143285-19-2Relevant academic research and scientific papers
Selective inhibitors of monoamine oxidase (MAO). 5.1,2 1-Substituted phenoxathiin inhibitors containing no nitrogen that inhibit MAO a by binding it to a hydrophobic site
Harfenist, Morton,McGee, Daniel P.C.,Reeves, Mark D.,White, Helen L.
, p. 2118 - 2125 (1998)
It is believed that a monoamine oxidase (MAO) inhibitor specific for MAO A, which is reversibly bound to this enzyme and displaceable by tyramine, will be an antidepressant which will not cause a rise in blood pressure when tyramine-containing foods are ingested. Some linear tricyclic compounds with a larger and a smaller group forming the central ring and with a lipophilic group ortho to the larger group (here mostly the SO2 function of phenoxathiin 10,10-dioxide) are reported to have the sought properties. Potency appears to require short length and relatively small cross section for the substituent. The 1-ethyl (13), 1-vinyl (22), 1-trifluoromethyl (27), and 1-iodo (76) phenoxathiin dioxides had the best profiles. Structure- activity relationships, syntheses, and a possible rationale for the selectivity of these compounds and related tricyclics are given. Compound 13 was selected for further development. A summary of pharmacological data for 13 is given.
