Flexible N-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine Analogues: Synthesis and Monoamine Oxidase Catalyzed Bioactivation

S. M.N. Efange, R. H. Michelson, R. P. Remmel, R. J. Boudreau, A. K. Dutta, A. Freshler

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Abstract

Eighteen analogues of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) were synthesized and evaluated as substrates of monoamine oxidase. In general, the flexible analogues, characterized by the presence of a methylene (or ethylene) bridge between the aryl/heteroaryl and tetrahydropyridyl moieties, were better substrates of the enzyme than the conformationally restricted MPTP. It is suggested that the increased oxidative activity of these flexible analogues reflects enhanced binding due to the ability of the C-4-aryl/heteroaryl substituent to gain access to a hydrophobic pocket within the substrate binding site.

Original languageEnglish (US)
Pages (from-to)3133-3138
Number of pages6
JournalJournal of Medicinal Chemistry
Volume33
Issue number12
DOIs
StatePublished - Dec 1990

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