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Aminopyrazole-substituted metallophthalocyanines: Preparation, aggregation behavior, and investigation of metabolic enzymes inhibition properties
(WILEY-V C H VERLAG GMBH, 2019) Guzel, Emre; Kocyigit, Umit M.; Arslan, Baris S.; Atas, Mehmet; Taslimi, Parham; Gokalp, Faik; Nebioglu, Mehmet; Sisman, Ilkay; Gulcin, Ilhami
The synthesis, characterization, aggregation behavior, theoretical studies, and investigation of antimicrobial, antidiabetic, and anticholinergic properties of 4-(2-(5-amino-4-(4-bromophenyl)-3-methyl-1H-pyrazol-1-yl)ethoxy)phthalonitrile (2) and its soluble aminopyrazole-substituted peripheral metallo (Mn, Co, and Ni)-phthalocyanine complexes (3-5) are reported for the first time. The synthesized compounds and phthalocyanine complexes were characterized spectroscopically. The new phthalonitrile derivative (2) and its peripheral metallophthalocyanine complexes (3-5) were found to be effective inhibitors of alpha-glycosidase, acetylcholinesterase (AChE), human carbonic anhydrase I and II isoforms (hCA I and II), and butyrylcholinesterase (BChE) with K-i values in the range of 1.55 +/- 0.47 to 10.85 +/- 3.43 nM for alpha-glycosidase, 8.44 +/- 0.32 to 21.31 +/- 7.91 nM for hCA I, 11.73 +/- 2.82 to 31.03 +/- 4.81 nM for hCA II, 101.62 +/- 26.58 to 326.54 +/- 89.67 nM for AChE, and 68.68 +/- 11.15 to 109.53 +/- 19.55 nM for BChE. This is the first study of peripherally substituted phthalocyanines containing an aminopyrazole group as potential carbonic anhydrase enzyme inhibitor. Also, the antimicrobial activities of the synthesized compounds were evaluated against six microorganisms (four bacteria and two Candida species) using the broth microdilution method. The gram-positive bacteria were detected to be more sensitive than gram-negative bacteria and yeasts in the synthesized compounds.
Characterization and inhibition effects of some metal ions on carbonic anhydrase enzyme from Kangal Akkaraman sheep
(WILEY, 2018) Kocyigit, Umit M.; Taslimi, Parham; Gulcin, Ilhami
In this work, the carbonic anhydrase (CA) enzyme was purified from Kangal Akkaraman sheep in Sivas, Turkey with specific activity value of 6681.57 EU/mg and yield of 14.90% with using affinity column chromatography. For designating the subunit molecular mass and enzyme purity. sodium dodecyl sulfate polyacrylamide gel electrophoresis method was used and single band for this procedure was obtained. The molecular mass of CA enzyme was found as 28.89 kDa. In this study, the optimum temperature and optimum pH were obtained from 30 and 7.5. V-max and K(m )values for p-nitrophenylacetate substrate of the CA were determined from Lineweaver-Burk graphs. Additionally, the inhibitory results of diverse heavy metal ions (He+, Fe2+, pb(2+), co(2+), A(g+), and Cu2+) on sheep were studied. Indeed, CA enzyme activities of Kangal sheep were investigated with using esterase procedure under in vitro conditions. The heavy metal concentrations inhibiting 50% of enzyme activity (IC50) and K-i values were obtained.
Determination of the inhibition profiles of pyrazolyl-thiazole derivatives against aldose reductase and ?-glycosidase and molecular docking studies
(Wiley-V C H Verlag Gmbh, 2020) Demir, Yeliz; Taslimi, Parham; Kocyigit, Umit M.; Akkus, Musa; Ozaslan, Muhammet Serhat; Duran, Hatice Esra; Budak, Yakup
Aldose reductase (AR) is the first and rate-limiting enzyme of the polyol pathway, which converts glucose to sorbitol in an NADPH-dependent reaction. alpha-Glycosidase breaks down starch and disaccharides to glucose. Hence, inhibition of these enzymes can be regarded a considerable approach in the treatment of diabetic complications. AR was purified from sheep liver using simple chromatographic methods. The inhibitory effects of pyrazolyl-thiazoles ((3aR,4S,7R,7aS)-2-(4-{1-[4-(4-bromophenyl)thiazol-2-yl]-5-(aryl)-4,5-dihydro-1H-pyrazol-3-yl}phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives;3a-i) on AR and alpha-glycosidase enzymes were investigated. All compounds showed a good inhibitory action against AR and alpha-glycosidase. Among these compounds, compound3dexhibited the best inhibition profiles against AR, with aK(i)value of 7.09 +/- 0.19 mu M, whereas compound3eshowed the lowest inhibition effects, with aK(i)value of 21.89 +/- 1.87 mu M. Also, all compounds showed efficient inhibition profiles against alpha-glycosidase, withK(i)values in the range of 0.43 +/- 0.06 to 2.30 +/- 0.48 mu M, whereas theK(i)value of acarbose was 12.60 +/- 0.78 mu M. Lastly, molecular modeling approaches were implemented to predict the binding affinities of compounds against AR and alpha-glycosidase. In addition, the ADME analysis of the molecules was performed.
Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan beta-Lactam Derivatives
(MDPI, 2016) Genc, Hayriye; Kalin, Ramazan; Koksal, Zeynep; Sadeghian, Nastaran; Kocyigit, Umit M.; Zengin, Mustafa; Gulcin, Ilhami; Ozdemir, Hasan
beta-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. beta-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that beta-lactams are inhibitors of hCA I, II and AChE. The Ki values of beta-lactams (2a-k) were 0.44-6.29 nM against hCA I, 0.93-8.34 nM against hCA II, and 0.25-1.13 nM against AChE. Our findings indicate that beta-lactams (2a-k) inhibit both carbonic anhydrases (CA) isoenzymes and AChE at low nanomolar concentrations.
Evaluation of acetylcholinesterase and carbonic anhydrase inhibition profiles of 1,2,3,4,6-pentasubstituted-4-hydroxy-cyclohexanes
(WILEY, 2017) Kocyigit, Umit M.; Taslimi, Parham; Gezegen, Hayreddin; Gulcin, Ilhami; Ceylan, Mustafa
Carbonic anhydrase (CA; EC 4.2.1.1) is used for remedial purposes for several years, as there is significant focus on expanding more new activators (CAAs) and high affinity inhibitors. Alzheimers disease and other similar ailments such as dementia and vascular dementia with Lewy bodies reduce cholinergic activity in the important areas involved in cognition and memory. Prevalent drugs for the symptomatic therapy of dementia are significant in increasing the associated cholinergic deficiency by inhibiting acetylcholinesterase (AChE). These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with K-i values in the range of 6.70-35.85nM for hCA I, 18.77-60.84nM for hCA II, and 0.74-4.60 for AChE, respectively.
Evaluation of antimicrobial, antibiofilm and carbonic anhydrase inhibition profiles of 1,3-bis-chalcone derivatives
(WILEY, 2019) Tutar, Ugur; Kocyigit, Umit M.; Gezegen, Hayreddin
A series of 1,3-bis-chalcone derivatives (3a-i, 6a-i and 8) were synthesized and evaluated antimicrobial, antibiofilm and carbonic anhydrase inhibition activities. In this evaluation, 6f was found to be the most active compound showing the same effect as the positive control against Bacillus subtilis and Streptococcus pyogenes in terms of antimicrobial activity. Biofilm structures formed by microorganisms were damaged by compounds at the minimum inhibitory concentration value between 0.5% and 97%.1,3-bis-chalcones ( 3a-i, 6a-i and 8) showed good inhibitory action against human (h) carbonic anhydrase (CA) isoforms I and II. hCA I and II were effectively inhibited by these compounds, with K-i values in the range of 94.33 +/- 13.26 to 787.38 +/- 82.64nM for hCA I, and of 100.37 +/- 11.41 to 801.76 +/- 91.11nM for hCA II, respectively. In contrast, acetazolamide clinically used as CA inhibitor showed K-i value of 1054.38 +/- 207.33nM against hCA I, and 983.78 +/- 251.08nM against hCA II, respectively.
