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Öğe 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, YakupAldose 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.Öğe Kalp yetmezliği olan hastalarda poliamin sentez yolundaki enzim düzeylerinin incelenmesi(Cumhuriyet Üniversitesi, 2017) Demir, Yeliz; Demirpençe, ÖzlemKalp yetmezliği (KY) kalbin, yaşam fonksiyonları açısından insan vücudunun ihtiyaçlarına uygun kanı pompalayamadığı bir klinik sendromdur. Yeni geliştirilen tedaviler ile mortalitenin ve morbiditenin azalmasına rağmen, KY hala sık görülen ve ciddi seyreden kardiyovasküler hastalıklardan biridir. Bu nedenle KY'nin seyrinde biyokimyasal yolakların incelenmesi önemini hala korumaktadır. Poliaminler (PA) protein kinazların hücre döngüsündeki aktivitesinde, transkripsiyon faktörlerinin aktivitelerinde, translasyon ve transkripsiyonda önemli rol oynarlar. Bu çalışmada KY olan hastalarda biyokimyasal belirteç olarak serumdaki PA konsantrasyonları değerlendirildi. Bu çalışmada, kardiyoloji servisine başvuran toplam 60 birey değerlendirildi. Hasta grubunda 30 KY hastası, kontrol grubunda ise KY hastalığı olmayan 30 birey vardı. Her iki grupta arjinaz, ornitin, ornitin dekarboksilaz, arjinin dekarboksilaz ve agmatinazın serum düzeyleri değerlendi. Kontrol grubundaki bireylerle karşılaştırıldığında, KY hastalarının serum arjinaz (P=0,001), ornitin (P=0,001), ornitin dekarboksilaz (P=0,019) düzeyleri arasındaki fark anlamlı olarak bulundu (p<0,05). Her iki gruptaki bireylerin arjinin dekarboksilaz (P=0,395) ve agmatinaz (P=0,053) düzeyleri karşılaştırıldığında ise, gruplar arası fark istatistiksel olarak anlamlı bulunmadı (p >0,05). Sonuç olarak, elde edilen veriler, KY hastalarında serum arjinaz, ornitin ve ornitin dekarboksilaz düzeylerinde KY olmayan bireylere göre farklılık olduğunu göstermiştir. Bazı PA'lerin konsantrasyonundaki artışın KY progresyonuyla ilişkili olabileceğine inanıyoruz ve bu nedenle, konuyla ilgili tüm PA'lerin ölçümlerini içeren daha kapsamlı çalışma yapılması gerektiğini düşünüyoruz. Anahtar kelimeler: Kalp yetmezliği, poliaminler, arjinaz, ornitin, arjinin dekarboksilaz, ornitin dekarboksilaz, agmatinazÖğe Some old 2-(4-(Aryl)- thiazole-2-yl)-3a,4,7,7a-tetrahydro-1H-4,7- tethanoisoindole-1,3(2H)-dione derivatives: Synthesis, inhibition effects and molecular docking studies on Aldose reductase and ?-Glycosidase(2021) Taslimi, Parham; Demir, Yeliz; Duran, Hatice Esra; Koçyiğit, Ü.Muhammet; Tuzun, Burak; Aslan, Osman Nuri; Ceylan, MustafaUtilizing the simple chromatic techniques, Aldose reductase (AR) was derived from sheep liver. In addition, ?-glycosidase from Saccharomyces cerevisiae was used as the enzyme. It was determined the interactions between compounds and the enzymes. Molecular docking method used to compare biological activity values of molecules against enzymes. In the current study, the inhibition effect of synthetic isoindol-substitute thiazole derivatives (3a-f) on AR, and ?-glycosidase enzymes was studied. In the thiazole series, compound 3b (Ki: 9.70±4.72 ?M) showed a maximum inhibitory impact towards AR while compound 3f (Ki: 44.40±17.18 ?M) showed a lowest inhibitory impact towards AR. It was investigated potent inhibition profiles with Ki values in the range of 24.54±6.92–44.25±10.34 ?M against ?-glycosidase. Theoretical results were found consistent with experimental results. Acting as antidiabetic agents, these compounds have the potential to be the selective inhibitor of ?-glycosidase and AR enzymes. The biological activities of the studied molecules against AR and ?-glycosidase enzymes will be compared with molecular docking method. ADME analysis of the molecules will be done.