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.
| Original language | English |
|---|---|
| Pages (from-to) | 1425-1428 |
| Number of pages | 4 |
| Journal | Journal of Microbiology and Biotechnology |
| Volume | 25 |
| Issue number | 9 |
| DOIs | |
| State | Published - 2 Jun 2015 |
Bibliographical note
Publisher Copyright:© 2015 by The Korean Society for Microbiology and Biotechnology.
Keywords
- Anithiactin A
- Competitive inhibitor
- Monoamine oxidase
- Selective inhibitor
- Streptomyces sp