Experimental, density functional theory, molecular docking and ADMET analyses on the role of different plant extracts of Aronia melanocarpa (Michx) Elliot species on acetylcholinesterase enzyme activity
(Elsevier, 2025) Gurer, Eda Sonmez; Yildirim, Suheda; Kocyigit, Umit M.; Berisha, Avni; Kaya, Savas
In the present study, different extracts obtained in different solvents from the fruits collected from the Aronia melanocarpa (Michx.) were prepared. The inhibition performances of these extracts on the inhibition of the acetylcholinesterase enzyme were checked via both theoretical and experimental analyses. Although all extracts used in experimental studies showed high inhibitory activity, it was observed that the extract obtained in methanol had higher inhibitory activity than the others. According to the enzyme activity results presented in the light of Ellman method, IC50 values were found between 0.0311-0.0857 mg/mL. Conceptual Density Functional Theory (CDFT) and Molecular Docking calculations were performed to identify the component or components of the extract with high inhibitory activity. Conceptual Density Functional Theoretical based data commented through popular electronic structure principles such as Maximum Hardness and Minimum Electrophilicity Principles showed that the most reactive one among studied dominant components of the extract is Malvin molecule. The interactions between studied molecules and AChE and mechanisms of these interactions were illuminated via Molecular Docking analyses and ADMET studies. As a result, it was shown that the most reactive molecule Malvin (with lowest hardness and the highest electrophilicity) interacts more powerful with AChE compared to other molecules. Within the framework of the theoretical analyses made, it was proposed that in the design and introduction of new AChE inhibitors, structures with low hardness and high electrophilicity values should be preferred.
In vitro cytotoxic and in vivo antitumoral activities of some aminomethyl derivatives of 2,4-dihydro-3H-1,2,4-triazole-3-thiones-Evaluation of their acetylcholinesterase and carbonic anhydrase enzymes inhibition profiles
(WILEY, 2019) Timur, Irfan; Kocyigit, Umit M.; Dastan, Taner; Sandal, Suleyman; Ceribasi, Ali Osman; Taslimi, Parham; Gulcin, Ilhami; Koparir, Metin; Karatepe, Mustafa; Ciftci, Mehmet
The 1,2,4-triazole and its derivatives were reported to exhibit various pharmacological activities such as antimicrobial, analgesic, anti-inflammatory, antitumoural, cytotoxic, and antioxidant properties. In this study, a series of triazole compounds (M1-M10) were evaluated for some biological activities. In vitro qualifications of these compounds on acetylcholinesterase (AChE) and human carbonic anhydrase enzyme activities were performed. Also, their antitumoral activities in human colon cancer (HT29) cell line cultures were examined. In addition, colon cancer experimentation was induced in rats by an in vivo method, and the in vivo anticancer effects of triazole derivatives were investigated. Also, the effects of these derivatives in levels of antioxidant vitamin A, vitamin E, and MDA were studied in rat liver and blood samples. Most of the compounds were found to exhibit significant antioxidant and antitumoral activities. All the compounds had cytotoxic activities on HT29 cell lines with their IC50 values lower than 10 mu M concentrations. The low IC50 values of the compounds are M1 (3.88 mu M), M2 (2.18 mu M), M3 (4.2 mu M), M4 (2.58 mu M), M5 (2.88 mu M), M6 (2.37 mu M), M7 (3.49 mu M), M8 (4.01 mu M), M9 (8.90 mu M), and M10 (3.12 mu M).
Inhibitory effects of oxytocin and oxytocin receptor antagonist atosiban on the activities of carbonic anhydrase and acetylcholinesterase enzymes in the liver and kidney tissues of rats
(WILEY, 2017) Kocyigit, Umit M.; Taskiran, Ahmet Sevki; Taslimi, Parham; Yokus, Ahmet; Temel, Yusuf; Gulcin, Ilhami
The aim of this study was to investigate the effects of oxytocin (OT), atosiban, which is an OT receptor antagonist, and OT-atosiban chemicals injected to rats on the activities of carbonic anhydrase (CA) and acetylcholinesterase (AChE) enzymes in liver and kidney tissues of rats. For this purpose, four different groups, each consisting of six rats (n=6), were formed (control group, OT administered group, atosiban administered group, and both OT and atosiban administered group). The rats were necropsied 60min after intraperitoneal injection of chemicals into the rats. Liver tissues of rats were extracted. CA and AChE enzyme activities were measured for each tissue by using hydratase, esterase, and acetylcholiniodide methods. Activity values for each enzyme obtained were statistically calculated.
