Sürdürülebilir Kalkınma Amaçları
Yazarlar
- Aygul, Imdat(3)
- Ozdemir, Hasan(2)
- Sarikaya, S. Beyza Ozturk(2)
- Supuran, Claudiu T.(2)
- Adem, Şevki(1)
- Afsin Kaya, A.(1)
- Akincioğlu, Hülya(1)
- Aslan, Osman Nuri(1)
- Aygül, İmdat(1)
- Balci, Neslihan(1)
- Cankaya, Murat(1)
- Ciftci, Mehmet(1)
- Danis, Ozkan(1)
- Demirdağ, Ramazan(1)
- Gerni, Serpil(1)
- Gulcin, Ilhami(1)
- Gülin, Ihami(1)
- Gülçin, İlhami(1)
- Kalay, Erbay(1)
- Karahalil, Fatma Yaylaci(1)
- Kaya, Elif Celenk(1)
- Kolayli, Sevgi(1)
- Kuzu, Müslüm(1)
- Ogan, Ayse(1)
- Onaran, Abdurrahman(1)
- Polat, Emrah(1)
- Sağlamtaş, Rüya(1)
- Sisecioglu, Melda(1)
- Tokali, Feyzi Sinan(1)
- Topal, Fevzi(1)
- Tuğba Demirbaş(1)
- Yaylaci Karahalil, Fatma(1)
- Çomaklı, Veysel(1)
- Öztürk Sarikaya, Sevim Beyza(1)
- Öztürk, Cansu(1)
- Şentürk, Murat(1)
Yayınlar
- MakaleYalnız künye2024Assessment of Anticholinergic and Antidiabetic Properties of Some Natural and Synthetic Molecules: An In Vitro and In Silico Approach
Çomaklı, Veysel; Aygül, İmdat; Sağlamtaş, Rüya; Kuzu, Müslüm; Demirdağ, Ramazan; Akincioğlu, Hülya; Adem, Şevki; Gülçin, İlhami
Introduction: This study aimed to determine the in vitro and in silico effects of some natural and synthetic molecules on acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and α-glucosidase enzymes. Background: Alzheimer's disease (AD) and Type II diabetes mellitus (T2DM) are considered the most important diseases of today’s world. However, the side effects of therapeutic agents used in both diseases limit their use. Therefore, developing drugs with high therapeutic efficacy and better pharmacological profile is important. Objectives: This study sets out to determine the related enzyme inhibitors used in treating AD and T2DM, considered amongst the most important diseases of today’s world. Methods: In the current study, the in vitro and in silico effects of dienestrol, hesperetin, L-thyroxine, 3,3',5-Triiodo-L-thyronine (T3) and dobutamine molecules on AChE, BChE and α-glycosidase enzyme activities were investigated. Results: All the molecules showed an inhibitory effect on the enzymes. The IC50 and Ki values of the L-Thyroxine molecule, which showed the strongest inhibition effect for the AChE enzyme, were determined as 1.71 µM and 0.83 ± 0.195 µM, respectively. In addition, dienestrol, T3, and dobutamine molecules showed a more substantial inhibition effect than tacrine. The dobutamine molecule showed the most substantial inhibition effect for the BChE enzyme, and IC50 and Ki values were determined as 1.83 µM and 0.845 ± 0.143 µM, respectively. The IC50 and Ki values for the hesperetin molecule, which showed the strongest inhibition for the α-glycosidase enzyme, were determined as 13.57 µM and 12.33 ± 2.57 µM, respectively. Conclusion: According to the results obtained, the molecules used in the study may be considered potential inhibitor candidates for AChE, BChE and α-glycosidase.
- MakaleYalnız künye2024Sulfonamide 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.
- Yüksek Lisans TeziAçık Erişim2023Farklı oranlarda kırmızı pancar ilave edilmiş ekşi mayalı ekmeğin renk ve antioksidan özelliklerinin araştırılması
Tuğba Demirbaş
Bu çalışmada insan sağlığı açısından önemi anlaşılan ve tüketimi yaygınlaşan ekşi mayalı ekmekte kırmızı pancar (Beta vulgaris L.) kullanılarak fonksiyonel bir ürünün hazırlanması amaçlanmıştır. Araştırma kapsamında mikrodalga, kurutma kabini ve sıcak hava kurutma yöntemleriyle kurutulup öğütülen pancar tozları kontrol %4, %8, %12 oranlarında ekşi mayalı hamura katıldı. Örneklerin pH, kuru madde ve kül miktarları tespit edildi. Antioksidan aktivitesi; Cu2+-Cu+ indirgeme kapasitesi, Fe3+-Fe2+ indirgeme kapasitesi, 1,1-difenil-2-pikril-hidrazil radikal (DPPH·) giderme aktivitesi, 2,2´-azino-bis(3-etilbenztiyoazolin-6-sülfonik asit) radikal (ABTS∙+) giderme aktivitesi, total fenolik bileşik miktarı ve total flavonoid bileşik miktarı, toplam betalain miktarı tayini yöntemleri ile berlirlenmiştir. Standart antioksidanlardan BHA, BHT, α-tokoferol ve troloks ile karşılaştırma yapılmıştır. Renk değişimleri için Hunter L*, a*, b* değerleri ölçülerek Hue, Chroma ve Browning İndeks parametreleri hesaplandı. ABTS inhibisyonu %12 pancar tozu ilave edilen örneklerde en yüksek düzeydedir. Total flavonoid miktarı mikrodalga kurutma yöntemiyle elde edilmiş pancar tozlu ekmeklerde 24.74 µg KE/mg daha yüksek bulunmuştur. En yüksek betalain miktarı 75.41 mg/kg mikrodalga ile kurutulmuş örneklerde görülmüştür. En yüksek a* , b*, kroma ve browning indeks değerleri mikrodalga tekniğiyle kurutulan pancar tozu ilave edilmiş ekmeklerde görülmüştür. Pancar tozu ilavesinin ABTS radikali giderme aktivitesi ve total flavonoid miktarını yükselttiği görülmüştür.
