Yazar "Ismayilov, Rayyat Huseyn" seçeneğine göre listele

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    Copper(II) monohelix complexes with pyrazine-modulated long-chain oligo-α-aminopyridine ligand: synthesis, crystal structures, and bioactivity studies
    (Elsevier, 2025) Ismayilova, Sabina Zahid; Ismayilov, Rayyat Huseyn; Tagiyev, Dilgam Babir; Senol, Halil; Medjidov, Ajdar Akber; Huseynova, Mansura Teyfur; Yalcin, Bahattin
    Using the pyrazine-modulated pentapyridyltetraamine ligand N-2,N-2 '-(pyridine-2,6-diyl)bis(N-6-(pyrazin-2-yl)pyridine-2,6-diamine) H4N9-2pz, three new mononuclear complexes [Cu(H4N9-2pz)](NO3)(2)center dot(CH3CN) 1, [Cu(H4N9-2pz)]Cl-2 center dot 2(H2O) 2 and [Cu(H3N9-2pz)] (CH3COO)center dot 2.5(H2O) 3 have been synthesized, structurally characterized, and their bioactivity properties studied. In vitro analysis of complexes 1-3 revealed that they inhibited AChE and BChE more effectively than the widely available inhibitor tacrine (IC50: 123.58 +/- 6.80 and 146.18 +/- 7.91 mu M). Additionally, their IC50 values for AChE and BChE ranged from 32.87 to 68.15 and 14.60 to 31.68 mu M, respectively. The g(
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    Öğe
    Synthesis, structure, and properties of a polymeric copper(II) complex with anion of maleic acid
    (Springer, 2025) Guliyeva, Esmira Arif Aga; Mejidov, Ajdar Akper; Ismayilov, Rayyat Huseyn; Rustam, Malahat Bagiyeva; Yalcin, Bahattin; Ozturkkan, Fureya Elif; Sahin, Onur
    A new polymeric copper(II)-maleato complex, used as a dicarboxylate ligand, was synthesized {Na2[Cu(C4H2O4)2]2H2O}n (1). The resulting complex was characterized by elemental analysis, infrared and UV-visible spectroscopy, and X-ray crystallography. Spectroscopic data indicate that the maleato ion coordinates in a chelating bidentate mode, creating a distorted square planar coordination environment around Cu(II). X-ray crystallography confirmed the formulation (1) and revealed that the central Cu(II) ion is in a distorted square planar. The maleato ion acts as a bidentate chelator, coordinating through two carboxylate oxygens to form a stable four-membered ring. This study extends our understanding of the coordination behavior of pi-conjugated dicarboxylic acids with transition-metal ions. Molecular docking studies demonstrated that the polymeric copper(II)-maleic acid complex exhibited strong binding affinity toward B-DNA (1BNA), with a binding energy of - 10.2 kcal/mol and multiple stable hydrogen bond interactions. The molecular docking results demonstrated that the polymeric copper(II) complex with maleic acid forms conventional hydrogen bonds with B-DNA. Specifically, interactions were observed with guanine and cytosine bases: the O2 atom of cytosine (DC21), the O4 ' atom of guanine (DG24), and the hydrogen atoms of guanine residues DG2, DG4, and DG22. The hydrogen bond distances (2.10-2.89 & Aring;) confirm the stability of these interactions. Moreover, several of these interactions are located within or near the minor groove of DNA, indicating a groove-binding mode. In addition, the complex exhibits an intramolecular hydrogen bond that stabilizes its conformation during binding.
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    Öğe
    Vanadyl (III)-(E)-N′-(3,5-di-tert-butyl-2-hydroxybenzylidene)-nicotinohydrazide complex: Synthesis, characterization and in vitro and in silico cholinesterase and α-glucosidase inhibition studies
    (Pergamon-Elsevier Science Ltd, 2025) Fatullayeva, Perizad Amrulla; Medjidov, Ajdar Akper; Senol, Halil; Tagiyev, Dilgam Babir; Ismayilov, Rayyat Huseyn; Sahin, Onur; Khrustalev, Victor Nikolaevic
    A new ligand N-nicotinoyl-N '-(3,5-ditertbuthyl-2-hydroxy)benzylidene hidrazine (H2L) was synthesized and a complex [VO(L)CH3O & sdot;CH3OH] with this ligand was obtained and their structures investigated by X-ray crystallography. It was found that the methanol molecule in the complex is easily exchanged for a pyridine molecule. The effects of H2L and [VO(L)CH3O CH3OH] complexes against AChE, BChE and alpha-glucosidase enzymes were investigated using Ellman and Tao methods and the results were calculated as IC50 and Ki. Both compounds demonstrated effective inhibition of all three enzymes, with varying degrees of potency. For AChE, H2L exhibited the lowest IC50 value (8.45 mu M, r2 = 0.993) and a Ki of 5.53 +/- 0.73 mu M, outperforming both its vanadium complex (IC50 = 10.61 mu M, Ki = 7.38 +/- 1.14 mu M) and the reference drug tacrine (IC50 = 13.75 mu M, Ki = 11.90 +/- 1.01 mu M). Additionally, Molecular docking studies were performed to elucidate the possible inhibition mechanisms and binding modes of the ligand (H2L) and its vanadium complex [VO(L)(CH3O)& sdot;CH3OH] against three target enzymes: acetylcholinesterase (AChE, PDB ID: 4EY7), butyrylcholinesterase (BChE, PDB ID: 6EQP), and alpha-glucosidase (alpha-Glu, PDB ID: 3WY1). To achieve a more accurate prediction of ligand-protein interactions and account for conformational flexibility, Induced Fit Docking (IFD) protocols were employed. These two complexes were studied in vitro and in silico and it was determined that they may be used for drug design.