Inhibitory effects of Pb2+, Fe2+, Cd2+ and Co2+ on carbonic anhydrase enzyme from muscle of the Kangal fish ( Garra rufa)
(Polish Society Magnesium Research, 2024) Kocyigit, Umit M.; Gulcin, Ilhami
The Kangal fish (Garra rufa), known as the doctor fish, lives in the Kangal Spring in Sivas, Turkiye. In this study, carbonic anhydrase (CA) was purified and characterized for the first time from the muscle tissues of the Kangal fish (Garra rufa). To this end, CA was purified using a Sepharose-4B-L-Tyrosine-sulfanilamide affinity column (STAC) with specific activity of 34.36 EU.mg(-1), yield of 17.98 % and 201.0 purification fold. To control the CA enzyme purity, SDS-PAGE was performed and a single band was found. The Michaelis constant (K-m) and maximum velocity (V-max) were determined for CA. Also, p-nitrophenylacetate (PNA) was used as CA substrate. Furthermore, inhibition constants (Ki) and half maximal enzyme inhibitory concentration (IC50) for each metal ion were determined using by Lineweaver-Burk graphs. Additionally, optimum ionic strength was found to be 1.0 M (Tris-SO4), optimum pH was calcu-lated as 9.0 (Tris-SO4) and stable 8.5 pH was found (phosphate buffer) for the CA from the muscle tissues of the fish. Furthermore, activation enthalpy (Delta H), activation energy (Ea), optimum temperature and Q(10) values were obtained from the Arrhenius plot of CA from Garra rufa muscle tissue as 6.70 kcal/mol, 7.32 Kcal mol(-1), 35.0 oC, 1.37, respectively. Kcat and V0values of CA from Garra rufa muscle CA were calculated as 19.21 s(-1) and 1.8x10(4) mM s(-1), respectively. Finally, Ki values of some heavy metal ions (Co2+, Pb2+, Cd2+, and Fe2+) in the Kangal fish muscle CA were calculated in the range of 0.25-26.09 mM using the esterase activity assay.
Inhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas, Turkey
(WILEY, 2018) Kocyigit, Umit M.; Dastan, Sevgi Durna; Taslimi, Parham; Dastan, Taner; Gulcin, Ilhami
In this study, carbonic anhydrase (CA) enzyme was purified and characterized from blood samples of Kangal Akkaraman sheep and inhibitory properties on certain antibiotics were examined. CA purification was composed of preparation of the hemolysate and conducting the Sepharose-4B-tyrosine-sulfanilamide affinity gel chromatography in having specific activity of 11626EUmg(-1), yield of 14.40%, and 242.76-fold purification. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed to assess the enzyme purity and a single band was observed. Some antibiotics were exhibited in vitro inhibition on the CA activity. IC50 values of these inhibitors were calculated by plotting activity percentage. IC50 values of certain drugs (dexamethasone; caffeine; metamizole sodium; tetramisol; ceftiofur HCl; ivermectin; tavilin 50; penokain G; neosym; and sulfamezathine) were found as 0.38, 8.24, 285.53, 114.77, 5.33, 2.76, 27.58, 213.50, 208.28, and 36.60M, respectively. K-i values of different drugs on Kangal Akkaraman sheep blood CA activity were found in the range of 0.21 +/- 0.038-266.64 +/- 37.11 mu M.
Investigation of acetylcholinesterase and mammalian DNA topoisomerases, carbonic anhydrase inhibition profiles, and cytotoxic activity of novel bis(-aminoalkyl)phosphinic acid derivatives against human breast cancer
(WILEY, 2017) Dastan, Taner; Kocyigit, Umit M.; Dastan, Sevgi Durna; Kilickaya, Pakize Canturk; Taslimi, Parham; Cevik, Ozge; Koparir, Metin; Orek, Cahit; Gulcin, Ilhami; Cetin, Ahmet
The aim of this study was to evaluate biologically active novel molecules having potentials to be drugs by their antitumor properties and by activities of apoptotic caspase and topoisomerase. Following syntheses of novel eight bis(-aminoalkyl)phosphinic acid derivatives (4a-h) as a result of array of reactions, compounds were evaluated by cytotoxic effects in vitro on human breast cancer (MCF-7) and normal endothelial (HUVEC) cell lines. All phosphinic acid derivatives were effective for cytotoxicity on both MCF-7 and HUVEC lines, while 4c, 4e, and 4f compounds were found significantly more effective. For the evaluation of antitumor properties of compounds in a highly sensitive method, their effects on inhibiting topoisomerases I and II were investigated. Also, some of the bis(-aminoalkyl)phosphinic acid derivatives (4a, 4e-h) showed nice inhibitory action against acetylcholinesterase and human carbonic anhydrase isoforms I and II.
