Artículos de revistas
Why p-OMe- and p-Cl-β-Methylphenethylamines display distinct activities upon MAO-B binding
Fecha
2016Registro en:
PLoS ONE, Volumen 11, Issue 5, 2018,
19326203
10.1371/journal.pone.0154989
Autor
Fierro, Angélica
Edmondson, Dale E.
Celis-Barros, Cristian
Rebolledo-Fuentes, Marco
Zapata-Torres, Gerald
Institución
Resumen
© 2016 Fierro et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Despite their structural and chemical commonalities, p-chloro-β-methylphenethylamine and p-methoxy-β-methylphenethylamine display distinct inhibitory and substrate activities upon MAO-B binding. Density Functional Theory (DFT) quantum chemical calculations reveal that β-methylation and para-substitution underpin the observed activities sustained by calculated transition state energy barriers, attained conformations and key differences in their interactions in the enzyme's substrate binding site. Although both compounds meet substrate requirements, it is clear that β-methylation along with the physicochemical features of the para-substituents on the aromatic ring determine the activity of these compounds upon binding to the MAO B-isof