120823-45-2

Upstream product

• 31731-23-4 3-(2-nitroethyl)indole 
• 3156-51-2 3-(2-nitroethenyl)-1H-indole 
• 487-89-8 Indole-3-carboxaldehyde 
• 120-72-9 indole 
• 61-54-1 tryptamine 
• 98-68-0 4-methoxy-phenyl-sulphonyl chloride 

Relevant academic research and scientific papers

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.

Diastereoselective tricyclization/dimerization of yne-indoles catalyzed by a Au(III) complex featuring an L2/Z-type ligand

In order to investigate catalyst activation via a (Au → B)8 interaction, Au(DPB)X3 (DPB = diphosphine-borane) featuring an L2/Z ligand was synthesized. The resulting cationic catalyst was utilized for the unprecedented diastereoselective tricyclization/dimerization of yne-indoles.

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.

Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases

The development of small molecules that inhibit protein-protein interactions continues to be a challenge in chemical biology and drug discovery. Herein we report the development of indole-based fragments that bind in a shallow surface pocket of a humanised surrogate of RAD51. RAD51 is an ATP-dependent recombinase that plays a key role in the repair of doublestrand DNA breaks. It both self-associates, forming filament structures with DNA, and interacts with the BRCA2 protein through a common "FxxA" tetrapeptide motif. We elaborated previously identified fragment hits that target the FxxA motif site and developed small-molecule inhibitors that are approximately 500-fold more potent than the initial fragments. The lead compounds were shown to compete with the BRCA2-derived Ac-FHTA-NH2 peptide and the self-association peptide of RAD51, but they had no effect on ATP binding. This study is the first reported elaboration of small-molecular-weight fragments against this challenging target.

Design and bio-evaluation of indole derivatives as potent Kv1.5 inhibitors

Atrial fibrillation (AF) is one of the common arrhythmias that threaten human health. Kv1.5 potassium channel is reported as an efficacious and safe target for the treatment of AF. In this paper, we designed and synthesized three series of compounds through modifying the lead compound RH01617 that was screened out by the pharmacophore model we reported earlier. All of the compounds were evaluated by the whole-patch lamp technology and most of them possessed potent inhibitory activities against Kv1.5. Compounds IIIi and IIIl were evaluated for the target selectivity as well as the pharmacodynamic effects in an isolated rat model. Due to the promising pharmacological behavior, compound IIIl deserves further pharmacodynamic and pharmacokinetic evaluations.

Inhibitors of 15-lipoxygenase

The present invention provides inhibitors of 15-LO according to Formula I, pharmaceutical compositions containing such inhibitors and methods for treating diseases related to the 15-LO cascade using such compounds and compositions.