4.6 Article

Valonea Tannin: Tyrosinase Inhibition Activity, Structural Elucidation and Insights into the Inhibition Mechanism

期刊

MOLECULES
卷 26, 期 9, 页码 -

出版社

MDPI
DOI: 10.3390/molecules26092747

关键词

valonea tannin; hydrolysable tannin; tyrosinase; enzyme binding; enzyme inhibition; inhibition mechanism

资金

  1. Natural Science Foundation of Guangdong Province, China [2020A1515011357]
  2. Department of Education of Guangdong Province, China [2018KQNCX081]
  3. Research and Development Start-up Foundation [NTF18031]

向作者/读者索取更多资源

Valonea tannin is a highly effective natural tyrosinase inhibitor with skin whitening properties, which inhibits the enzyme through a mixed competitive-uncompetitive mechanism. The substance binds non-selectively to the surface of tyrosinase via hydrogen bonds and hydrophobic interactions, and also possesses copper ion chelating and antioxidant abilities.
Valonea tannin is a natural product readily extracted from acorn shells that has been suggested to have potential skin whitening properties. This study investigated the tyrosinase inhibition activity of extracted valonea tannin and the associated structure-function activity. Nuclear magnetic resonance spectroscopy and molecular weight analysis with gel permeation chromatography revealed that valonea tannin could be characterized as a hydrolysable tannin with galloyl, hexahydroxydiphenoyl and open formed-glucose moieties and an average molecular weight of 3042 +/- 15 Da. Tyrosinase inhibition assays demonstrated that valonea tannin was 334 times more effective than gallic acid and 3.4 times more effective than tannic acid, which may relate to the larger molecular size. Kinetic studies of the inhibition reactions indicated that valonea tannin provided tyrosinase inhibition through mixed competitive-uncompetitive way. Stern-Volmer fitted fluorescence quenching analysis, isothermal titration calorimetry analysis and in silico molecule docking showed valonea tannin non-selectively bound to the surface of tyrosinase via hydrogen bonds and hydrophobic interactions. Inductively coupled plasma-optical emission spectroscopy and free radical scavenging assays indicated the valonea tannin had copper ion chelating and antioxidant ability, which may also contribute to inhibition activity. These results demonstrated the structure-function activity of valonea tannin as a highly effective natural tyrosinase inhibitor that may have commercial application in dermatological medicines or cosmetic products.

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