Artículo de revista
Monoamine Oxidase Inhibitory Properties of Optical Isomers and N-substituted Derivatives of 4-methylthioamphetamine
Fecha
2003-03-10Registro en:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 18 (4), p. 339–347, 2003
1475-6374
Autor
Hurtado Guzmán, Claudio
Fierro, Angélica
Iturriaga-Vásquez, Patricio
Sepúlveda Boza, Silvia
Cassels Niven, Bruce
Reyes Parada, Miguel
Institución
Resumen
(6)-4-Methylthioamphetamine (MTA) was resolved into
its enantiomers, and a series of N-alkyl derivatives of the
parent compound, as well as its a-ethyl analogue, were
prepared. The monoamine oxidase (MAO) inhibitory
properties of these substances were evaluated in vitro,
using a crude rat brain mitochondrial suspension as the
source of enzyme. All compounds produced a selective,
reversible and concentration-related inhibition of
MAO-A. (1)-MTA proved to be the most potent inhibitor
studied, while all the other derivatives were less active
than the parent compound, with (2)-MTA being about 18
times less potent than the (1) isomer. The analysis of
structure–activity relationships indicates that the introduction
of alkyl substituents on the amino group of MTA
leads to a reduction in the potency of the derivatives as
MAO-A inhibitors, an effect which increases with the
size of the substituent.