5626-90-4Relevant articles and documents
Inhibition of carbonic anhydrase II by sulfonamide derivatives
Li, W.,Xuan, G. S.,Zhan, J. H.,Zhang, A. M.,Zheng, K.
, p. 412 - 415 (2021/11/22)
A series of sulfonamide derivatives were synthesized, and the enzyme inhibitory activity of the synthesized compounds on carbonic anhydrase II was evaluated. Through molecular docking studies, it was found that compounds 1b, 1e, 2a, 2b, 3a have a strong binding affinity to carbonic anhydrase II. The IC50 values of the four compounds 1e, 2b, 3a, and 3b were lower than that of the positive control drug acetazolamide. What’s more, the compounds had a high inhibitory activity for A549 lung cancer cell growth, among them, 1e and 3a could inhibit both carbonic anhydrase II and lung cancer cell proliferation.
Catalytic activity of magnetic Fe3O4@Diatomite earth and acetic acid for the N-acylation of sulfonamides
Ghasemi, Mohammad Hadi,Kowsari, Elaheh,Hosseini, Seyed Kiumars
supporting information, p. 387 - 391 (2016/01/12)
The Br?nsted and Lewis acidic promoted N-acylation of sulfonamides with acetic anhydride or benzoyl chloride has been achieved using glacial acetic acid and magnetic Fe3O4@Diatomite earth. Use of acetic acid as solvent omits the need for organic bases and permits the isolation of products by filtration and precipitation. Additionally, the magnetic composite Fe3O4@Diatomite acts as a conjugate proton super acid, enabling the acylation of sulfonamide compounds.
Identification of a β1/β2-Specific Sulfonamide Proteasome Ligand by Crystallographic Screening
Beck, Philipp,Reboud-Ravaux, Michèle,Groll, Michael
supporting information, p. 11275 - 11278 (2016/07/06)
The proteasome represents a validated drug target for the treatment of cancer, however, new types of inhibitors are required to tackle the development of resistant tumors. Current fluorescence-based screening methods suffer from low sensitivity and are limited to the detection of ligands with conventional binding profiles. In response to these drawbacks, a crystallographic screening procedure for the discovery of agents with a novel mode of action was utilized. The optimized workflow was applied to the screening of a focused set of compounds, resulting in the discovery of a β1/β2-specific sulfonamide derivative that noncovalently binds between subunits β1 and β2. The binding pocket displays significant differences in size and polarity between the immuno- and constitutive proteasome. The identified ligand thus provides valuable insights for the future structure-based design of subtype-specific proteasome inhibitors.