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.
Ga Young Lee  1 ,  Byoung Ok Cho  2 ,  Jae Young Shin  2 ,  Seon Il Jang  2 ,  In Sook Cho  3 ,  Hyo Young Kim  4 ,  Ji Su Park  1 ,  Chong Woon Cho  1 ,  Jong Seong Kang  1 ,  Jang Hoon Kim  5 ,  Young Ho Kim  6
Affiliations
  • 1. College of Pharmacy, Chungnam National University, Daejeon, 34134, Republic of Korea.
  • 2. Department of Health Care & Science, Jeonju University, Jeonju, 55069, Republic of Korea.
  • 3. Department of Horticultural and Crop Environment, National Institute of Horticultural and Herbal Science, RDA, Wanju, 55365, Republic of Korea.
  • 4. Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, 56212, Republic of Korea.
  • 5. Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, 56212, Republic of Korea. [email protected].
  • 6. College of Pharmacy, Chungnam National University, Daejeon, 34134, Republic of Korea. [email protected].
PMID: 29721815 DOI: 10.1007/s12272-018-1032-4
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.
Products