Synthesis, Molecular Docking Analysis, and Carbonic Anhydrase Inhibitory Evaluations of Benzenesulfonamide Derivatives Containing Thiazolidinone
| Autor: | Zhi-peng Wang, Yang Liu, Jian Wang, Maosheng Cheng, Qian-Jie Wu, Zuo-Peng Zhang, Jia-Yue Li, Ze-Fa Yin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Stereochemistry
Pharmaceutical Science Inhibitory postsynaptic potential Carbonic Anhydrase II 01 natural sciences thiazolidinone Article Analytical Chemistry lcsh:QD241-441 03 medical and health sciences lcsh:Organic chemistry Antigens Neoplasm Catalytic Domain Carbonic anhydrase Drug Discovery Humans Molecule Physical and Theoretical Chemistry Carbonic Anhydrase IX Carbonic Anhydrase Inhibitors 030304 developmental biology Sulfonamides 0303 health sciences biology 010405 organic chemistry Chemistry Organic Chemistry human carbonic anhydrase IX Molecular Docking Analysis Active site 0104 chemical sciences benzenesulfonamide Molecular Docking Simulation Enzyme inhibition Chemistry (miscellaneous) Docking (molecular) biology.protein Molecular Medicine docking study |
| Zdroj: | Molecules, Vol 24, Iss 13, p 2418 (2019) Molecules Volume 24 Issue 13 |
| ISSN: | 1420-3049 |
| Popis: | To find novel human carbonic anhydrase (hCA) inhibitors, we synthesized thirteen compounds by combining thiazolidinone with benzenesulfonamide. The result of the X-ray single-crystal diffraction experiment confirmed the configuration of this class of compounds. The enzyme inhibition assays against hCA II and IX showed desirable potency profiles, as effective as the positive controls. The docking studies revealed that compounds (2) and (7) efficiently bound in the active site cavity of hCA IX by forming sufficient interactions with active site residues. The fragment of thiazolidinone played an important role in the binding of the molecules to the active site. |
| Databáze: | OpenAIRE |
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