Novel Schiff Base Sulfonate Derivatives as Carbonic Anhydrase and Acetylcholinesterase Inhibitors: Synthesis, Biological Activity, and Molecular Docking Insights DOI Open Access
Ümit Yaşar, Yeliz Demir, İlyas Gönül

et al.

Chemistry & Biodiversity, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 10, 2024

ABSTRACT Sulfonate derivatives are an essential class of compounds with diverse pharmacological applications. This study presents the synthesis and detailed characterization six novel Schiff base sulfonate ( L 1 –L 6 ) through spectroscopic techniques (FT‐IR NMR). Their inhibitory potential was evaluated against human carbonic anhydrase isoenzymes h CA I II) acetylcholinesterase (AChE), which crucial therapeutic targets for diseases such as glaucoma, epilepsy, Alzheimer's disease. The K values concerning AChE, I, II enzymes were in ranges 106.10 ± 14.73 to 422.80 17.64 nM (THA: 159.61 8.41 nM), 116.90 24.40 268.00 35.84 (AAZ: 439.17 9.30 177.00 35.03 435.20 75.98 98.28 1.69 respectively. Molecular docking analyses revealed key interactions within active sites enzymes, including hydrogen bonding critical residues π–π stacking interactions. Notably, 3 demonstrated superior inhibition : nM) AChE positioning it a promising lead compound. comprehensive investigation contributes development isoform‐specific inhibitors use provides valuable insights into their binding mechanisms. findings underscore sulfonates scaffolds drug discovery neurodegenerative metabolic disorders.

Language: Английский

Novel benzenesulfonamides containing dual triazole moiety with selective carbonic anhydrase inhibition and anticancer activity DOI

Aida Buza,

Cüneyt Türkeş, Mustafa Arslan

et al.

RSC Medicinal Chemistry, Journal Year: 2024, Volume and Issue: unknown

Published: Jan. 1, 2024

A series of sulfonamides incorporating a 1,2,3-triazolyloxime substituted 1,2,3-triazolyl moiety were conceptualized and synthesized as human carbonic anhydrase (

Language: Английский

Citations

6
Interactions of novel 1,3-diaryltriazene-sulfamethazines with carbonic anhydrases: Kinetic studies and in silico simulations DOI
Nebih Lolak, Cüneyt Türkeş, Süleyman Akocak

et al.

Archives of Biochemistry and Biophysics, Journal Year: 2024, Volume and Issue: 761, P. 110181 - 110181

Published: Oct. 11, 2024

Language: Английский

Citations

5
Design, Synthesis, and Inhibition of α-Glucosidase by Novel L-Phenylalanine-Derived Hydrazones: Kinetic, Molecular Docking, and Dynamics Studies DOI
Erbay Kalay, Şevki Adem, Yeliz Demir

et al.

Archives of Biochemistry and Biophysics, Journal Year: 2025, Volume and Issue: unknown, P. 110368 - 110368

Published: March 1, 2025

Language: Английский

Citations

0
Sulfonamide‐Bearing Pyrazolone Derivatives as Multitarget Therapeutic Agents: Design, Synthesis, Characterization, Biological Evaluation, In Silico ADME/T Profiling and Molecular Docking Study DOI Creative Commons
Nebih Lolak, Süleyman Akocak, Meryem Topal

et al.

Pharmacology Research & Perspectives, Journal Year: 2025, Volume and Issue: 13(2)

Published: March 24, 2025

The research and design of new inhibitors for the treatment diseases such as Alzheimer's disease glaucoma through inhibition cholinesterases (ChEs; acetylcholinesterase, AChE butyrylcholinesterase, BChE) carbonic anhydrase enzymes are among important targets. Here, a series novel sulfonamide-bearing pyrazolone derivatives (1a-f 2a-f) were successfully synthesized characterized by using spectroscopic analytical methods. inhibitory activities these newly compounds evaluated both in vitro silico their effect on anhydrases (hCA I hCA II isoenzymes) ChEs. studies showed that demonstrated potential activity, with KI values covering following ranges: 18.03 ± 2.86-75.54 4.91 nM I, 24.84 1.57-85.42 6.60 II, 7.45 0.98-16.04 1.60 AChE, 34.78 5.88-135.70 17.39 BChE. Additionally, many promising some higher potency than reference compounds. While have also identified binding positions compounds, crystal structures BChE receptors. varying affinities designed ChEs isoenzymes show could hold promise alternative agents selectively inhibiting hCAs glaucoma.

