Selective inhibition of monoamine oxidase B by aminoethyl substituted benzyl ethers

Carolyn C. Woodroofe, Romayleh Mostashari, Xingliang Lu, Rona R. Ramsay, Richard B. Silverman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Aminoethyl 3-chlorobenzyl ether was shown previously to be a potent and selective time-dependent, but reversible inhibitor of monoamine oxidase B (MAO B). Based on this result, a series of novel aminoethyl substituted benzyl ethers was synthesized and the compounds were examined as potenial inhibitors of both isozymic forms of MAO. Each compound in the series inhibits both MAO A and MAO B competitively, and IC50 values for each compound were determined. In general, the B isozyme is much more sensitive to these inhibitors than the A isozyme (except for the o- and p-substituted nitro analogues), in some cases by more than two orders of magnitude. The selectivity in favor of MAO B inhibition is relatively high for all of the meta-substituted analogues and quite low for all of the ortho-substituted analogues. Having the substituent at the ortho-position is most favorable for MAO A inhibition. With MAO B the meta-analogues were, in general, more potent than the corresponding ortho- and para-analogues with respect to their reversible binding constants. The meta-iodo analogue is the most potent analogue.

Original languageEnglish (US)
Pages (from-to)11-21
Number of pages11
JournalJournal of Enzyme Inhibition
Volume15
Issue number1
StatePublished - Dec 1 1999

Keywords

  • Aminoethyl benzyl ethers
  • Inhibition
  • Monoamine oxidase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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