Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: Insights from molecular modeling studies

Fierro, A.; Osorio-Olivares, M; CASSELS, BK; Edmondson, DE; Sepulveda-Boza, S; Reyes-Parada, M

Abstract

Four enantiomerically pure (S)-4-alkylthioamphetamine derivatives were evaluated as monoamine oxidase (MAO) inhibitors using the human and rat isoforms of the enzyme. Molecular dockings were performed in order to gain insights regarding the binding mode of these inhibitors. All compounds were potent and selective MAO-A inhibitors although different rank orders of potencies were observed against the enzymes from different species. This behavior can be rationalized on the basis of different binding modes to each enzyme, as determined in silico. These findings further support the concept that MAO inhibitory activity of novel compounds, determined with enzymes from diverse mammalian species, should be considered with caution if human MAO is the final target to be addressed. © 2007 Elsevier Ltd. All rights reserved.

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Título según WOS: Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: Insights from molecular modeling studies
Título según SCOPUS: Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: Insights from molecular modeling studies
Título de la Revista: BIOORGANIC & MEDICINAL CHEMISTRY
Volumen: 15
Número: 15
Editorial: PERGAMON-ELSEVIER SCIENCE LTD
Fecha de publicación: 2007
Página de inicio: 5198
Página final: 5206
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S0968089607004208
DOI:

10.1016/j.bmc.2007.05.021

Notas: ISI, SCOPUS