Yazar "Taslimi, Parham" seçeneğine göre listele

Listeleniyor 1 - 7 / 7
  • [ X ]
    Öğe
    Novel 1,2,4-triazole-maleamic acid derivatives: synthesis and evaluation as anticancer agents with carbonic anhydrase inhibitory activity
    (Elsevier, 2024) Tapera, Michael; Kekecmuhammed, Huseyin; Tuzun, Burak; Dastan, Sevgi Durna; Celik, Muhammed Safa; Taslimi, Parham; Dastan, Taner
    Hybrid compounds with 1,2,4-triazole ring and a hydrazone moiety were designed and synthesized by amine acylation of uncommon triaminogunidine derivatives using maleic anhydride. Synthesized compounds were characterized by various spectral techniques, including FTIR, 1H NMR, 13C NMR, and HRMS. Furthermore, the proposed structure of TM-2 was resolved by single-crystal X-ray analysis. The compounds were evaluated for their anticancer activity in vitro against the colon cancer cell line HCT116 and the ovarian cancer cell line A2780. Among them, some compounds, TM-3, TM-4, and TM-14, exhibited remarkable antiproliferative activity in the cell line A2780, with IC50 values of 6.11, 5.15, and 5.93 mu M, respectively. Further investigation revealed that these compounds could inhibit cancerous cell growth by inducing an increase in caspase-3 activity. In addition, antioxidant capabilities, interaction with plasmid pBR322 DNA, and inhibitory effects against two physiologically and pharmacologically relevant human carbonic anhydrase (hCA) isoforms, namely hCA I and hCA II, of the synthesized compounds were also assessed. Finally, computational studies, such as DFT calculation, molecular docking, and in silico predictions of ADME/T analysis, were conducted to gain an understanding of the specific reactive sites of the compounds, the binding modes in the active sites, and the pharmacokinetic parameters of the newly synthesized hybrid compounds, which were calculated to establish their drug-likeness properties.
  • [ X ]
    Öğe
    Novel piperazine and morpholine substituted quinolines: Selective synthesis through activation of 3,6,8-tribromoquinoline, characterization and their some metabolic enzymes inhibition potentials
    (Elsevier, 2020) Cakmak, Osman; Okten, Salih; Alimli, Dilek; Ersanli, Cem Cuneyt; Taslimi, Parham; Kocyigit, Umit Muhammet
    Regioselective routes are described for convenient preparation of novel piperazine/morpholine substituted quinoline derivatives at C-3, C-6 and C-8 starting with 3,6,8-tribromoquinoline (6) by nucleophilic substitution via conventional heating or microwave assisted reaction conditions. 3,6,8-Tribromoquinoline (6) was treated with piperazine and morpholine under microvawe irradiation, which selectively furnished 3-mopholinyl and 3-piperazinyl quinoline derivatives 7 and 8 in yields of 58% and 60%, respectively. On the other hand, the activation of benzene cycle of quinoline by nitration of 3,6,8-tribromoquinoline, giving 5-nitro-3,6,8-tribromoquinoline (18) in quantitative yield, was enabled. Then, the bromines at C-6 and C-8 were selectively exchanged by morpholine and piperazine via SNAr reactions. Thus, 6,8-dimopholinylquinoline (22) and 5-nitro-6,8-dipiperazinylquinoline (24), biologically valuable derivatives, were prepared in high yields (82% and 72%, respectively). The synthesized compounds were fully characterizated by H-1 NMR, C-13 NMR, 2D NMR, XRD, HRMS and IR spectra. The novel molecules had effective inhibition profiles against some metabolic enzymes. Also, they have the potential of drug candidates to treat of some diseases including glaucoma, epilepsy, Alzheimer's disease (AD), leukemia, and type-2 diabetes mellitus (T2DM). (C) 2020 Elsevier B.V. All rights reserved.
