Ozturk S

References (2)

Title : Experimental and Theoretical Biological Probing of Schiff Bases as Esterase Inhibitors: Structural, Spectral and Molecular Insights - Raza_2023_Molecules_28_5703
Author(s) : Raza MA , Mumtaz MW , Ozturk S , Latif M , Aisha , Ashraf A , Dege N , Dogan OE , Agar E , Rehman SU , Noor A
Ref : Molecules , 28 :5703 , 2023
Abstract : The present study was designed to evaluate the in vitro and in silico potential of the Schiff bases (Z)-4-ethoxy-N-((5-nitrothiophen-2-yl)methylene)benzenamine (1) and (Z)-2,4-diiodo-6-((2-methyl-3-nitrophenylimino)methyl)phenol (2). These Schiff bases were synthesized according to a reported method using ethanol as a solvent, and each reaction was monitored on a TLC until completion of the reaction. The structures of both compounds were elucidated using spectroscopic techniques such as UV-Vis, FTIR, (1)H NMR and (13)C NMR. Molecular structure was determined using single-crystal XRD, which revealed that compounds 1 and 2 were monoclinic and triclinic, respectively. Hirshfeld surface analysis (HS) and 2D fingerprint plots were used to determine the intermolecular interactions along the contact contribution in the crystalline molecules. The structures of both compounds were optimized through a hybrid functional method B3LYP using the 6-31G(d,p) basis set, and various structural parameters were studied. The experimental and theoretical parameters (bond angle and bond length) of the compounds were compared with each other and are in close agreement. The in vitro esterase potential of the synthesized compounds was checked using a spectrophotometric model, while in silico molecular docking studies were performed with AutoDock against two enzymes of the esterase family. The docking studies and the in vitro assessment predicted that such molecules could be used as enzyme inhibitors against the tested enzymes: acetylcholine esterase (AChE) and butyrylcholine esterase (BChE).
ESTHER : Raza_2023_Molecules_28_5703
PubMedSearch : Raza_2023_Molecules_28_5703
PubMedID: 37570673

Title : Kinetic Studies, Antioxidant Activities, Enzyme Inhibition Properties and Molecular Docking of 1,3-Dihydro-1,3-Dioxoisoindole Derivatives - Yakan_2023_Acta.Chim.Slov_70_29
Author(s) : Yakan H , Ozturk S , Uyar Tolgay E , Yenigun S , Marah S , Doruk T , Ozen T , Kutuk H
Ref : Acta Chim Slov , 70 :29 , 2023
Abstract : The acid catalyzed hydrolysis of the N-(p-substitutedphenyl) phthalimides in three different acids was investigated at 50.0+/-0.1 degreesC. Two different antioxidant activity tests as DPPH* and ABTS*+ scavenging activities, and three various enzyme inhibition activity tests as urease, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibition activities, were applied. Compound 3c (2.03 microg/mL ) has higher antioxidant activity than other compounds and standards according to DPPH test. In AChE assay, compounds 3a and 3b (13.13 and 9.59 microg/mL) has higher enzyme inhibition activity than the standard Galantamine (14.37 microg/mL). In BChE and urease tests, all compounds (6.84-13.60 and 10.49-17.73 microg/mL) have higher enzyme inhibition activity than the standard Galantamine (49.40 microg/mL) and thiourea (26.19 microg/mL), respectively. The molecule interaction for each of the three compounds with the active sites of AChE, BChE, and urease enzymes was examined via molecular docking simulations.
ESTHER : Yakan_2023_Acta.Chim.Slov_70_29
PubMedSearch : Yakan_2023_Acta.Chim.Slov_70_29
PubMedID: 37005614