Yazar "Kose, Leyla Polat" seçeneğine göre listele

Listeleniyor 1 - 6 / 6
  • Küçük Resim Yok
    Öğe
    Evaluation of Antioxidant Capacity, Anticholinergic and Antidiabetic Activities, and Phenolic Ingredients of Asphodelus aestivus by LC-MS/MS
    (Wiley-V C H Verlag Gmbh, 2024) Kose, Leyla Polat
    Herein, it was aimed to evaluate three different extracts of the plant Asphodelus aestivus in terms of their antioxidant capacity, total phenolic content, flavonoid profile, and anticholinergic and antidiabetic activity. In addition, the phenolic content of the A. aestivus extracts was determined by liquid chromatography-mass spectrometry/mass spectrometry. The results obtained in the antioxidant studies were checked against butylated hydroxyanisole, butylated hydroxytoluene, Trolox, and alpha-tocopherol antioxidants, which are reference standards. The half-maximal inhibition concentration (IC50) values of A. aestivus for 1,1-diphenyl-2-picryl-hydrazyl and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) removal activity were 245.015-285.851 and 285.818-371.563 mu g/mL, respectively. Then, the reducing impact of A. aestivus extracts was evaluated by the cupric ion (Cu2+), ferric ion (Fe3+), and Fe3+-TPTZ reducing capabilities. Moreover, 0.058, 0.064, and 0.100 mu g of gallic acid equivalent of phenolic and 0.500, 1.212, and 2.074 mu g of quercetin equivalent of flavonoid contents were determined from 1 mg of ethanol, water, and water-ethanol extracts, respectively. For water-ethanol, ethanol, and water extracts of A. aestivus, IC50 values of 0.062 +/- 0.0001, 0.068 +/- 0.0002, and 0.090 +/- 0.0001 mu g/mL against acetylcholinesterase, respectively, were calculated. In addition, against the enzyme alpha-glucosidase IC50 values of 16.376 +/- 0.2216, 18.907 +/- 0.3004, and 24.471 +/- 0.4929 mu g/mL, respectively, were calculated. Extracts showed considerable biological activities thanks to the important molecules they contain.
  • Küçük Resim Yok
    Öğe
    Identification of hCA I, hCA II, AChE and BChE Inhibitory Properties of Some Norcantharimide Derivatives; Molecular Docking, SAR and in silico ADME Studies
    (Wiley-V C H Verlag Gmbh, 2024) Kose, Leyla Polat; Kose, Aytekin
    (3aR,4S,7R,7aS)-2-Alkyl/aryl-3a,4,7,7a-tetrahydro-1H-4,7-epoxyisoindole-1,3(2H)-diones, which are norcantharimide derivatives, were synthesized and their effects on carbonic anhydrase I (hCA I) and II (hCA II), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibitory activity were investigated. For enzyme activity studies, hCA I and II isoenzymes purified from human erythrocytes and the commercially available enzymes AChE and BChE, which are both markers and significantly affect the known symptoms of Alzheimer's disease, were used. The two derivatives exerted efficient inhibition with IC50=4.530 nM (Ki=4.483) and 4.426 nM (Ki=4.696) against hCA I and with IC50=3.825 nM (Ki=3.854) and 3.457 nM (Ki=3.292) against hCA II, respectively. The another two derivatives exerted considerable inhibition with IC50=0.526 nM (Ki=0.224) and 0.575 nM (Ki=0.292) against AChE and with IC50=0.135 nM (Ki=0.057) and IC50=0.180 nM (Ki=0.070) against BChE, respectively. The compounds showed activity at the nanomolar level. These remarkable inhibition results were compared with those of standard inhibitors (acetazolamide for hCA I and II and tacrine for AChE and BChE) of each enzyme, reported, and graphed. In addition, molecular docking studies were carried out by in silico methods and the structure-activity relationship was discussed. The poses of compound 4 c are presented along with the ligand-receptor interaction against all metabolic enzymes. Inhibition activity studies of some norcantharimide derivatives were carried out on hCA I and II, AChE, and BChE enzymes. It was found that the inhibition results had values that were similar to the standards. In addition, molecular docking studies of the N-Ph-norcantharimide derivative were carried out and the structure-activity relationship was elucidated. image
  • Küçük Resim Yok
    Öğe
    An Insight into the Asymmetric Resolution of 1-Aminoindane Derivatives
    (Wiley-V C H Verlag Gmbh, 2023) Akincioglu, Akin; Akbaba, Yusuf; Kose, Leyla Polat; Goksu, Suleyman
    Compounds with 1-aminoindane motif exhibit vital biological activities in the central nervous system. Therefore, it is very important to synthesize new compounds with this moiety and to obtain them in high enantiopurity. In this study, novel substituted 1-aminoindane derivatives were synthesized, and their asymmetric resolutions were carried out. Accordingly, the reduction of 1-indanones with NaBH4, conversion of alcohols to azides via an alternative Mitsunobu reaction followed by reduction of azides afforded (+/-)-1-aminoindane hydrochloride or hydrobromide salts. Amine salts were converted into their free amines by using excess amount of Et3N and then in situ occurred free (+/-)-amines were reacted with (R)-O-acetylmandeloyl chloride to give diastereomeric mixtures. The crystallization of the diastereomeric mixtures followed by hydrolysis yielded the corresponding asymmetric amines with high enantio-purity.
