Synthesis and 5α-reductase inhibitory activities of benzofuran derivatives with a carbamoyl group

A New Approach to 2,3-Disubstituted Benzo[b]furans from o-Alkynylphenols via 5-endo-dig-Iodocyclisation/Palladium-Catalysed Reactions

“…7 Benzo[b]furans with a carbamoyl group have been synthesised and evaluated for rat and human testosterone 5areductase inhibitory activities in vitro. 8 Though a number of synthetic routes exist for their preparation, 9,10 in the last few years there has been a growing interest in developing more general and versatile synthetic methodologies to this class of compounds. Recent efforts have centred around the construction of the benzo[b]furan ring by using palladium catalyst systems, 11 including our own procedures based on the palladium-catalysed coupling/cyclization of 1-alkynes with o-hydroxyaryl-or o-hydroxyheteroaryl halides 12 and the oxypalladation/reductive elimination tandem reaction.…”

Selective non-steroidal inhibitors of 5α-reductase type 1

“…3). The most selective, although not very potent, type 1 inhibitor, among the plethora of compounds reported so far (most of them, moreover, tested only versus rat enzymes) is compound 23 with IC 50 = 310 nM towards type 1 isozyme and >100,000 towards type 2 [70,71]. Also compounds 24a-c displayed some selectivity toward human 5␣R-1, although the best structural combination is that of compound 26 from Pfizer [6,72] in which the methyl group on the indole ring forces the molecule to adopt only the 'trans' conformation.…”

Synthesis of New 2-Arylbenzo[b]furan Derivatives via Palladium-Catalyzed Suzuki Cross-Coupling Reactions in Aqueous Media

“…The results showed that three structurally modified derivatives ( Figure 1 , 3a – 3c ) inhibited significantly the production of inflammatory mediator nitric oxide without showing cytotoxicity. Moreover, Nishi and coworkers synthesized a series of 2-phenylbenzofuran derivatives with both carboxy and 5- or 6-diphenylmethylcarbamoyl groups ( Figure 1 , 4a – 4c ), which showed inhibitory activities against both enzymes and were more active against human type I enzyme than against type II enzyme [ 20 ].…”