29608-76-2

Upstream product

• 6283-25-6 H₂NC₆H₃(Cl)NO₂ 
• 16588-26-4 3-bromo-4-chloronitrobenzene 
• 98-80-6 phenylboronic acid 
• 29608-75-1 2-amino-5-nitro-biphenyl 

Downstream Products

• 56970-25-3 6-chloro-[1,1'-biphenyl]-3-amine 

Relevant academic research and scientific papers

Ligand-free Suzuki-Miyaura cross-coupling with low Pd content: rapid development by a fluorescence-based high-throughput screening method

Suzuki-Miyaura (SM) cross-coupling is one of the most effective strategies for carbon-carbon bond formation, but previous methods have several drawbacks, such as the requirement of complicated ligands, toxic organic solvents, and high-content-Pd catalysts. Thus, in this study, a highly efficient SM cross-coupling was developed using metal oxide catalysts: 0.02 mol% Pd, aqueous solvent, no ligand, and room temperature. Metal oxides containing low Pd content (ppm scale) were prepared by a simple co-precipitation method and used as a catalyst for the SM reaction. A fluorescence-based high-throughput screening (HTS) method was developed for the rapid evaluation of catalytic activity and reaction conditions. Among the various metal oxides, Pd/Fe2O3showed the highest activity for the SM reaction. After further optimization by HTS, various biaryl compounds were obtained under optimal conditions: Pd/Fe2O3(0.02 mol% Pd) in aqueous ethanol at mild temperature without any ligands.

Structurally simple inhibitors of lanosterol 14α-demethylase are efficacious in a rodent model of acute Chagas disease

We report structure-activity studies of a large number of dialkyl imidazoles as inhibitors of Trypanosoma cruzi lanosterol-14α-demethylase (L14DM). The compounds have a simple structure compared to posaconazole, another L14DM inhibitor that is an anti-Chagas drug candidate. Several compounds display potency for killing T. cruzi amastigotes in vitro with values of EC 50 in the 0.4-10 nM range. Two compounds were selected for efficacy studies in a mouse model of acute Chagas disease. At oral doses of 20-50 mg/kg given after establishment of parasite infection, the compounds reduced parasitemia in the blood to undetectable levels, and analysis of remaining parasites by PCR revealed a lack of parasites in the majority of animals. These dialkyl imidazoles are substantially less expensive to produce than posaconazole and are appropriate for further development toward an anti-Chagas disease clinical candidate.

Design and synthesis of potent nonpeptidic farnesyltransferase inhibitors based on a terphenyl scaffold

By modification of key carboxylate, hydrophobic, and zinc-binding groups projected from a sterically restricted terphenyl scaffold, a series of simple and nonpeptide mimetics of the CysVal-Ile-Met tetrapeptide substrate of protein farnesyltransferase (FTase) have been designed and synthesized. A crystal structure of 4-nitro-2-phenyl-3′-methoxycarbonylbiphenyl shows that the triphenyl fragment provides a large hydrophobic surface that potentially mimics the hydrophobic side chains of the three terminal residues in the tetrapeptide. 2-Phenyl-3-(N-(1-(4-cyanobenzyl)-1H-imidazol-5-yl)methyl)amino- 3′carboxylbiphenyl, in which the free thiol group was replaced with a 1-(4-cyanobenzyl)imidazole group, shows submicromolar inhibition activity against FTase in vitro and inhibits H-Ras processing in whole cells.

Development of a tripeptide mimetic strategy for the inhibition of protein farnesyltransferase

This paper describes the development of a novel terphenyl-based tripeptide mimetic of the CAAX carboxy terminal sequence of Ras. We employ a concise synthesis to form a series of differently functionalized terphenyl inhibitors of protein farnesyltransfera