Tyrosinase inhibitory components from the seeds of Cassia tora

Arch Pharm Res. 2018 May;41(5):490-496. doi: 10.1007/s12272-018-1032-4. Epub 2018 May 2.

Abstract

Ten compounds (1-10) isolated from the seeds of Cassia tora were evaluated for tyrosinase inhibition. Compounds 3, 4, and 7 inhibited tyrosinase enzymatic activity in a dose-dependent manner, with IC50 values of 3.0 ± 0.8, 7.0 ± 0.4, and 9.2 ± 3.4 μM, respectively. Kinetic analyses revealed a mechanism consistent with competitive inhibition. In silico molecular docking showed that compounds 3 and 4 docked in the active site of tyrosinase, whereas 7 interacted with Ala246 and Val248 at outside of the active site, and His244 and Glu256 at inside. Additionally, compounds 3, 4, and 7 suppressed melanogenesis in α-MSH-treated B16F10 melanoma cells at a concentration of 10 μM.

Keywords: Cassia tora; Competitive type; Melanogenesis; Molecular docking; Tyrosinase inhibitor.

MeSH terms

  • Animals
  • Cinnamomum aromaticum / chemistry*
  • Dose-Response Relationship, Drug
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Mice
  • Molecular Docking Simulation
  • Molecular Structure
  • Monophenol Monooxygenase / antagonists & inhibitors*
  • Monophenol Monooxygenase / metabolism
  • Plant Extracts / chemistry
  • Plant Extracts / isolation & purification
  • Plant Extracts / pharmacology*
  • Seeds / chemistry*
  • Structure-Activity Relationship
  • Tumor Cells, Cultured

Substances

  • Enzyme Inhibitors
  • Plant Extracts
  • Monophenol Monooxygenase