2. Academic Validation
  3. Tyrosinase inhibitory components from the seeds of Cassia tora

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

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. oasis5325@gmail.com.
  • 6 College of Pharmacy, Chungnam National University, Daejeon, 34134, Republic of Korea. yhk@cnu.ac.kr.
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.

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