Yazar "Yakali, Gul" seçeneğine göre listele

Listeleniyor 1 - 4 / 4
  • Küçük Resim Yok
    Öğe
    Imidazol-2-Ylidene-Silver(I) Complexes Bearing 4-Acetylphenyl Side Arm: Design, Synthesis, Characterization, Crystal Structure, and Inhibitory Properties Against Some Metabolic Enzymes
    (Wiley, 2025) Demirci, Ozlem; Demir, Yeliz; Gok, Yetkin; Yakali, Gul; Taskin-Tok, Tugba; Muhammed, Muhammed Tilahun; Aktas, Aydin
    Herein, the synthesis of silver(I)-N-heterocyclic carbene (Ag(I)NHC) complexes is presented. These complexes were synthesized from imidazolium salts and silver oxide via the deprotonation method. Ag(I)NHC complexes were characterized using various spectroscopic and analytical techniques, including FTIR, NMR, and elemental analysis. The single crystal structures of the complexes 1e and 1g were illuminated through x-ray crystallography. The study demonstrates that the geometrical characteristics of both complexes closely match those of previously described complexes with a comparable ligand structure. Acetylcholinesterase (AChE) inhibitors prevent the excessive breakdown of acetylcholine by acting on acetylcholinesterase in its neurotransmission. In this way, they help to improve cognitive functions in patients with AD. On the other hand, human carbonic anhydrase inhibitors (CAIs) have been used clinically for many years as antiepileptic, antiglaucoma, antimetastatic, antitumor, and diuretic agents. In this study, the enzyme inhibition abilities of seven imidazol-2-ylidene-silver(I) complexes bearing 4-acetylphenyl side arm were examined against AChE and hCAs. These molecules exhibited a highly potent inhibition effect on AChE and hCAs (Ki values are in the range of 16.27 +/- 1.81 to 130.79 +/- 11.98 nM for AChE, 13.22 +/- 1.88 to 182.14 +/- 33.93 nM for hCA I, and 12.72 +/- 1.99 to 62.36 +/- 9.21 nM for hCA II). Novel imidazol-2-ylidene-silver(I) complexes bearing 4-acetylphenyl side arms 1a-g displayed efficient inhibitory profiles for the examined metabolic enzymes. Docking was additionally performed to investigate the interactions of the current complexes 1a-g with hCA I, hCA II, and AChE proteins. It has been determined that compound 1d has activity against all the tested proteins, with the most effective interaction observed with hCA I. The pharmacokinetic properties of the three top potent complexes for each target against the related proteins were also examined using the SwissADME and pkCSM web tools. In the meantime, the stabilities of the complexes with the highest binding potential according to the docking study were assessed through molecular dynamics simulation. The AChE-1a complex was found to be the one with relatively high stability. Also, further energy computations were made by using the MD simulation results. The compounds have been estimated to bind strongly with their targets.
  • Küçük Resim Yok
    Öğe
    The palladium-based complexes bearing 1,3-dibenzylbenzimidazolium with morpholine, triphenylphosphine, and pyridine derivate ligands: synthesis, characterization, structure and enzyme inhibitions
    (Cell Press, 2022) Aktas, Aydin; Yakali, Gul; Demir, Yeliz; Gulcin, Ilhami; Aygun, Muhittin; Gok, Yetkin
    The palladium-based complexes bearing N-heterocyclic carbene (NHC) ligand have long attracted attention as active catalysts for many catalytic reactions. Recently, the biological activities of these complexes, which are stable to air and moisture, have also been wondered. With the aim, we report the synthesis of a series of (NHC) Pd(Br2)(L) complexes (NHC: 1,3-dibenzylbenzimidazolium, L: morpholine, triphenylphosphine, pyridine, 3-chloropyridine, and 2-aminopyridine). All complexes were characterized by NMR (1H and 13C), FTIR spectroscopic and elemental analysis techniques. In addition, the single crystal structures of the complex 3, 4, and 6 were determined through single crystal x-ray crystallographic method. Furthermore, the carbonic anhydrase I and II isoenzymes (hCAs) and acetylcholinesterase (AChE) inhibition effects of these palladium-based complexes bearing NHC ligand were investigated. They showed highly potent inhibition effect with Ki values are between 10.06 +/- 1.49-68.56 +/- 11.53 nM for hCA I isoenzyme, 7.74 +/- 0.66 to 49.39 +/- 6.50 nM for hCA II isoenzyme and 22.83 +/- 3.21 to 64.09 +/- 9.05 nM for AChE enzyme.
  • Küçük Resim Yok
    Öğe
    Pentafluorobenzyl-substituted benzimidazolium salts: Synthesis, characterization, crystal structures, computational studies and inhibitory properties of some metabolic enzymes
    (Elsevier, 2022) Hamide, Mahmut; Gok, Yetkin; Demir, Yeliz; Yakali, Gul; Tok, Tugba Taskin; Aktas, Aydin; Sevincek, Resul
    This work contains the synthesis and characterization of the pentafluorobenzyl-substituted benzimidazolium salts which N -heterocyclic carbene (NHC) precursors. All compounds were characterized by using 1 H, 13 C, and 19 F NMR, FT-IR spectroscopy, and elemental analysis techniques. All the spectroscopy and elemental analysis data fully confirm the proposed formulas. In the synthesized compounds, the molecular structures of compounds 1-(2-methylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1b ), 1-(4-methylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1d ) and 1-(4-trifluoromethylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1f ) were enlightened by single crystal X-ray diffraction studies. After enzyme inhibition study, a new series of pentafluorobenzyl-substituted NHC precursors were determined to be highly potent inhibitors for acetylcholinesterase (AChE) enzyme and carbonic anhydrases (hCAs) isoenzymes. K i values were found in the range of 7.20 +/- 1.31 to 28.26 +/- 5.72 nM for AChE , 10.25 +/- 0.93 to 40.93 +/- 3.89 nM toward hCA I as pervasive metal containing enzymes present in prokaryotes and eukaryotes, and 3.33 +/- 0.15 to 58.22 +/- 6.99 nM for hCA II as the key enzyme promising strategy for the treatment of neurological disorders such as Alzheimer's disease. The molecular docking study performed for compounds had higher potential inhibitory properties involved in a novel series of pentafluorobenzyl-substituted NHC precursors based on the binding energy and interaction types against AChE and hCAs. (c) 2022 Elsevier B.V. All rights reserved.
  • Küçük Resim Yok
    Öğe
    Platinum (II) N-heterocyclic carbene complexes: Synthesis, characterization and cytotoxic properties
    (Wiley, 2019) Karaca, Emine Ozge; Ciftci, Osman; Ozdemir, Ilknur; Yakali, Gul; Aygun, Muhittin; Gurbuz, Nevin; Ozdemir, Ismail
    Platinum (II) complexes bearing N-heterocyclic carbene (NHC) ligands have been widely used in catalytic chemistry, but there are very few reports of biological properties of this type of complexes. A series of [PtCl2(NHC)(PEt3)] complexes were synthesized. The structures of all compounds were characterized by H-1-NMR, C-13-NMR, IR and elemental analysis techniques, which supported the proposed structures. The single crystal structures of complexes 1a and 1e were determined. The title complexes show slightly distorted square-planar coordination around the platinum (II) metal center. The cytotoxic properties of the platinum (II)-NHC complexes have been assessed in various human cancer lines, including cisplatin-sensitive and resistant cells. IC50 values of these four complexes were determined by the MTS-based assay on three human cell lines-brain (SHSY5Y), colon (HTC116) and liver (HEP3B). These complexes have been highlighted cancer therapeutic agent with unique structures and functions.