- 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.
- MakaleYalnız künye2017Effects of certain drugs on dihydropyrimidine dehydrogenase enzyme purified from bovine liver
Aygul, Imdat; Ozdemir, Hasan; Ciftci, Mehmet
The inhibitory effects of certain drugs on dihydropyrimidine dehydrogenase from the bovine liver have been investigated. Dihydropyrimidine dehydrogenase [5, 6-dihydrouracil: NADP+ oxidoreductase, EC 1.3.1.2; DPD] enzyme was purified from the bovine liver. The purification was performed by preparation of homogenate, ammonium sulphate precipitation, and affinity chromatography. Moreover, some important modifications were made in the purification procedure. Purification of bovine liver DPD enzyme was obtained with a yield of 12.5%. SDS polyacrylamide gel electrophoresis was performed after the purification of the enzyme, and the electrophoretic pattern is discussed in this article. In addition, the effects of certain drugs on bovine liver dihydropyrimidine dehydrogenase enzyme activity were investigated. Oxytetracycline, ciprofloxacin, ceftazidime, cefoperazone, amikacin, ornidazole, metronidazole, cefuroxime, cefepime, ampicillin, and amoxicillin, were used as drugs. All the drugs indicated the inhibitory effects on the enzyme. IC50 values of the drugs were determined by plotting activity % vs [I]. IC50 values of oxytetracycline, ciprofloxacin, ceftazidime, cefoperazone, amikacin, ornidazole, metronidazole, cefuroxime, cefepime, ampicillin, and amoxicillin 0.030, 0.046, 0.140, 0.610,1.820, 2.500, 3.600, 4.330, 4.370, 4.920, and 6.300, mM; the Ki constants were 0.050±0.01,0.090± 0.06, 0.130±0.045, 0.185±0.057, 2.010±0.55, 2.096±1.06, 2.115±1.00, 2.700±0.56, 3.730±1.48, 5.240±1.04, and 9.570±2.84, mM for bovine liver DPD, respectively. Ki constants for dihydropyrimidine dehydrogenase were determined by Lineweaver-Burk graphs. All drugs showed non-competitive inhibition patterns.
- MakaleAçık Erişim2016Investigation of the inhibitory properties of some phenolic standards and bee products against human carbonic anhydrase I and II
Aygul, Imdat; Yaylaci Karahalil, Fatma; Supuran, Claudiu T.
Polyphenols are important secondary products of plants with the potential to inhibit carbonic anhydrases. The aim of this study was to investigate the inhibition effects of various phenolic standards, honey, propolis, and pollen species on human carbonic anhydrase I and II. The inhibition values (IC50) of the phenolics (gallic acid, protocatechuic acid, quercetin, catechin, tannic acid, and chrysin) ranged from 0.009 to 0.32 μg/mL, tannic acid emerging as the best inhibitor. The inhibition values of three different types of honey, heather, rhododendron, and chestnut ranged between 2.32 and 25.10 μg/mL, the chestnut honeys exhibiting the best inhibition. The ethanolic extracts of pollen and propolis exhibited good inhibitory properties, with IC50 values between 0.486 and 3.320 μg/mL. In order to evaluate the phenolic composition of bee products, phenolic profiles and total phenolic contents (TFC) were also measured. The inhibition ranking among the natural products studied was phenolic standards > propolis > pollen > honeys, and inhibition was related to TFC.
- MakaleYayıncıda açık erişim2015Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme
Sarikaya, S. Beyza Ozturk; Sisecioglu, Melda; Cankaya, Murat; Gulcin, Ilhami; Ozdemir, Hasan
Lactoperoxidase (LPO) catalyzes the oxidation of numerous of organic and inorganic substrates by hydrogen peroxide. It has very vital activity in the innate immune system by decreasing or stopping the activation of the bacteria in milk and mucosal secretions. This study's purpose was to investigate in vitro effect of some phenolic acids (ellagic, gallic, ferulic, caffeic, quercetin, p-coumaric, syringic, catechol and epicatechin) on the purified LPO. This enzyme was purified from milk by using different methods such as Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange and Sephadex G-100 gel filtration chromatography. LPO was purified 28.7-fold with a yield of 20.03%. We found phenolic acids have inhibition effects on bovine LPO enzyme to different concentrations. Our study showed lower concentrations of caffeic acid, ferulic acid and quercetin exhibited much higher inhibitory effect on enzyme, so these three of them were clearly a more potent inhibitor than the others were. All of compounds were non-competitive inhibitors.
- 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 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.