Comparative Study of Binding Behaviors of Cyanidin, Cyanidin-3-Galactoside, Peonidin with Tyrosinase.
Autor: | Wang M; The College of Chemistry, Changchun Normal University, Changchun, 130032, China., Chen R; The College of Chemistry, Changchun Normal University, Changchun, 130032, China.; Zhaoqing Xuanqing Middle School, Zhaoqing, China., Wang S; The College of Chemistry, Changchun Normal University, Changchun, 130032, China., Cui J; The College of Chemistry, Changchun Normal University, Changchun, 130032, China., Lian D; The College of Chemistry, Changchun Normal University, Changchun, 130032, China., Li L; The College of Chemistry, Changchun Normal University, Changchun, 130032, China. lilchem@163.com. |
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Jazyk: | angličtina |
Zdroj: | Journal of fluorescence [J Fluoresc] 2024 Jul; Vol. 34 (4), pp. 1747-1760. Date of Electronic Publication: 2023 Aug 21. |
DOI: | 10.1007/s10895-023-03384-z |
Abstrakt: | Cyanidin, peonidin and cyanidin-3-galactoside are the common anthocyanins with a variety of biological activities. Tyrosinase is a speed-limiting enzyme associated with melanin production. The inhibition of tyrosinase activity can prevent melanin disease while contributing to whitening. The interaction behaviors of the three anthocyanins against tyrosinase have been discussed in this paper. Cyanidin has strongest inhibitory effect on tyrosinase, and then peonidin, cyanidin-3-galactoside. Furthermore, the inhibition of tyrosinase by the three anthocyanins is mixed modes. The three anthocyanins can induce the static fluorescence quenching of tyrosinase. Cyanidin exhibits strongest binding affinity on tyrosinase, and then peonidin, cyanidin-3-galactoside based on K (© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.) |
Databáze: | MEDLINE |
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