New hydrazone derivatives: synthesis, characterization, carbonic anhydrase I-II enzyme inhibition, anticancer activity and in silico studies
(Walter De Gruyter Gmbh, 2025) Cevik, Ulviye Acar; Unver, Hakan; Bostanci, Hayrani Eren; Tuzun, Burak; Gedik, Nurten Irem; Kocyigit, Umit M.
A new series of hydrazone derivatives (1a-1l) were prepared from a condensation reaction between different hydrazide derivatives and 3-formylbenzoic acid. Through the use of several spectral techniques, such as 1H-NMR, 13C-NMR, and elemental analysis, the structures of the compounds were clarified. The crystal structure of compound 1d was obtained by single-crystal X-ray crystallography. They were found to have inhibitory effects on the anticancer potentials and human carbonic anhydrase isoforms I and II. Compound 1d was found to be the strongest inhibitor, with IC50 values of 0.133 mu M against hCA I. Also, compound 1l showed the highest inhibitory activity with IC50 values of 3.244 mu M against hCA II. Moreover, their cytotoxic effects on rat glioma cell and colon adeno carcinoma cell lines were evaluated. According to the cytotoxicity results, compounds 1j and 1l exhibited the highest cytotoxicity on the HT29 cell, while compounds 1e, 1g, and 1l showed the strongest cytotoxic effect on C6 cell line. Compound 1l, which carries the methoxy substituent at the 3rd position on the phenyl ring, was effective against both cancer cells and showed the highest inhibitory effect on hCA II. The ADME/T properties and molecular docking of the molecules with the highest activity were examined.
New Thiazole Derivatives: Carbonic Anhydrase I-II and Cholinesterase Inhibition Profiles, Molecular Docking Studies
(Wiley-V C H Verlag Gmbh, 2024) Karakaya, Abdullatif; Ercetin, Tugba; Yildirim, Suheda; Kocyigit, Umit M.; Rudrapal, Mithun; Rakshit, Gourav; Cevik, Ulviye Acar
Thiosemicarbazone derivative was obtained by the addition of thiosemicarbazide to 5-nitro-thiophene-2-carbaldehyde. The addition-cyclization of the 2-bromoacetophenone derivative to thiosemicarbazone derivative gave the new thiazole derivatives (2 a-k). Acetylcholinesterase (AChE), butyrylcholinesterase (BChE), antioxidant, and human carbonic anhydrase (hCA) I and II isoform inhibitory activities of the thiazole derivatives 2 a-k were investigated. The effects of thiazole derivatives on carbonic anhydrase I and II (hCA I-II) isoenzymes were examined in vitro using the esterase method. IC50 values for enzyme inhibition were found to be 2.661-22.712 mu M for hCA I and 5.372-26.813 mu M for hCA II. All derivatives reduced the activities of carbonic anhydrase I and II isoenzymes and were new potential inhibitor molecule candidates. These compounds were found to have minimal effects on AChE and BChE. The antioxidant properties of the target compounds were determined using DPPH and ferric ion-chelating assays. In particular, compounds 2 k and 2 h had the highest antioxidant effect in the series with IC50 values of 30.11 +/- 0.008 mu M and 30.21 +/- 0.006 mu M, respectively. ADMET properties of the compounds found to be effective were evaluated and their interactions with the enzyme were determined by molecular docking.
Novel Aminothiazole-Chalcone Analogs: Synthesis, Evaluation Acetylcholinesterase Activity, In Silico Analysis
(Wiley-V C H Verlag Gmbh, 2025) Sarikaya, Meryem Kececi; Yildirim, Suheda; Kocyigit, Umit M.; Ceylan, Mustafa; Yirtici, Umit; Eyupoglu, Volkan
In this study, novel thiazole-chalcone analogs were synthesized, and their inhibitory effects on acetylcholinesterase (AChE) were examined. In vitro enzyme activity studies were conducted to calculate IC50 values, which were found to range between 2.55 and 72.78 mu M (tacrine IC50 = 53.31 mu M). The Ki values of the compounds showing the best inhibition (6g and 6e) were calculated and compared to those of the standard substance tacrine. All compounds reduced the AChE activity. Additionally, predictions made with SwissADME indicated that all compounds complied with Lipinski's rules and possessed good oral bioavailability properties, and the inhibitory effects of compounds 6e and 6g on AChE were evaluated using molecular docking and molecular dynamics simulations (100 ns). The results showed that compounds 6e and 6g had strong and stable interactions with AChE.
