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Inhibition of Monoamine Oxidase by Anithiactins from Streptomyces sp.

  • Lee, Hyun Woo (Department of Pharmacy, Sunchon National University) ;
  • Jung, Won Kyeong (Research Institute of Life Pharmaceutical Sciences, Sunchon National University) ;
  • Kim, Hee Jung (Department of Pharmacy, Sunchon National University) ;
  • Jeong, Yu Seok (Department of Pharmacy, Sunchon National University) ;
  • Nam, Sang-Jip (Department of Chemistry and Nano Science, Ewha Women’s University) ;
  • Kang, Heonjoong (Center for Marine Natural Products and Drug Discovery, School of Earth and Environmental Sciences, Seoul National University) ;
  • Kim, Hoon (Department of Pharmacy, Sunchon National University)
  • Received : 2015.05.08
  • Accepted : 2015.05.27
  • Published : 2015.09.28

Abstract

Monoamine oxidase (MAO) is found in most cell types and catalyzes the oxidation of monoamines. Three anithiactins (A-C, modified 2-phenylthiazoles) isolated from Streptomyces sp. were tested for inhibitory activity of two isoforms, MAO-A and MAO-B. Anithiactin A was effective and selective for the inhibition of MAO-A, with an IC50 value of 13.0 μM; however, it was not effective for the inhibition of MAO-B. Anithiactins B and C were weaker inhibitors for MAO-A and MAO-B. Anithiactin A was a reversible and competitive inhibitor for MAO-A with a Ki value of 1.84 μM. The hydrophobic methyl substituent in anithiactin A may play an important role in the inhibition of MAO-A. It is suggested that anithiactin A is a selective reversible inhibitor for MAO-A, with moderate potency, and can be considered a new potential lead compound for further development of novel reversible inhibitors for MAO-A.

Keywords

References

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