Language: Английский

Citations

0
Aldose reductase inhibition properties of novel thiazolidin-2,4-diones: In vitro and in silico approach for the treatment of diabetes-related complications DOI
Feyzi Sinan Tokalı, Yeliz Demir, Halil Şenol

et al.

Journal of Molecular Liquids, Journal Year: 2025, Volume and Issue: unknown, P. 127487 - 127487

Published: March 1, 2025

Language: Английский

Citations

0
Isoindole‐1,3‐Dione Sulfonamides as Potent Inhibitors of Glucosidase, Aldose Reductase, and Tyrosinase: A Molecular Docking and Enzyme Inhibition Study DOI
Zafer Aslan, Esra Yılmaz,

Nurgül Pulat

et al.

Biotechnology and Applied Biochemistry, Journal Year: 2025, Volume and Issue: unknown

Published: April 1, 2025

Diabetes mellitus, especially type 2, is a global health challenge, and effective enzyme inhibitors are essential for its control. Conventional have drawbacks such as gastrointestinal side effects regional availability, examples being acarbose epalrestat. Moreover, tyrosinase, which controls melanin synthesis also target reducing hyperpigmentation disorders. In this study, we demonstrate the inhibitory action of novel isoindole-1,3-dione-based sulfonamides against key enzymes associated with diabetes hyperpigmentation, α-Glucosidase (α-Glu), aldose reductase (ALR2), tyrosinase. The presynthesized compounds (3, 4a-k) tested in vitro inhibition α-Glu, ALR2, tyrosinase compared reference acarbose, epalrestat, kojic acid. Kinetic studies showed that both competitive noncompetitive modes were observed. Among them, compound 4a displayed highest ALR2 potency (Ki: 0.211 µM) was superior to terms 4k shown be more potent Ki 0.049 µM, particularly versus acarbose. Compound 4d excellent activity 1.43 assays, much than Molecular docking revealed details enzyme-binding interactions, justify respective mechanisms Structure-activity relationships reflected strong hydrogen bonding hydrophobic interactions led higher potency. These findings highlight importance therapeutic agents will provide valuable leads developing multifunctional diabetic complications hyperpigmentation.

Language: Английский

Citations

0
Novel Schiff Base Sulfonate Derivatives as Carbonic Anhydrase and Acetylcholinesterase Inhibitors: Synthesis, Biological Activity, and Molecular Docking Insights DOI Open Access
Ümit Yaşar, Yeliz Demir, İlyas Gönül

et al.

Chemistry & Biodiversity, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 10, 2024

ABSTRACT Sulfonate derivatives are an essential class of compounds with diverse pharmacological applications. This study presents the synthesis and detailed characterization six novel Schiff base sulfonate ( L 1 –L 6 ) through spectroscopic techniques (FT‐IR NMR). Their inhibitory potential was evaluated against human carbonic anhydrase isoenzymes h CA I II) acetylcholinesterase (AChE), which crucial therapeutic targets for diseases such as glaucoma, epilepsy, Alzheimer's disease. The K values concerning AChE, I, II enzymes were in ranges 106.10 ± 14.73 to 422.80 17.64 nM (THA: 159.61 8.41 nM), 116.90 24.40 268.00 35.84 (AAZ: 439.17 9.30 177.00 35.03 435.20 75.98 98.28 1.69 respectively. Molecular docking analyses revealed key interactions within active sites enzymes, including hydrogen bonding critical residues π–π stacking interactions. Notably, 3 demonstrated superior inhibition : nM) AChE positioning it a promising lead compound. comprehensive investigation contributes development isoform‐specific inhibitors use provides valuable insights into their binding mechanisms. findings underscore sulfonates scaffolds drug discovery neurodegenerative metabolic disorders.

Language: Английский

Citations

0