Novel diarylated tacrine derivatives: Synthesis, characterization, anticancer, antiepileptic, antibacterial, and antifungal activities
(Wiley, 2024) Misir, Busra A.; Derin, Yavuz; Okten, Salih; Aydin, Ali; Kocyigit, Umit M.; Sahin, Hatice; Tutar, Ahmet
In this study, our goal was to synthesize novel aryl tacrine derivatives and assess their potential as anticancer, antibacterial agents, and enzyme inhibitors. We adopted a two-step approach, initiating with the synthesis of dibromotacrine derivatives 3 and 4 through the Friedlander reaction. These intermediates underwent further transformation into diarylated tacrine derivatives 3a-e and 4a-e using a Suzuki-Miyaura cross-coupling reaction. Thorough characterization of these novel diarylated tacrines was achieved using various spectroscopic techniques. Our findings highlighted the potent anticancer effects of these innovative compounds across a range of cancer cell lines, including lung, gynecologic, bone, colon, and breast cancers, while demonstrating low cytotoxicity against normal cells. Notably, these compounds surpassed the control drug, 5-Fluorouracil, in terms of antiproliferative activity in numerous cancer cell lines. Moreover, our investigation included an analysis of the inhibitory properties of these novel compounds against various microorganisms and cytosolic carbonic anhydrase enzymes. The results suggest their potential for further exploration as cancer-specific, enzyme inhibitory, and antibacterial therapeutic agents. Notably, four compounds, namely, 5,7-bis(4-(methylthio)phenyl)tacrine (3d), 5,7-bis(4-(trifluoromethoxy)phenyl)tacrine (3e), 2,4-bis(4-(trifluoromethoxy)phenyl)-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-amine (4e), and 6,8-dibromotacrine (3), emerged as the most promising candidates for preclinical studies. The novel aryl substituted tacrine were efficiently synthesized and their anticancer potentials were highlighted in this study. Their inducing apoptosis, cell migration, and mitochondrial membrane potentials were screened. image
Phthalocyanine complexes with (4-isopropylbenzyl)oxy substituents: preparation and evaluation of anti-carbonic anhydrase, anticholinesterase enzymes and molecular docking studies
(Taylor & Francis Inc, 2022) Guzel, Emre; Kocyigit, Umit M.; Taslimi, Parham; Gulcin, Ilhami; Erkan, Sultan; Nebioglu, Mehmet; Arslan, Baris S.
In this study, the preparation, aggregation behavior and investigation of carbonic anhydrase and cholinesterase enzyme inhibition features of non-peripherally (4-isopropylbenzyl)oxy-substituted phthalocyanines (4-6) are reported for the first time. The chemical structures of these new phthalocyanines were elucidated by UV-Vis (ultraviolet-visible), FT-IR (Fourier transform infrared spectrometry), NMR (nuclear magnetic resonance) and MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass spectrometry. The substitution of 4-isopropylbenzyl)oxy groups benefits a remarkable solubility and redshift of the phthalocyanines Q-band. Also, these complexes were tested against some enzymes such as butyrylcholinesterase enzyme, human carbonic anhydrase I and II isoforms and acetylcholinesterase enzyme. The phthalocyanine complexes showed Ki values of in the range of 478.13 +/- 57.25-887.25 +/- 101.20 mu M against hCA I, 525.16 +/- 45.87-921.14 +/- 81.25 mu M against hCA II, 68.33 +/- 9.13-201.15 +/- 35.86 mu M against AChE and 86.25 +/- 13.65-237.54 +/- 24.7 mu M against BChE. Molecular docking studies were performed to investigate the binding modes and interaction energies of the (2-6) complexes with the hCA I (PDB ID:1BMZ), hCA II (PDB ID:2ABE), AChE (PDB ID:4EY6) and BChE (PDB ID:2PM8).
Purification of glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocytes and inhibition effects of some metal ions on enzyme activity
(WILEY, 2017) Temel, Yusuf; Kocyigit, Umit M.
