3192-10-7

Basic information

• Product Name: Ethenesulfonamide, N-phenyl-
• Synonyms: ethenesulfonanilide;Aethylensulfonsaeure-anilid;Aethensulfonanilid;N-Phenyl-aethensulfonamid;Aethensulfonsaeure-anilid;Aethylensulfonanilid
• CAS NO: 3192-10-7
• Molecular Formula: C8H9NO2S
• Molecular Weight: 183.231
• Mol File: 3192-10-7.mol
• Article Data: 12

Chemical Properties

• CAS DataBase Reference: Ethenesulfonamide, N-phenyl-(CAS DataBase Reference)
• NIST Chemistry Reference: Ethenesulfonamide, N-phenyl-(3192-10-7)
• EPA Substance Registry System: Ethenesulfonamide, N-phenyl-(3192-10-7)

Safety Data

• Hazardous Substances Data: 3192-10-7(Hazardous Substances Data)

Upstream product

• 31469-08-6 ethane-1,2-disulfonyl chloride 
• 62-53-3 aniline 
• 71-43-2 benzene 
• 6608-47-5 vinylsulfonyl chloride 
• 1622-32-8 2-Chloroethanesulfonyl chloride 
• 60-29-7 diethyl ether 
• 67-64-1 acetone 

Downstream Products

• 91905-00-9 2-piperidin-1-yl-ethanesulfonic acid anilide 
• 28792-97-4 N-methyl-N-phenylethenesulfonamide 
• 1316224-27-7 C₁₄H₁₄ClNO₂S 
• 1346254-76-9 C₂₀H₁₉NO₂S 

Relevant articles and documents

Visible-Light-Promoted Radical Cyclization of N -Arylvinylsulfonamides: Synthesis of CF 3/CHF 2/CH 2CF 3-Containing 1,3-Dihydrobenzo[ c ]isothiazole 2,2-Dioxide Derivatives

A photocatalyzed and highly efficient trifluoromethylation of N-arylvinylsulfonamides using commercially available CF3SO2Cl as the trifluoromethyl radical source under blue LEDs is reported. The reaction proceeds through radical cyclization under mild con

N-Phenyl-N-aceto-vinylsulfonamides as Efficient and Chemoselective Handles for N-Terminal Modification of Peptides and Proteins

A number of vinylsulfonamides were synthesized and screened to identify reagents that can be used to modify octreotide under biological pH and room temperature with improved efficiency. N-Phenyl-N-aceto-vinylsulfonamide exhibits higher reactivity and has emerged as an efficient reagent that has the ability to realize the selective modification of peptides and proteins at the N-terminus via aza-Michael addition. We showed that, after conjugation of peptides and proteins with the reagent containing a bioorthogonal functional group, the derivatives could be further labelled by functionalities, including fluorescent tags, modified drugs and polyethylene glycol (PEG) polymers without the need for prior treatment. Somatostatin, lysozyme, and RNaseA were selectively modified at the N-terminus, which illustrated the application of the method.

Selective lysine modification of native peptides: Via aza-Michael addition

A series of vinylsulfonamides were synthesized and screened for site-selective modification of the ?-amino group of lysine-bearing free α-amine residues. N-Methyl-N-phenylethenesulfonamide has emerged as an applicable reagent and has been developed for efficient and highly selective modification of the lysine residue of native peptides in the presence of a free N-terminus via aza-Michael addition. We demonstrated that functional N-phenylvinylsulfonamide derivatives with a fluorescent moiety or drug could also be conjugated to the lysine residue of octreotide and insulin with high specificity, without modifying the N-terminus. Our method provides a promising strategy for site-selective lysine functionalization in native peptides with a free N-terminus.