Stylbasole analogues of MPTP as monoamine oxidase (MAO) substrates.

Abstract

Stylbasole analogs of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) were studied as monoamine oxidase (MAO) substrates. Dehydrogenation of these compounds was shown to be catalyzed by both serotonine specifical and benzylamine specifical MAO activities. Markedly high affinity of stylbasoles to B type of MAO was found. Influence of substrate structure on its biotransformation effectiveness is realized by the principle--"better binding-worse catalysis". MAO inactivation during the reaction is appeared to be realized as result of product inhibition and perhaps of substrate inhibition.