Monoamine oxidase inhibitory properties of optical isomers and N-substituted derivatives of 4-methylthioamphetamine

Hurtado-Guzman, C; Fierro, A.; Iturriaga-Vasquez, P; Sepulveda-Boza, S; CASSELS, BK; Reyes-Parada, M

Abstract

(±)-4-Methylthioamphetamine (MTA) was resolved into its enantiomers, and a series of N-alkyl derivatives of the parent compound, as well as its ?-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. (+)-MTA proved to be the most potent inhibitor studied, while all the other derivatives were less active than the parent compound, with (-)-MTA being about 18 times less potent than the (+) 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.

Más información

Título según WOS: Monoamine oxidase inhibitory properties of optical isomers and N-substituted derivatives of 4-methylthioamphetamine
Título según SCOPUS: Monoamine oxidase inhibitory properties of optical isomers and N-substituted derivatives of 4-methylthioamphetamine
Título de la Revista: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volumen: 18
Número: 4
Editorial: TAYLOR & FRANCIS LTD
Fecha de publicación: 2003
Página de inicio: 339
Página final: 347
Idioma: English
URL: http://journalsonline.tandf.co.uk/Index/10.1080/1475636031000118437
DOI:

10.1080/1475636031000118437

Notas: ISI, SCOPUS