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Öğe Erratum: Evaluation of benzaldehyde derivatives as being bovine kidney aldose reductase inhibitors(2023) Şengül, BülentAldose reductase (AR) catalyzes the production of sorbitol from glucose in the polyol pathway, and it is a critical enzyme that causes an aberrant aggregation of sorbitol in insulin- independent tissues, create some problems including retinopathy, neuropathy, and nephropathy. AR inhibition has been shown to be a viable approach for reducing these side effects. The current study aimed to introduce new AR inhibitors to the literature. For this purpose, benzaldehydes were examined as being AR inhibitors. Firstly, the homogenate was prepared from the bovine kidney, then inhibition studies were carried out. It was found that all derivatives inhibited AR. The inhibitory potency of 4- Phenyl benzaldehyde (3) and 2- Bromobenzaldehyde (6), having IC50 values as 0.23 and 1.37 ?M, respectively, was determined higher than standard inhibitor sorbinil. After in vitro inhibition studies, estimated binding energies and binding modes of derivatives with enzyme were predicted by molecular docking. Compound 3 exhibited a maximum docking score of -8,61 kcal/mol. In conclusion, these compounds especially compound 3 may be guiding agents that can be used to synthesize new drug candidate molecules to treat or prevent diabetic complications.Öğe Evaluation of benzaldehyde derivatives as being bovine kidney aldose reductase inhibitors(2023) Şengül, BülentAldose reductase (AR) catalyzes the production of sorbitol from glucose in the polyol pathway, and it is a critical enzyme that causes an aberrant aggregation of sorbitol in insulin- independent tissues, create some problems including retinopathy, neuropathy, and nephropathy. AR inhibition has been shown to be a viable approach for reducing these side effects. The current study aimed to introduce new AR inhibitors to the literature. For this purpose, benzaldehydes were examined as being AR inhibitors. Firstly, the homogenate was prepared from the bovine kidney, then inhibition studies were carried out. It was found that all derivatives inhibited AR. The inhibitory potency of 4- Phenyl benzaldehyde (3) and 2- Bromobenzaldehyde (6), having IC50 values as 0.23 and 1.37 ?M, respectively, was determined higher than standard inhibitor sorbinil. After in vitro inhibition studies, estimated binding energies and binding modes of derivatives with enzyme were predicted by molecular docking. Compound 3 exhibited a maximum docking score of -8,61 kcal/mol. In conclusion, these compounds especially compound 3 may be guiding agents that can be used to synthesize new drug candidate molecules to treat or prevent diabetic complications.Öğe Evaluation of Inhibition Effects of Some Cardiovascular Therapeutics on Human Erythrocyte Carbonic Anhydrase Isoenzymes(2018) Kılınç, Namık; Alım, Zuhal; Şengül, Bülent; İşgör, Mehmet Mustafa; Beydemir, ŞükrüCarbonic anhydrase enzyme plays a vital role in metabolic events such as acid-base regulation and respiration. Inour research, it is tried to determine the inhibitory influences of the cardiovascular therapeutics esmololhydrochloride, amiodarone hydrochloride and lidocaine hydrochloride on human erythrocytes carbonic anhydrases(hCA I and II). In accordance with this purpose, carbonic anhydrase isoenzymes were purified from humanerythrocytes by using affinity chromatography method. Enzyme purity was checked by SDS-PAGEelectrophoresis method. After the carbonic anhydrase enzymes were purified, the inhibitory affects ofcardiovascular therapeutics on these enzymes, using esterase activity, which is the method of measuring in vitroactivity, were examined. The three cardiovascular therapeutics dose-dependently decreased activity of hCAs. IC50values of amiodarone hydrochloride, esmolol hydrochloride and lidocaine hydrochloride were found to be,respectively, 0.91 mM, 5 mM, 5.8 mM for hCA-I and 0.41 mM, 3.5 mM, and 6.36 mM for hCA-II. Our resultsproved that, under in vitro conditions, cardiovascular therapeutics significantly inhibit human CA-I and IIactivities. So, irregular use of these medicines may cause serious adverse effects in terms of human health.