamides] graphs. Also, Ki values were calculated from the Lineweaver-Burk graphs. Some symmetric sulfamides compounds (11–18) demonstrated excellent inhibition effects against hCA I, and II isoenzymes. These compounds demonstrated effective inhibitory profiles with IC50 values in ranging from 21.66–28.88 nM against hCA I, 14.44–30.13 nM against hCA II. Among these compounds, the best Ki value for hCA I (Ki: 8.34±1.60 nM) and hCA II (Ki: 16.40±1.00 nM) is compound number 11. Besides, the IC50 value of acetazolamide used as a standard was determined as hCA I, hCA II 57.75 nM, 49.50 nM, respectively. Moreover, in silico ADME-Tox study showed that all synthesized compounds (11–18) had good oral bioavailability in light of Jorgensen's rule of three, and of Lipinski's rule of five.
- MakaleYalnız künye2019Inhibition profiles of Voriconazole against acetylcholinesterase, α-glycosidase, and human carbonic anhydrase I and II isoenzymes
Topal, Fevzi
In this work, the inhibitory activity of Voriconazole was measured against some metabolic enzymes, including human carbonic anhydrase (hCA) I and II isoenzymes, acetylcholinesterase (AChE), and α-glycosidase; the results were compared with standard compounds including acetazolamide, tacrine, and acarbose. Half maximal inhibition concentration (IC50) values were obtained from the enzyme activity (%)-[Voriconazole] graphs, whereas Ki values were calculated from the Lineweaver-Burk graphs. According to the results, the IC50 value of Voriconazole was 40.77 nM for α-glycosidase, while the mean inhibition constant (Ki) value was 17.47 ± 1.51 nM for α-glycosidase. The results make an important contribution to drug design and have pharmacological applications. In addition, the Voriconazole compound demonstrated excellent inhibitory effects against AChE and hCA isoforms I and II. Voriconazole had Ki values of 29.13 ± 3.57 nM against hCA I, 15.92 ± 1.90 nM against hCA II, and 10.50 ± 2.46 nM against AChE.
- MakaleYalnız künye2018Investigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates
Aygul, Imdat; Karahalil, Fatma Yaylaci; Danis, Ozkan; Ogan, Ayse; Kolayli, Sevgi
Introduction: This study investigated the in vitro inhibition properties of newly synthesized coumarin derivates (C1-C5) against human carbonic anhdyrase I (hCA-I) and jack bean urease. Activities were expressed as IC50 (mg/mL), the concentration reducing 50% of the enzymes. The IC50 values for hCA-I ranged 5.20 µM from 12.10 µM, with compound C3 exhibiting the highest activity. The inhibition values for urease ranged 22.30 µM to 39.00 µM, the highest activity being observed in C5. Conclusion: Comparing the inhibitions with standard inhibitors of the enzymes, while the samples exhibited moderate inhibitions against hCA I, high inhibition was determined against urease.
- MakaleAçık Erişim2017Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors
Topal, Fevzi; Gulcin, Ilhami; Dastan, Arif; Guney, Murat
Eugenol was used as starting material to obtain some phenolic compounds. The synthesis of these phenolic compounds was performed in a two-step procedure. The structures of the formed products (novel eugenol derivatives 1–6) have been determined on the basis of NMR spectroscopy and other spectroscopic methods. The compounds were tested in terms of carbonic anhydrase (CA) inhibition potency. Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes, which catalyse the reaction between carbon dioxide (CO2) and water (H2O), to generate bicarbonate (HCO3−) and protons (H+). CO2, HCO3− and H+ are essential molecules and ions for many important physiologic processes occurring in all living organisms. Acetylcholinesterase (AChE, E.C.3.1.1.7) is found in high concentrations in the red blood cells and brain. Novel eugenol derivatives (1–6) were tested for the inhibition of two cytosolic CA isoforms I, and II (hCA I, and II) and AChE. These compounds demonstrated effective inhibitory profiles with Ki values in ranging of 113.48-738.69 nM against hCA I, 92.35-530.81 nM against hCA II, and 90.10-379.57 nM against AChE, respectively. On the other hand, acetazolamide clinically used as CA inhibitor, shoed Ki value of 594.11 nM against hCA I, and 120.68 nM against hCA II, respectively. Also, AChE was inhibited by tacrine as an AChE inhibitor at the 71.18 nM level.