  • [ X ]
    Öğe
    Novel zinc compound with thiosemicarbazone of glyoxylic acid: Synthesis, crystal structure, and bioactivity properties
    (Elsevier, 2020) Huseynova, Mansura; Farzaliyev, Vaqif; Medjidov, Ajdar; Aliyeva, Mahizar; Taslimi, Parham; Sahin, Onur; Yalcin, Bahattin
    Reaction of zinc nitrate with thiosemicarbazone of glyoxylic acid (H(2)GAT) leads to the formation of the new complex that have been characterized by spectroscopic methods. Crystal structure of the compound Zn3C18H34N18O17S6 (1) was determined using single crystal X-ray diffraction methods. Single crystal X-ray measurements showed that the complex crystallized in a triclinic system with the space group P-1. The structure of complex 1 presents distorted octahedral geometry around the zinc ion centre. In the crystal structure, Zn(II) ion is coordinated by two nitrogen, two oxygen and two sulfur atoms from two different thiosemicarbazone of glyoxylic acid and two oxygen atoms from two different water molecules. Thermogravimetry shows four steps of decomposition in the temperature range 225-990 degrees C. This complex was an inhibitor of butyrylcholinesterase (BChE), cytosolic carbonic anhydride I and II isoforms (hCA I and II) and acetylcholinesterase (AChE) enzymes for complex 1 with Ki values of 0.95 +/- 0.10 mu M for hCA I, 1.54 +/- 0.24 mu M for hCA II, 25.98 +/- 2.44 mu M for BChE, 166.21 +/- 13.63 mu M for alpha-glycosidase and 18.53 +/- 1.36 mu M for AChE, respectively. (C) 2019 Elsevier B.V. All rights reserved.
  • [ X ]
    Öğe
    Synthesis, biological and theoretical properties of crystal zinc complex with thiosemicarbazone of glyoxylic acid
    (Elsevier, 2022) Huseynova, Mansura; Farzaliyev, Vaqif; Medjidov, Ajdar; Aliyeva, Mahizar; Ozdemir, Mucahit; Taslimi, Parham; Zorlu, Yunus
    A new zinc complex with thiosemicarbazone of glyoxylic acid (1) was synthesized with zinc acetate dihy-drate and thiosemicarbazone of glyoxylic acid and crystallized in water. The absolute crystal structure of the complex was defined using the single-crystal X-ray diffraction technique. It was seen in X-ray mea-surements that the complex crystallized in the triclinic system with the P-1 space group. The structure of 1 represents distorted octahedral geometry around the central zinc metal. Zn(II) complex with thiosemi-carbazone of glyoxylic acid was an inhibitor of acetylcholinesterase (AChE), butyrylcholinesterase (BChE), human carbonic anhydrase I and II isoforms (hCA I and II) receptors and the inhibitor constant (Ki) values of the synthesized complex were 38.94 +/- 8.2 mu M for hCA I, 48.62 +/- 11.3 mu M for hCA II, 65.16 +/- 11.4 mu M for BChE and 82.04 +/- 16.0 mu M for AChE, respectively. The molecular docking method was used to show the complex-enzyme interactions. The pharmacokinetic properties of the complex were determined by ADME/Tox predictions and the results obtained showed that the complex could be a potential drug can-didate. (C) 2021 Elsevier B.V. All rights reserved.
  • [ X ]
    Öğe
    Synthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach
    (Elsevier, 2021) Tokali, Feyzi Sinan; Taslimi, Parham; Usanmaz, Hande; Karaman, Muhammet; Sendil, Kivilcim
    In this study, eight new Schiff base derivatives (2a-h) were synthesized and their inhibition activities against Acetylcholinesterase (AChE), Butyrylcholinesterase (BChE), alpha-Glucosidase and Lactoperoxidase (LPO) were investigated. Structures of the synthesized compounds were characterized using H-1 and C-13 nuclear magnetic resonance (NMR), infrared spectroscopy (IR), and high-resolution mass spectrometry (HRMS) spectroscopic methods. AChE was inhibited by these novel Schiff bases (2a-h) in low nanomolar levels, the K-i of which differed between 592.66 +/- 57.04 and 810.78 +/- 84.06 nM. Against BChE, the novel compounds demonstrated Kis varying from 358.31 +/- 37.88 to 577.24 +/- 59.91 nM. Also, these novel Schiff bases effectively inhibited alpha-glucosidase, with K-i values in the range of 1.56 +/- 0.32 to 14.78 +/- 2.57 nM. For LPO, K-i values were in the range of 3.96 +/- 0.37 to 12.75 +/- 0.06 nM. For alpha-glucosidase, the most effective molecules were 2b and 2 g with K-i values of 1.56 +/- 0.32 and 14.78 +/- 2.57 nM, respectively. Molecular docking results showed that the compounds have binding affinity with -5.559,-9.698, -7.606, and -6.971 kcal/mol against LPO, AChE, BChE, and alpha-glucosidase enzyme, respectively. It has been observed that the furan and thiosemicarbazone moieties play an important role in the inhibition of these enzymes. (C) 2020 Elsevier B.V. All rights reserved.