Glucose-6-phosphate dehydrogenase (G6PD) is the first enzyme on which the pentose phosphate pathway was checked. In this study, purification of a G6PD enzyme was carried out by using rat erythrocytes with a specific activity of 13.7EU/mg and a yield of 67.7 and 155.6-fold by using 2,5-ADP Sepharose-4B affinity column chromatography. For the purpose of identifying the purity of enzyme and molecular mass of the subunit, a sodium dodecyl sulfate-polyacrylamide gel electrophoresis was carried out. The molecular mass of subunit was calculated 56.5kDa approximately. Then, an investigation was carried out regarding the inhibitory effects caused by various metal ions (Fe2+, Pb2+, Cd2+, Ag+, and Zn2+) on G6PD enzyme activities, as per Beutler method at 340nm under in vitro conditions. Lineweaver-Burk diagrams were used for estimation of the IC50 and K-i values for the metals. K-i values for Pb+2, Cd+2, Ag+, and Zn+2 were 113.3, 215.2, 19.4, and 474.7M, respectively.
Purification of glutathione S-transferase enzyme from quail liver tissue and inhibition effects of (3aR,4S,7R,7aS)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives on the enzyme activity
(WILEY, 2018) Temel, Yusuf; Kocyigit, Umit M.; Taysi, M. Serif; Gokalp, Faik; Gurdere, Meliha Burcu; Budak, Yakup; Ceylan, Mustafa; Gulcin, Ilhami; Ciftci, Mehmet
The use of quail meat and eggs has made this animal important in recent years, with its low cost and high yields. Glutathione S-transferases (GST, E.C.2.5.1.18) are an important enzyme family, which play a critical role in detoxification system. In our study, GST was purified from quail liver tissue with 47.88-fold purification and 12.33% recovery by glutathione agarose affinity chromatography. The purity of enzyme was checked by SDS-PAGE method and showed a single band. In addition, inhibition effects of (3aR,4S,7R,7aS)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1H-4,7methanoisoindole-1,3(2H)-dion derivatives (1a-g) were investigated on the enzyme activity. The inhibition parameters (IC50 and K-i values) were calculated for these compounds. IC50 values of these derivatives (1a-e) were found as 23.00, 15.75, 115.50, 10.00, and 28.75M, respectively. K-i values of these derivatives (1a-e) were calculated in the range of 3.04 +/- 0.50 to 131.50 +/- 32.50M. However, for f and g compounds, the inhibition effects on the enzyme were not found.
Quinoline-based promising anticancer and antibacterial agents, and some metabolic enzyme inhibitors
(Wiley-V C H Verlag Gmbh, 2020) Okten, Salih; Aydin, Ali; Kocyigit, Umit M.; Cakmak, Osman; Erkan, Sultan; Andac, Cenk A.; Taslimi, Parham
A series of substituted quinolines was screened for their antiproliferative, cytotoxic, antibacterial activities, DNA/protein binding affinity, and anticholinergic properties by using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide cell proliferation, lactate dehydrogenase cytotoxicity, and microdilution assays, the Wolfe-Shimmer equality method, the Ellman method, and the esterase assay, respectively. The results of the cytotoxic and anticancer activities of the compounds displayed that 6-bromotetrahydroquinoline (2), 6,8-dibromotetrahydroquinoline (3), 8-bromo-6-cyanoquinoline (10), 5-bromo-6,8-dimethoxyquinoline (12), the novelN-nitrated 6,8-dimethoxyquinoline (13), and 5,7-dibromo-8-hydroxyquinoline (17) showed a significant antiproliferative potency against the A549, HeLa, HT29, Hep3B, and MCF7 cancer cell lines (IC50 = 2-50 mu g/ml) and low cytotoxicity (similar to 7-35%) as the controls, 5-fluorouracil and cisplatin. The compound-DNA linkages are hyperchromic or hypochromic, causing variations in their spectra. This situation shows that they can be bound to DNA with the groove-binding mode, withK(b)value in the range of 2.0 x 10(3)-2.2 x 10(5) M-1. Studies on human Gram(+) and Gram(-) pathogenic bacteria showed that the substituted quinolines exhibited selective antimicrobial activities with MIC values of 62.50-250 mu g/ml. All tested quinoline derivatives were found to be effective inhibitors of acetylcholinesterase (AChE) and the human carbonic anhydrase I and II isoforms (hCA I and II), withK(i)values of 46.04-956.82 nM for hCA I, 54.95-976.93 nM for hCA II, and 5.51-155.22 nM for AChE. As a result, the preliminary data showed that substituted quinolines displayed effective pharmacological features. Molecular docking studies were performed to investigate the binding modes and interaction energies for compounds2-17with AChE (PDB ID: 4EY6), hCA I (PDB ID: 1BMZ), and hCA II (PDB ID: 2ABE).

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