- MakaleAçık Erişim2017Detection of autoantibodies against carbonic anhydrase I and II in the plasma of patients with gastric cancer
Mentese, Ahmet; Fidan, Evren; Alver, Ahmet; Demir, Selim; Yaman, Serap Ozer; Sumer, Aysegul; Fidan, Sami; Kavgaci, Halil; Turan, Ibrahim
Cancer is the second leading cause of death and gastric cancer is the fourth most common cancer type worldwide. Investigation of autoantibodies in cancer patients has been a popular research area in recent years. The aim of the current study was to investigate carbonic anhydrase I and II (CA I and II) autoantibodies in the plasma of subjects with gastric cancer based on the information and considerations of autoimmune relation of gastric cancer. Anti-CA I and II antibody levels were investigated by ELISA in plasma samples of fifty two patients with gastric cancer and thirty five healthy peers. Anti-CA I and II antibody titers of the gastric cancer group were significantly higher compared with the control group (p = 0.004, p = 0.0001, respectively). Plasma anti-CA I levels of the metastatic group were lower than the non-metastatic group and this difference was found statistically significant (p < 0.05), but there was no statistical difference between plasma anti-CA II levels of the groups. CA I and II autoantibody titers in patients with gastric cancer were found higher compared to healthy subjects and the results suggest that these autoantibodies may be involved in the pathogenesis of gastric cancer.
- MakaleYalnız künye2017Carbonic anhydrase I and II autoantibodies in Behcet's disease
Mentese, A.; Alver, A.; Demir, S.; Sumer, A.; Yaman S, Ozer; Karkucak, M.; Capkin A, Aydin; Us, Altay D.; Turan, I
Background: Behcet's disease ( BD) is a vasculitis, seen more frequently around the Mediterranean and the Far East, and evinces with oral and genital ulcerations, skin lesions and uveitis. Carbonic anhydrase ( CA) is a metalloenzyme which is widely distributed in the living world, and it is essential for the regulation of acid-base balance. Anti-CA antibodies have been reported in many disorders, such as systemic lupus erythematosus, Sjogren's syndrome, rheumatoid arthritis, endometriosis, idiopathic chronic pancreatitis, type 1 diabetes and Graves' disease. The goal of this study was to investigate CA I and II autoantibodies in BD. Methods: 35 patients with BD and 29 healthy controls were included in the study and CA I and II autoantibody levels were investigated by ELISA. Results: The CA I and II autoantibody levels of BD group were significantly higher than the healthy group (p= 0.013, p= 0.0001, respectively). A cut-off value of 0.250 absorbance unit (ABSU) for anti-CA I was associated with 34% sensitivity and 100% specificity and a cut-off value of 0.171 ABSU for anti-CA II was associated with 54% sensitivity and 100% specificity for predicting BD. Conclusion: The CA I and II autoantibody levels in pa-tients with BD were found higher compared to control group and the results suggest that CA I and II autoantibodies may be involved in the pathogenesis of BD
- MakaleAçık Erişim2016Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and II
Ekhteiari Salmas, Ramin; Mestanoglu, Mert; Durdagi, Serdar; Sentürk, Murat; Kaya, A. Afşin; Kaya, Elif Çelenk
A series of hydroxy and phenolic compounds have been assayed for the inhibition of two physiologically relevant carbonic anhydrase (CA, EC 4.2.1.1) isozymes, the cytosolic human isozymes I and II. The investigated molecules showed inhibition constants in the range of 1.07-4003 and 0.09-31.5 μM at the hCA I and hCA II enzymes, respectively. In order to investigate the binding mechanisms of these inhibitors, in silico studies were also applied. Molecular docking scores of the studied compounds are compared using three different scoring algorithms, namely Glide/SP, Glide/XP and Glide/IFD. In addition, different ADME (absorption, distribution, metabolism and excretion) analysis was performed. All the examined compounds were found within the acceptable range of pharmacokinetic profiles.
- MakaleAçık Erişim20169,10-Dibromo-N-aryl-9,10-dihydro-9,10-[3,4]epipyrroloanthracene-12,14-diones: Synthesis and Investigation of Their Effects on Carbonic Anhydrase Isozymes I, II, IX, and XII
Göksu, Haydar; Topal, Meryem; Keskin, Ali; Gültekin, Mehmet S.; Çelik, Murat; Gülçin, Ilhami; Tanc, Muhammet; Supuran, Claudiu T.
N-substituted maleimides were synthesized from maleic anhydride and primary amines. 1,4-Dibromo-dibenzo[e,h]bicyclo-[2,2,2]octane-2,3-dicarboximide derivatives (4a-f) were prepared by the [4+2] cycloaddition reaction of dibromoanthracenes with the N-substituted maleimide derivatives. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory effects of the new derivatives were assayed against the human (h) isozymes hCA I, II, IX, and XII. All tested bicyclo dicarboximide derivatives exhibited excellent inhibitory effects in the nanomolar range, with Ki values in the range of 117.73-232.87 nM against hCA I and of 69.74-111.51 nM against hCA II, whereas they were low micromolar inhibitors against hCA IX and XII. A series of 9,10-dibromo-N-aryl-9,10-dihydro-9,10-[3,4]epipyrroloanthracene-12,14-diones (4a-f) were synthesized from N-substituted maleimide derivatives and 9,10-dibromoanthracene. Compounds 4a-f were assayed against human carbonic anhydrases (hCA) IX and XII, which are the two tumor-associated isozymes, and hCA I and II, which represent the most common off-targets for the development of selective anticancer CA inhibitors.