Öğe Some old 2-(4-(Aryl)- thiazole-2-yl)-3a,4,7,7a-tetrahydro-1H-4,7-tethanoisoindole-1,3(2H)-dione derivatives: Synthesis, inhibition effects and molecular docking studies on Aldose reductase and α-Glycosidase(Sivas Cumhuriyet Üniversitesi, 2021) Taslımı, Parham; Demir, Yeliz; Duran, Hatice Esra; Koçyiğit, Ümit Muhammet; Tüzün, Burak; Aslan, Osman Nuri; Ceylan, MustafaUtilizing the simple chromatic techniques, Aldose reductase (AR) was derived from sheep liver. In addition, α-glycosidase from Saccharomyces cerevisiae was used as the enzyme. It was determined the interactions between compounds and the enzymes. Molecular docking method used to compare biological activity values of molecules against enzymes.In the current study, the inhibition effect of synthetic isoindol-substitute thiazole derivatives (3a-f) on AR, and α-glycosidase enzymes was studied. In the thiazole series, compound 3b (Ki: 9.70±4.72 M) showed a maximum inhibitory impact towards AR while compound 3f (Ki: 44.40±17.18 M) showed a lowest inhibitory impact towards AR. It was investigated potent inhibition profiles with Ki values in the range of 24.54±6.92–44.25±10.34 M against α-glycosidase. Theoretical results were found consistent with experimental results.Acting as antidiabetic agents, these compounds have the potential to be the selective inhibitor of α-glycosidase and AR enzymes. The biological activities of the studied molecules against AR and α-glycosidase enzymes will be compared with molecular docking method. ADME analysis of the molecules will be done.Öğe Synthesis of 1,3-Disubtitituted Tetrahydropyrimidinium Salts and Determination of Their Biological Properties and Molecular Docking(Wiley-V C H Verlag Gmbh, 2024) Karaca, Emine Ozge; Gurbuz, Nevin; Demir, Yeliz; Tuzun, Burak; Ozdemir, Ismail; Gulcin, IlhamiSeveral of 3,4,5,6-tetrahydropyrimidinium salts with 1-methyl functionalization are produced. By using techniques for 1H-NMR, 13C-NMR, and IR spectroscopy, all compounds were investigated. Additionally, these compounds' abilities to block enzymes were looked into. They had a highly effective inhibitory effect on the isoenzymes of carbonic anhydrases I and II, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE). Ki values were found in the range of 57.43 +/- 7.09-170.09 +/- 50.91 nM for AChE, 7.19 +/- 0.42-69.08 +/- 2.44 nM for BChE, and 46.48 +/- 5.74-203.38 +/- 46.15 nM for hCA I, and 30.19 +/- 4.03-171.96 +/- 30.27 nM for hCA II. As a result, 1,3-disubtitituted tetrahydroprimidinium salts exhibited potent inhibition profiles toward indicated metabolic enzymes. One of the most important methods for designing and creating novel, potent medications to treat Alzheimer's disease (AD) worldwide is the synthesis and discovery of new AChE and BChE inhibitors. The activities of synthesized 3,4,5,6-tetrahydropyrimidinium salts were compared against various proteins that are crystal structure of AChE (PDB ID: 4 M0E), crystal structure of BChE (PDB ID: 5NN0), crystal structure of hCA I (PDB ID: 2CAB), and crystal structure of hCA II (PDB ID: 3DC3), and then the drug properties of these molecules were examined. In this study, we have designed and synthesized a series of 1,3-disubtitituted tetrahydropyrimidinium salts were synthesized and characterized by IR and NMR spectra. These compounds were evaluated against the AChE, BChE, hCA I and hCA II enzymes. These compounds showed good enzyme inhibition profiles. The activities of the investigated 1,3-disubstituted tetrahydropyrimidinium salts were compared to the theoretical calculations results using molecular docking. image
