MAO inhibition by arylisopropylamines: the effect of oxygen substituents at the beta-position.
Twenty-nine arylisopropylamines, substituted at the beta-position of their side chain by an oxo, hydroxy, or methoxy group, were evaluated in vitro as MAO-A and MAO-B inhibitors. The oxo derivatives ('cathinones') were in general less active as MAO-A inhibitors than the corresponding arylisopropylamines, but exhibited an interesting MAO-B inhibiting activity, which was absent in the hydroxy, methoxy, and beta-unsubstituted analogues. These results suggest that selective affinity for the two MAO isoforms in this family of compounds is modulated not only by the aryl substitution pattern but also by the side-chain substituents on the arylalkylamine scaffold.
Osorio-Olivares
Mauricio
M
Facultad de Química y Biología, Universidad de Santiago, Casilla 40, Correo 33, Santiago, Chile.
Rezende
Marcos Caroli
MC
Sepúlveda-Boza
Silvia
S
Cassels
Bruce K
BK
Fierro
Angélica
A
D000470:Alkaloids / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D008958:Models, Molecular; D015394:Molecular Structure; D008995:Monoamine Oxidase / Q000187:drug effects*; D010100:Oxygen / Q000737:chemistry*; D011437:Propylamines / Q000494:pharmacology*
D000470:Alkaloids; D004791:Enzyme Inhibitors; D011437:Propylamines; C023665:cathinone; D008995:Monoamine Oxidase; D010100:Oxygen