18386-45-3

Usage

InChI:InChI=1/C19H26O3/c1-18-7-5-11(20)9-15(18)16(21)10-12-13-3-4-17(22)19(13,2)8-6-14(12)18/h9,11-14,20H,3-8,10H2,1-2H3/t11-,12-,13-,14-,18+,19-/m0/s1

Upstream product

• 19449-09-3 3β-acetoxyandrost-4-ene-6,17-dione 
• 54604-81-8 5-bromo-3β-hydroxy-5α-androstan-6,17-dione 3-acetate 
• 4229-69-0 3β-acetoxy-5-bromo-6β-hydroxy-5α-androstan-17-one 
• 53-43-0 dehydroepiandrosterone 
• 39933-10-3 3β,5-dihydroxy-5α-androstane-6,17-dione 3-acetate 
• 7745-40-6 3β-hydroxy-17,17-ethylenedioxo-5-androstene 
• 115350-45-3 C₂₃H₃₄O₅ 
• 14456-20-3 3β-acetoxy-5-androsten-17-one-17-ethyleneketal 

Relevant academic research and scientific papers

3β-HYDROXYANDROST-4-EN-6-ONE DERIVATIVES AS AROMATASE INHIBITORS

The 3-formate (II), 3-acetate (III), 3-bromoacetate (IV), 3-propionate (V), 3-methyl ether (VI), and 3-deoxy-derivative (VII) of 3β-hydroxyandrost-4-ene-6,17-dione (I) were synthesized and tested in human placental microsomes for their ability to inhibit aromatase.II, III, and VII of this series were potent inhibitors of aromatase with the IC50's (1.7 and 3.3 μM) of the latter two comparable to that (1.2 μM) of 4-hydroxyandrostenedione.Kinetic studies showed that the three steroids are competitive inhibitors of the enzyme with Ki's of 16.0, 5.5, and 0.61 μM for II, III, and VII.Furthermore, II showed a time-dependent, pseudo-first order rate of inactivation of aromatase with Ki of 20.5 μM and kinact of 1.54 * 10-2 min-1, while III gave a time-dependent, biphasic loss of the enzyme activity.NADPH and oxygen were required for the time-dependent inactivation and the substrate, androstenedione, prevented it.

Synthesis of cytotoxic 6E-hydroximino-4-ene steroids: Structure/activity studies

In an effort to determine the pharmaceutical utility and the structural requirements for activity against various tumor cell lines, several 6E-hydroximino-4-ene steroids with different side chains and degrees of unsaturation on ring A were synthesized in our laboratory. Evaluation of the synthesized compounds for cytotoxicity against P-388, A-549, HT-29, and MEL-28 tumor cells revealed that some important structural features are required for activity. The presence of a cholesterol-type side chain, which appears to play a major role in determining the biological activity, the existence of a ketone functionality at C-3, and an elevated degree of oxidation on ring A all result in higher bioctivity than other structural motifs.