  • [ X ]
    Öğe
    Synthesis, characterization, crystal structure, electrochemical studies and biological evaluation of metal complexes with thiosemicarbazone of glyoxylic acid
    (Pergamon-Elsevier Science Ltd, 2018) Huseynova, Mansura; Taslimi, Parham; Medjidov, Ajdar; Farzaliyev, Vagif; Aliyeva, Mahizar; Gondolova, Gulnar; Sahin, Onur
    Cobalt and nickel nitrates form with thiosemicarbazone of glyoxylic acid (H(2)GAT) complexes of empirical composition Co(C3H4N3O2S)(2)center dot 2H(2)O, Ni(C3H4N3O2S)(2)center dot 2H(2)O and Ni(C3H6N3O2S)(2). X-ray diffraction studies have shown that the Co(HGAT)(2)center dot 2H(2)O, Ni(HGAT)(2)center dot 2H(2)O complexes are mononuclear, in which the coordination around the metal is octahedral, made up of two sulfur atoms, two nitrogen atoms and two oxygen atoms from two ligands. By the interaction of NiCl2 center dot H2O with 2-[2-(aminothioxomethyl)hydrazinyl] acetic acid (H(2)TAA) instead of the expected the metal thiosemicarbazonate complex with the hydrogenated on the azomethine group ligand was obtained. The redox properties of these compounds were also investigated by voltammetry on Pt in dimethylsulfoxide/tetrabutylammonium perchlorate. These thiosemicarbazone of glyoxylic acid derivatives had effective inhibition against alpha-glycosidase, cytosolic carbonic anhydrase I and II isoenzymes, butyrylcholinesterase and acetylcholinesterase. K-i values were found as 26.12-36.58 nM for hCA I, 20.73-40.78 nM for hCA II, 184.30-642.18 nM for AChE, 123.67-342.37 nM for BChE, and 14.66-45.62 nM for alpha-glycosidase. (C) 2018 Elsevier Ltd. All rights reserved.
  • [ X ]
    Öğe
    Synthesis, crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N-salicyloil-N-maleoil-hydrazine as anticholinergic and antidiabetic agents
    (Wiley, 2018) Gondolova, Gulnar; Taslimi, Parham; Medjidov, Ajdar; Farzaliyev, Vagif; Sujayev, Afsun; Huseynova, Mansura; Sahin, Onur
    [Ni(C11H9N2O5)(2)(H2O)(2)]center dot 3(C3H7NO) (1) and [Co(C11H9N2O5)(2)(H2O)(2)]center dot 3(C3H7NO) (2) are synthesized and characterized by elemental analysis, FT-IR spectra, magnetic susceptibility, and thermal analysis. In addition, the crystal structure of Ni(II) complex is presented. Both complexes show distorted octahedral geometry. In 1 and 2, metal ions are coordinated by two oxygen atoms of salicylic residue and two nitrogen atoms of maleic amide residue from two ligands, and two oxygen atoms from two water molecules. In this paper, both compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I, and II, -glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Compounds 1 and 2 had Ki values of 18.36 +/- 4.38 and 26.61 +/- 7.54 nM against hCA I and 13.81 +/- 3.02 and 29.56 +/- 6.52 nM against hCA II, respectively. On the other hand, their Ki values were found to be 487.45 +/- 54.18 and 453.81 +/- 118.61 nM against AChE and 199.21 +/- 50.35 and 409.41 +/- 6.86 nM against BChE, respectively.