311781-49-4

Basic information

• Product Name: Benzenesulfonamide, N-[2-(1H-indol-3-yl)ethyl]-2-nitro-
• CAS NO: 311781-49-4
• Molecular Formula: C16H15N3O4S
• Molecular Weight: 345.379
• Mol File: 311781-49-4.mol

Chemical Properties

• CAS DataBase Reference: Benzenesulfonamide, N-[2-(1H-indol-3-yl)ethyl]-2-nitro-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzenesulfonamide, N-[2-(1H-indol-3-yl)ethyl]-2-nitro-(311781-49-4)
• EPA Substance Registry System: Benzenesulfonamide, N-[2-(1H-indol-3-yl)ethyl]-2-nitro-(311781-49-4)

Safety Data

• Hazardous Substances Data: 311781-49-4(Hazardous Substances Data)

Upstream product

• 61-54-1 tryptamine 
• 1694-92-4 2-Nitrobenzenesulfonyl chloride 

Downstream Products

• 1370734-16-9 C₂₅H₃₁N₃O₄S 
• 1370734-18-1 C₂₆H₃₁N₃O₄S 
• 1370734-62-5 C₂₄H₂₅N₃O₄S 
• 1370734-63-6 C₂₈H₂₉N₃O₄S 
• 1370734-64-7 C₂₅H₃₀BrN₃O₄S 
• 1370734-69-2 C₂₆H₃₀BrN₃O₄S 
• 1370734-70-5 C₂₄H₂₄BrN₃O₄S 
• 1370734-71-6 C₂₈H₂₈BrN₃O₄S 
• 1350455-08-1 C₂₂H₂₅BrN₂ 
• 1370734-15-8 C₂₃H₂₁N₃O₄S 
• 1370734-14-7 C₁₉H₁₇N₃O₄S 
• 1370734-01-2 C₂₁H₂₃N₃O₄S 

Relevant articles and documents

Intercepting bacterial indole signaling with flustramine derivatives

Indole signaling is one of the putative universal signaling networks in bacteria. We have investigated the use of desformylflustrabromine (dFBr) derivatives for the inhibition of biofilm formation through modulation of the indole-signaling network in Escherichia coli and Staphylococcus aureus. We have found dFBr derivatives that are 10-1000 times more active than indole itself, demonstrating that the flustramine family of indolic natural products represent a privileged scaffold for the design of molecules to control pathogenic bacterial behavior.

Highly active modulators of indole signaling alter pathogenic behaviors in gram-negative and gram-positive bacteria

Indole is a universal signal that regulates various bacterial behaviors, such as biofilm formation and antibiotic resistance. To generate mechanistic probes of indole signaling and control indole-mediated pathogenic phenotypes in both Gram-positive and Gram-negative bacteria, we have investigated the use of desformylflustrabromine (dFBr) derivatives to generate highly active indole mimetics. We have developed non-microbicidal dFBr derivatives that are 27-2000 times more active than indole in modulating biofilm formation, motility, acid resistance, and antibiotic resistance. The activity of these analogues parallels indole, because they are dependent on temperature, the enzyme tryptophanase TnaA, and the transcriptional regulator SdiA. This investigation demonstrates that molecules based on the dFBr scaffold can alter pathogenic behaviors by mimicking indole-signaling pathways. Phenotype control: Non-microbicidal desformylflustrabromine (dFBr) derivatives that are 27-2000 times more active than indole in modulating biofilm formation, motility, acid resistance, and antibiotic resistance were developed. This investigation demonstrates that molecules based on the dFBr scaffold can alter pathogenic behaviors by mimicking indole-signaling pathways (see scheme).

Rhodium-Catalyzed Stereoselective Cyclization of 3-Allenylindoles and N-Allenyltryptamines to Functionalized Vinylic Spiroindolenines

Herein, we report a highly enantio- and diastereoselective rhodium-catalyzed cyclization of N-allenyltryptamines and 3-allenylindoles to 6-membered spirocyclic indolenines. This allylic addition methodology offers the advantage of using a comparably cheap commercially available ligand with low loadings of an affordable rhodium precursor. The products can be converted into functionalized spirooxindoles and spiroindolines, which are regarded as important building blocks for the synthesis of a lot of natural products with biological activities.

