154715-61-4

Basic information

• Product Name: Benzenesulfonamide, 4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]-
• CAS NO: 154715-61-4
• Molecular Formula: C11H10N2O6S
• Molecular Weight: 298.276
• Mol File: 154715-61-4.mol
• Article Data: 11

Chemical Properties

• CAS DataBase Reference: Benzenesulfonamide, 4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzenesulfonamide, 4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]-(154715-61-4)
• EPA Substance Registry System: Benzenesulfonamide, 4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]-(154715-61-4)

Safety Data

• Hazardous Substances Data: 154715-61-4(Hazardous Substances Data)

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 138-41-0 4-(aminosulfonyl)-benzoic acid 

Downstream Products

• 1228371-48-9 C₃₁H₃₉N₅O₉S₂ 

Relevant articles and documents

Poly(amidoamine) dendrimers with carbonic anhydrase inhibitory activity and antiglaucoma action

Four generations of poly(amidoamine) (PAMAM) dendrimers decorated with benzenesulfonamide moieties were prepared by derivatizing the amino groups of the dendrimer with 4-carboxy-benzenesulfonamide functionalities. Compounds incorporating 4, 8, 16, and 32

Clickable gold-nanoparticles as generic probe precursors for facile photoaffinity labeling application

Rapid access to appropriately functionalized probes is crucial in chemical labeling approaches to target identification studies. We designed and synthesized clickable gold-nanoparticles as generic probe precursors that enable (1) one-step ligand derivatization by click chemistry, and (2) facile photoaffinity labeling application. Using cholesterol as a model ligand, we successfully demonstrated the utility of the ligand-clicked probe in photoaffinity labeling of endogenously expressed oxysterol-binding protein (OSBP) in cell lysate.

Protein-Induced Supramolecular Disassembly of Amphiphilic Polypeptide Nanoassemblies

Mimicking noncovalent interaction based processes in nature has been an important goal of supramolecular chemistry. Here, we report on amphiphilic polypeptides that self-assemble to form nanoscale supramolecular assemblies and are programmed to disassemble in response to a specific protein. Benzenesulfonamide and carbonic anhydrase have been chosen as the ligand and protein, respectively, to demonstrate this possibility. Since the amphiphilic nanoassembly sequesters hydrophobic guest molecules, the protein-specific disassembly event provides a protein-sensitive molecular release as well. We envision that the binding induced disassembly and guest release might open up new opportunities for the next generation of supramolecular assemblies for protein-specific delivery and diagnostics.