  • Küçük Resim Yok
    Öğe
    New 4-methanesulfonyloxy benzohydrazide derivatives as potential antioxidant and carbonic anhydrase I and II inhibitors: synthesis, characterization, molecular docking, dynamics & ADME studies
    (Elsevier, 2025) Kose, Aytekin; Kose, Leyla Polat; Senol, Halil; Ulusoy-Guzeldemirci, Nuray
    As an archetypal molecule, hydrazides have a crucial vital role in numerous applications, so hydrazide-related inhibitors, especially sulfur-enriched, are favored. In the present work, we designed, synthesized and characterized fifteen novel benzohydrazide derivatives containing 4-methanesulfonyloxy and arylidene building blocks with a four-step synthesis pathway. The inhibitory potential of the compounds was assessed using human carbonic anhydrases I and II (hCA I and II) isozymes and the results were compared to those of the standard inhibitor, acetazolamide (AZA). The antioxidant activity profiles for all compounds were also examined using various bioanalytical methods and the results were compared with the standards. The hCA I and II were the best inhibited by compounds 5f, 5g, and 5i with inhibition constants IC50 in the range 20.45-51.43 nM (AZA: IC50=218.38) for hCA I and 33.54-42.45 nM (AZA: IC50=44.39) for hCA II. Structure-activity relationships were also discussed and discovered that hCA I and II inhibition was unaffected by the presence of an electronwithdrawing or releasing group. This effectiveness was the only result of the sort of substituted group(s), which was located at the reagent. Molecular docking and dynamics simulations showed that compounds 5f, 5g, and 5i have strong and stable interactions with key amino acids and zinc ions in the active sites of enzymes, which supports their ability to block enzyme activity. In silico ADME studies predicted favorable drug-like properties and high human oral absorption for all synthesized compounds. In silico ADME studies predicted favorable drug-like properties and high human oral absorption for all synthesized compounds. These findings highlight the multifunctional potential of the synthesized benzohydrazide derivatives as hCA I and II inhibitors and antioxidants, paving the way for their further development and optimization for therapeutic applications.
  • Küçük Resim Yok
    Öğe
    Synthesis and asymmetric resolution of substituted 2-aminoindane and 2-aminotetralin derivatives
    (Pergamon-Elsevier Science Ltd, 2023) Akincioglu, Akin; Akbaba, Yusuf; Kose, Leyla Polat; Akyuz, Leyla Demirkol; Goksu, Sueleyman
    We performed the racemic synthesis and asymmetric resolution of one 2-aminoindane and three 2-aminotertalins due to their crucial biological roles in the central nervous system (CNS). For this reason, desired (+/-)-2-aminoindane and (+/-)-2-aminotetralin derivatives were synthesized starting from appropriate reagents. While highly enantio pure (+)-39, (+)-40, and ( inverted exclamation )-40 were obtained from the reaction of racemic amines with (R)-O-acetylmandeloyl chloride followed by crystallization, hydrolysis with KOH and acidification with HCl, (S)-42 and (-)-43 were synthesized via the reaction of racemic amines with (S)-mandelic acid and hydrolysis.(c) 2023 Elsevier Ltd. All rights reserved.
  • Küçük Resim Yok
    Öğe
    Synthesis and biological evaluation of some 1-naphthol derivatives as antioxidants, acetylcholinesterase, and carbonic anhydrase inhibitors
    (Wiley-V C H Verlag Gmbh, 2021) Erdogan, Musa; Kose, Leyla Polat; Essiz, Selcuk; Gulcin, Ilhami
    A series of some naphthol derivatives 4a-f, 5a,f, 6a, and 7a,b (six novel ones: 4c,d, 5a, 6a, 7a,b) bearing F, Cl, Br, OMe, and dioxole substituents at different positions of the aromatic rings was designed, synthesized, and characterized. The naphthol derivatives were synthesized in three steps, namely the addition reaction of furan via Diels-Alder cycloaddition reaction, copper(II) trifluoromethanesulfonate (Cu(OTf)(2))-catalyzed aromatization reaction, and the bromination reaction, respectively. The structures of the newly obtained compounds (4c,d, 5a, 6a, 7a,b) were characterized by spectroscopic techniques. In addition, some biological activity studies were investigated under in vitro conditions. Inhibition studies of these compounds were performed on human carbonic anhydrase (hCA) I and II isoenzymes purified from human erythrocytes as a biological evaluation. Moreover, their potential antioxidant and antiradical activities were studied by analytical methods like ABTS(center dot+) and DPPH center dot scavenging, and it was determined that some molecules showed good activity. Also, inhibition of acetylcholinesterase (AChE), which is a marker of many degenerative neurological diseases, was tested and the results were discussed. Excellent enzyme inhibition results were recorded for most of the molecules. These 1-naphthol derivatives were found as effective inhibitors for hCA I, hCA II, and AChE with K-i values ranging from 0.034 +/- 0.54 to 0.724 +/- 0.18 mu M for hCA I, 0.172 +/- 0.02 to 0.562 +/- 0.21 mu M for hCA II, and 0.096 +/- 0.01 to 0.177 +/- 0.02 mu M for AChE.