- MakaleAçık Erişim2016Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin
Gocer, Hulya; Topal, Fevzi; Topal, Meryem; Küçük, Murat; Teke, Dilek; Gülçin, Ilhami; Alwasel, Saleh H.; Supuran, Claudiu T.
Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate (HCO3-) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K-i of 29.2nM against hCA I, and 24.2nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K-i parameter of taxifolin was determined to be 16.7nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.
- MakaleAçık Erişim2015N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes i and II
Yildirim, Alper; Atmaca, Ufuk; Keskin, Ali; Topal, Meryem; Çelik, Murat; Gülçin, Ilhami; Supuran, Claudiu T.
Sulfonamides represent a significant class of biologically active compounds that inhibit carbonic anhydrase (CA, EC.: 4.2.1.1) isoenzymes involved in different pathological and physiological events. Sulfonamide CA inhibitors are used therapeutically as diuretic, antiglaucoma, antiobesity and anticancer agents. A series of new sulfonamides were synthesized using imides and tosyl chloride as starting materials. These N-acylsulfonamides efficiently inhibited the cytosolic human carbonic anhydrase isoenzymes I, and II (hCA I, and II), with nanomolar range inhibition constants ranging between 36.4 ± 6.0-254.6 ± 18.0 and 58.3 ± 0.6-273.3 ± 2.5 nM, respectively.
- MakaleYalnız künye2015Synthesis, antifungal activity and carbonic anhydrase inhibitory properties of Cu (II) Bis (3, 4 dimethoxybenzoate) bis (nicotinamide) dihydrate
Afsin Kaya, A.; Kaya, Elif Celenk; Sarikaya, S. Beyza Ozturk; Onaran, Abdurrahman
The new 3,4-dimethoxybenzoate complex of Cu(II) with nicotinamide was synthesized and characterized by elemental analysis, FT-IR spectroscopic study, UV-Vis spectrophotometry and mass spectrometry. The thermal behavior of the complex was studied by simultaneous TG, DTG and DTA methods in static air atmosphere. The infrared spectral characteristics of the complex is also discussed. In this complex, all ligands are coordinated to the metal ion as monodendate ligands. The final decomposition products were found to be the respective metal oxide. As it is well known, metal complexes of biologically important ligands are sometimes more effective than the free ligands. In this study the new compound was synthesized due to its functional groups such as veratric acid and nikotin amide, which have known biological characteristics and effective in terms of both enzyme and antifungal properties from recent studies. Therefore, antifulgal activity and enzyme inhibition properties of this complex have been examined.
- MakaleAçık Erişim2015Synthesis and determination of some biological activities of novel 2,4-dinitrophenyl derivatives
Öztürk Sarikaya, Sevim B.; Kaya, Afşin A.; Kaya, Elif C¸elenk; Şentürk, Murat
The antioxidant and radical scavenging activities of the synthesized compounds 3, 5, and 6 were determined by various in vitro assays such as 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid radical (ABTS.+) scavenging, ferric ion (Fe3+) reducing power and ferrous ion (Fe2+) chelating activities. Moreover, these activities were compared to those of standard antioxidants such as butylated hydroxyanisole, butylated hydroxytoluene, and trolox. The results showed that the new compounds (3, 5, and 6) had potential antioxidant activity. Besides, inhibition of the two human cytosolic carbonic anhydrase (hCA, EC 4.2.1.1) isozymes I and II with some nitrobenzene compounds was investigated. Compounds 1-6 showed Ki values in the range of 4.88-193.4 μM and 5.295-54.75 μM for hCA I and hCA II, respectively.
- MakaleAçık Erişim2011In vitro inhibition of α-carbonic anhydrase isozymes by some phenolic compounds
Öztürk Sarikaya, Sevim Beyza; Topal, Fevzi; Şentürk, Murat; Gülin, Ihami; Supuran, Claudiu T.
Carbonic anhydrase inhibitors (CAIs) are a class of pharmaceuticals used as antiglaucoma agents, diuretics, antiepileptics, in the management of mountain sickness, gastric and duodenal ulcers, neurological disorders or osteoporosis. We report here the inhibitory capacities of some phenolic compounds against three human CA isozymes (hCA I, hCA II, and hCA VI) and the gill carbonic anhydrase of the teleost fish Dicentrarchus labrax (European seabass) (dCA). The isozymes showed quite diverse inhibition profiles with these compounds. These data may lead to design novel CAIs with a diverse inhibition mechanism compared to sulfonamide/sulfamate inhibitors.