Access to Indole-Fused Benzannulated Medium-Sized Rings through a Gold(I)-Catalyzed Cascade Cyclization of Azido-Alkynes

Because benzannulated and indole-fused medium-sized rings are found in many bioactive compounds, combining these fragments might lead to unexplored areas of biologically relevant and uncovered chemical space. Herein is shown that α-imino gold carbene chem

Small-Molecule Activators of Glucose-6-phosphate Dehydrogenase (G6PD) Bridging the Dimer Interface

We recently identified AG1, a small-molecule activator that functions by promoting oligomerization of glucose-6-phosphate dehydrogenase (G6PD) to the catalytically competent forms. Biochemical experiments indicate that the activation of G6PD by the original hit molecule (AG1) is noncovalent and that one C2-symmetric region of the G6PD homodimer is important for ligand function. Consequently, the disulfide in AG1 is not required for activation of G6PD, and a number of analogues were prepared without this reactive moiety. Our study supports a mechanism of action whereby AG1 bridges the dimer interface at the structural nicotinamide adenine dinucleotide phosphate (NADP+) binding sites of two interacting G6PD monomers. Small molecules that promote G6PD oligomerization have the potential to provide a first-in-class treatment for G6PD deficiency. This general strategy could be applied to other enzyme deficiencies in which control of oligomerization can enhance enzymatic activity and/or stability.

Synthesis, molecular docking, and QSAR study of sulfonamide-based indoles as aromatase inhibitors

Thirty four of indoles bearing sulfonamides (11–44) were synthesized and evaluated for their anti-aromatase activities. Interestingly, all indole derivatives inhibited the aromatase with IC50 range of 0.7–15.3 μM. Indoles (27–36) exerted higher aromatase inhibitory activity than that of ketoconazole. The phenoxy analogs 28 and 34 with methoxy group were shown to be the most potent compounds with sub-micromolar IC50 values (i.e., 0.7 and 0.8 μM, respectively) without affecting to the normal cell line. Molecular docking demonstrated that the indoles 28, 30 and 34 could occupy the same binding site on the aromatase pocket and share several binding residues with those of the natural substrate (androstenedione), which suggested the competitive binding could be the mode of inhibition of the compounds. The most potent analog 28 could mimic H-bond interactions of the natural androstenedione with MET374 and ASP309 residues on the aromatase. QSAR model also revealed that the para-phenoxy indole (28) affords the higher value of electronegativity descriptor MATS6e as well as the higher inhibitory activity compared with that of the ortho-phenoxy compound (34). The study highlighted a series of promising indoles to be potentially developed as novel aromatase inhibitors for therapeutics.

Highly Enantioselective Tandem Michael Addition of Tryptamine-Derived Oxindoles to Alkynones: Concise Synthesis of Strychnos Alkaloids

A highly enantioselective tandem Michael addition of tryptamine-derived oxindoles to alkynones was developed by taking advantage of a chiral N,N′-dioxide Sc(OTf)3 catalyst. The reaction enables the facile preparation of enantioenriched spiro[pyrrolidine-3,3′-oxindole] compounds, which provides a novel strategy for the synthesis of monoterpenoid indole alkaloids. As a demonstration, the asymmetric synthesis of strychnos alkaloids [(?)-tubifoline, (?)-tubifolidine, (?)-dehydrotubifoline] was achieved in 10–11 steps.

A simple and efficient method for constructing azepino[4,5-b]indole derivatives via acid catalysis

A new synthetic methodology has been developed to prepare the biologically important azepino[4,5-b]indole derivatives under Br?nsted acid catalysis. The notable features of this protocol include its operational simplicity, high reaction yields and environmentally benign and mild reaction conditions.

COMPOUNDS AND USES THEREOF IN THE TREATMENT OF CANCERS AND OTHER MEDICAL CONDITIONS

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Preparation of N-Substituted N-Arylsulfonylglycines and Their Use in Peptoid Synthesis

To increase the chemical diversity accessible with peptoids and peptide-peptoid hybrids, N-alkylated arylsulfonamides were used to prepare side chain protected N-substituted glycines compatible with solid-phase synthesis. The described procedures give acc