Öğe Exploring the Potential of Isoindole-1,3-Dione Derivatives as Novel Inhibitors of Aldose Reductase: An In Silico and In Vitro Insight into Therapeutic Strategies for Diabetic Complications(John Wiley and Sons Inc, 2024) Şengül, Bülent; Gündoğdu, Özlem; Kilinç, Namık; Kishali, NurhanThis study explores the potential of isoindole-1,3-dione derivatives as novel inhibitors of aldose reductase (AR), focusing on their in silico and in vitro effects for therapeutic strategies against diabetic complications. Aldose reductase, a critical enzyme in the polyol pathway, plays a significant role in glucose metabolism and has been linked to diabetic complications. In this comprehensive study, isoindole-1,3-dione derivatives were synthesized and evaluated for their inhibitory effects on the recombinant human AR enzyme. The compounds’ inhibitory activities were measured both in vitro and through in silico techniques, employing molecular docking and free binding energy calculations and ADME studies. The newly synthesized compounds demonstrated varied inhibitory effects, with ethyl and phenyl substituents at specific positions enhancing inhibitory activity. Notably, compounds with carboxylic acid derivatives exhibited potent inhibitory effects, especially compound 6 with an IC50 value of 1.649 ?M. In conclusion, this study provides valuable insights into the inhibitory potential of isoindole-1,3-dione derivatives against AR, suggesting their potential therapeutic application in mitigating diabetic complications. The combination of experimental and computational approaches offers a comprehensive understanding of the compounds’ interaction mechanisms and pharmacokinetic profiles, supporting their further exploration as antidiabetic agents. © 2024 Wiley-VCH GmbH.Öğe Gökkuşağı Alabalığı (Oncorhynchus mykiss) İşletmelerinde Bazı Antioksidan Enzim Aktivitelerinin Ağır Metal İnhibisyonlarının Araştırılması(2018) Şengül, Bülent; Önalan, Şükrü; Demir, YelizEndüstriyel, tarımsal ve ticari kimyasalların, sucul ekosistemlerde meydana getirdiği kirlilik, giderek artanciddi bir problemdir. Çevresel kirleticiler, sucul organizmalarda çeşitli zararlı etkilere neden olur. Balıklar, suculorganizmalar arasında ağır metallere en çok maruz kalan türlerdir. Ağır metallerin balıklarda birikmesi balıkhastalıkları konusunda önemli bir sorun olmanın yanında, oksidatif stres sebebi olan reaktif oksijen türlerinin(ROT) artmasına da neden olmaktadır. Biyolojik sistemlerde oksidatif strese bağlı reaktif oksijen türlerindekiartış antioksidan savunma sistemlerinde hasara yol açar. Bu çalışmanın amacı gökkuşağı alabalık çiftliklerindeüretimi yapılan balıkların karaciğer, böbrek ve solungaç dokularındaki bazı antioksidan enzim aktiviteleri ileağır metal iyonlarından kaynaklanan su kirliliği arasındaki ilişkiyi ortaya koymaktır. Bu amaçla; Suörneklerindeki ağır metal iyonlarının (Zn, Fe, Cu, Ni, Co, Hg, As, Mn) seviyeleri belirlenerek, bu iyonlarınbalıklardan alınan kalp, karaciğer ve solungaç dokularındaki antioksidan enzimlerin (Süperoksid dismutaz(SOD), Katalaz (CAT), Glutatyon redüktaz (GR), Glutatyon S-transferaz (GST), Glutatyon peroksidaz (GPx))aktiviteleri üzerine etkileri incelenmiştir.Öğe Koyun Karaciğerinden Alkol Dehidrogenaz: Saflaştırma, Karakterizasyon, ve Bazı Antibiyotiklerin Etkileri(2017) Demir, Yeliz; Şengül, Bülent; Ergun, Bülent; Beydemir, ŞükrüAlkol dehidrogenaz (ADH), her bir alt biriminin bir Zn2 metal içeren katalitik alana ve bir kofaktör bağlama alanına sahip olduğu dimerik bir enzimdir. Bu enzim, alkolü, aldehide dönüştürür. Bu makale koyun karaciğerinden alkol dehidrogenazın saflaştırılması, karakterizasyonu enzimin aktivitesi üzerine bazı antibiyotiklerin in vitro ekilerine odaklanmaktadır. ADH, DEAE-Sephadex A-50 iyon değişim kromatografisi ve Sephadex G-100 jel filtrasyon kromatografisi vasıtasıyla koyun karaciğerinden 0.5 U mg-1 protein spesifik aktivite ve yaklaşık olarak 52.03-kat saflaştırıldı. Enzimin alt birim ve doğal hallerinin molekül kütleleri jel filtrasyon kromatografisi ve SDS-PAGE ile sırasıyla 38.16 kDa ve 80.49 kDa olarak belirlendi. ADH'ın optimum iyonik şiddeti, sıcaklığı ve pH'sı sırasıyla 400 mM, 40C ve 10.5 idi. Antibiyotiklerin inhibitor etkileri çeşitli konsantrasyonlarda denendi. Kanamisin sülfat, amikasin sülfat, gentamisin, linkomisin ve klindamisin için IC değerleri sırasıyla, 43.31, 36.47, 20.38, 18.73 ve 1.31 mM olarak bulundu
