Screen of monoamine oxidase inhibitors by protein-liposome conjugate capillary electrophoresis

Bing Li, Xue Fei Lü, Hong Qing, Yu Lin Deng*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Based on the interaction between enzyme and substrate, a simple and elegant method was developed to screen the inhibitors of monoamine oxidase (MAO). Four kinds of N-propargyl amine compounds with gradient concentrations were added in the CE running buffer solution containing protein-liposome conjugate to inhibit the activity of MAO to some extent. The relative migration time ratio (RMTR) of Kyn was investigated in running buffer solution containing different compounds in gradient concentrations. The results indicate that R-N-(2-heptyl)-N- methylpropargylamine (R-2-HMP) and N-propargyl-R-2-heptylamine (R-2-HPA) could inhibit the activity of MAO obviously, such that the interaction between MAO and Kyn was weakened, RMTR of Kyn increased with the increase of R-2-HMP and R-2-HPA. The inhibition activities of N-dipropargyl-R-2-hexylamine and N, N-dipropargyl-R-2-octylamine were not obvious; RMTR of Kyn changed little with the increase of the two compounds. This result was consistent with that of activity assay of compounds incubation offline. In comparison with the traditional screening method for MAO inhibitors, this method is rapid, low cost, less consumption of enzyme and independent of voltage and other interference factors.

Original languageEnglish
Pages (from-to)1336-1340
Number of pages5
JournalChinese Journal of Analytical Chemistry
Volume40
Issue number9
DOIs
Publication statusPublished - Sept 2012

Keywords

  • Capillary electrophoresis
  • Inhibitors
  • Interaction
  • Liposome
  • Monoamine oxidase

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