Cited by A novel series of thiosemicarbazone hybrid scaffolds: Design, synthesis, DFT studies, metabolic enzyme inhibition properties, and molecular docking calculations

Synthesis, characterization, inhibition effects, and molecular docking studies as acetylcholinesterase, α-glycosidase, and carbonic anhydrase inhibitors of novel benzenesulfonamides incorporating 1,3,5-triazine structural motifs DOI

Nebih Lolak, Süleyman Akocak, Cüneyt Türkeş

et al.

Bioorganic Chemistry, Journal Year: 2020, Volume and Issue: 100, P. 103897 - 103897

Published: May 4, 2020

Language: Английский

Citations

151

Exploration of 1,2,3-triazole linked benzenesulfonamide derivatives as isoform selective inhibitors of human carbonic anhydrase DOI

Chnar Kakakhan,

Cüneyt Türkeş, Özcan Güleç

et al.

Bioorganic & Medicinal Chemistry, Journal Year: 2022, Volume and Issue: 77, P. 117111 - 117111

Published: Nov. 29, 2022

Language: Английский

Citations

Cytotoxic effect, enzyme inhibition, and in silico studies of some novel N-substituted sulfonyl amides incorporating 1,3,4-oxadiazol structural motif DOI

Özcan Güleç, Cüneyt Türkeş, Mustafa Arslan

et al.

Molecular Diversity, Journal Year: 2022, Volume and Issue: 26(5), P. 2825 - 2845

Published: April 9, 2022

Language: Английский

Citations

Design, synthesis, biological evaluation and molecular docking studies of novel 1H-1,2,3-Triazole derivatives as potent inhibitors of carbonic anhydrase, acetylcholinesterase and aldose reductase DOI

Derya Aktaş Anıl, Busra Ozturk Aydin, Yeliz Demir

et al.

Journal of Molecular Structure, Journal Year: 2022, Volume and Issue: 1257, P. 132613 - 132613

Published: Feb. 10, 2022

Language: Английский

Citations

Discovery of novel benzenesulfonamides incorporating 1,2,3-triazole scaffold as carbonic anhydrase I, II, IX, and XII inhibitors DOI

Aida Buza,

Cüneyt Türkeş, Mustafa Arslan

et al.

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 239, P. 124232 - 124232

Published: March 29, 2023

Language: Английский

Citations

Novel beta-lactam substituted benzenesulfonamides: in vitro enzyme inhibition, cytotoxic activity and in silico interactions DOI

Özcan Güleç, Cüneyt Türkeş, Mustafa Arslan

et al.

Journal of Biomolecular Structure and Dynamics, Journal Year: 2023, Volume and Issue: 42(12), P. 6359 - 6377

Published: Aug. 4, 2023

In this study, a library of twelve beta-lactam-substituted benzenesulfonamides (

Language: Английский

Citations

Design, synthesis, characterization, in vitro and in silico evaluation of novel imidazo[2,1-b][1,3,4]thiadiazoles as highly potent acetylcholinesterase and non-classical carbonic anhydrase inhibitors DOI

Sercan Askin,

Hakan Tahtacı, Cüneyt Türkeş

et al.

Bioorganic Chemistry, Journal Year: 2021, Volume and Issue: 113, P. 105009 - 105009

Published: May 23, 2021

Language: Английский

Citations

Thiazolyl-pyrazoline derivatives: In vitro and in silico evaluation as potential acetylcholinesterase and carbonic anhydrase inhibitors DOI

Belgin Sever, Cüneyt Türkeş, Mehlika Dilek Altıntop

et al.

International Journal of Biological Macromolecules, Journal Year: 2020, Volume and Issue: 163, P. 1970 - 1988

Published: Sept. 13, 2020

Language: Английский

Citations

Benzenesulfonamide derivatives as potent acetylcholinesterase, α-glycosidase, and glutathione S-transferase inhibitors: biological evaluation and molecular docking studies DOI

Parham Taslımı, Mesut Işık, Fikret Türkan

et al.

Journal of Biomolecular Structure and Dynamics, Journal Year: 2020, Volume and Issue: 39(15), P. 5449 - 5460

Published: July 21, 2020

Sulfonamide derivatives exhibit a wide biological activity and can function as potential medical molecules in the development of drug. Studies have reported that compounds an effect on many enzymes. In this study, amine sulfonamide (1i-11i) were prepared with reduced imine (1-11) NaBH4 methanol. The synthesized fully characterized by spectral data analytical. acetylcholinesterase (AChE), glutathione S-transferase (GST) α-glycosidase (α-GLY) enzymes determined. For AChE α-GLY, most powerful inhibition was observed 10 10i series KI value range 2.26 ± 0.45–3.57 0.97 95.73 13.67–102.45 11.72 µM, respectively. values for GST found 22.76 1.23–49.29 4.49. Finally, stronger inhibitor lower concentrations attachment functional electronegative groups such two halogens (-Br -CI), -OH to benzene ring -SO2NH2. crystal structures AChE, complex selected 4 show importance moieties binding modes within receptors.Communicated Ramaswamy H. Sarma

Language: Английский

Citations

Synthesis, Characterization, and Inhibition Study of Novel Substituted Phenylureido Sulfaguanidine Derivatives as α‐Glycosidase and Cholinesterase Inhibitors DOI

Süleyman Akocak, Parham Taslımı, Nebih Lolak

et al.

Chemistry & Biodiversity, Journal Year: 2021, Volume and Issue: 18(4)

Published: Feb. 23, 2021

Abstract A series of six N ‐carbamimidoyl‐4‐(3‐substituted phenylureido)benzenesulfonamide derivatives were synthesized by reaction sulfaguanidine with aromatic isocyanates. In vitro and in silico inhibitory effects the novel ureido‐substituted investigated spectrophotometric methods for α‐glycosidase (α‐GLY), acetylcholinesterase (AChE), butyrylcholinesterase (BChE) enzymes associated diabetes mellitus (DM) Alzheimer's disease (AD). ‐Carbamimidoyl‐4‐{[(3,4‐dichlorophenyl)carbamoyl]amino}benzene‐1‐sulfonamide ( 2f ) showed AChE BChE effects, K I values 515.98±45.03 nM 598.47±59.18 nM, respectively, while ‐carbamimidoyl‐4‐{[(3‐chlorophenyl)carbamoyl]amino}benzene‐1‐sulfonamide 2e strong α‐GLY effect, 103.94±13.06 nM. The antidiabetic compounds are higher than their anti‐Alzheimer's because inhibition effect on diabetic enzyme is greater esterase enzymes. Indeed, metabolic important treatment DM AD.

Language: Английский

Citations