Abstract
A series of 4-phenoxybutyric acid derivatives attached to a tricyclic skeleton were prepared and evaluated as 5a-reductase inhibitors. Structure activity relationships for these compounds in terms of rat epididymis (type 2) 5a-reductase inhibitory activities reveal that 1) the substitution pattern at the 11-position of dibenz[b,e]oxepin influenced potency, 2) higher lipophilicity of the tricyclic skeleton improved potency, whereas the existence of a basic nitrogen atom in this skeleton was detrimental to potency, and 3) isobutyl substitution at the 8 positon of the azepine skeleton was tolerated. Among the tricyclic compounds studied, 4-[3-[5-benzyl-8-(2-methyl)propyl10,11-dihydrodibenz[b, f ]azepine-2-carboxamido]phenoxy]butyric acid (26) was the most potent inhibitor of rat type 2 5a-reductase at 0.1 m M.
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