Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish

Tyrosinase is an oxidase that is the rate-limiting enzyme for controlling the production of melanin in the human body. Overproduction of melanin can lead to a variety of skin disorders. Calycosin is an isoflavone from Astragali Radix, which is a traditional Chinese medicine that exhibits several pha...

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Autores principales:	Nilupaier Tayier, Ning-Yi Qin, Li-Nan Zhao, Yi Zeng, Yu Wang, Guang Hu, Yuan-Qiang Wang
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	calycosin tyrosinase melanin zebrafish molecular docking Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/08efd68dd9854db5bbc5b6f0d1721eb8
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spelling	oai:doaj.org-article:08efd68dd9854db5bbc5b6f0d1721eb82021-11-25T18:29:00ZTheoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish10.3390/molecules262269981420-3049https://doaj.org/article/08efd68dd9854db5bbc5b6f0d1721eb82021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/22/6998https://doaj.org/toc/1420-3049Tyrosinase is an oxidase that is the rate-limiting enzyme for controlling the production of melanin in the human body. Overproduction of melanin can lead to a variety of skin disorders. Calycosin is an isoflavone from Astragali Radix, which is a traditional Chinese medicine that exhibits several pharmacological activities including skin whitening. In our study, the inhibitory effect of calycosin on melanin production is confirmed in a zebrafish in vivo model by comparing with hydroquinone, kojic acid, and arbutin, known as tyrosinase inhibitors. Moreover, the inhibitory kinetics of calycosin on tyrosinase and their binding mechanisms are determined using molecular docking techniques, molecular dynamic simulations, and free energy analysis. The results indicate that calycosin has an obvious inhibitory effect on zebrafish pigmentation at the concentration of 7.5 μM, 15 μM, and 30 μM. The IC<sub>50</sub> of calycosin is 30.35 μM, which is lower than hydroquinone (37.35 μM), kojic acid (6.51 × 10<sup>3</sup> μM), and arbutin (3.67 × 10<sup>4</sup> μM). Furthermore, all the results of molecular docking, molecular dynamics simulations, and free energy analysis suggest that calycosin can directly bind to the active site of tyrosinase with very good binding affinity. The study indicates that the combination of computer molecular modeling and zebrafish in vivo assay would be feasible in confirming the result of the in vitro test and illustrating the target-binding information.Nilupaier TayierNing-Yi QinLi-Nan ZhaoYi ZengYu WangGuang HuYuan-Qiang WangMDPI AGarticlecalycosintyrosinasemelaninzebrafishmolecular dockingOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6998, p 6998 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	calycosin tyrosinase melanin zebrafish molecular docking Organic chemistry QD241-441
spellingShingle	calycosin tyrosinase melanin zebrafish molecular docking Organic chemistry QD241-441 Nilupaier Tayier Ning-Yi Qin Li-Nan Zhao Yi Zeng Yu Wang Guang Hu Yuan-Qiang Wang Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
description	Tyrosinase is an oxidase that is the rate-limiting enzyme for controlling the production of melanin in the human body. Overproduction of melanin can lead to a variety of skin disorders. Calycosin is an isoflavone from Astragali Radix, which is a traditional Chinese medicine that exhibits several pharmacological activities including skin whitening. In our study, the inhibitory effect of calycosin on melanin production is confirmed in a zebrafish in vivo model by comparing with hydroquinone, kojic acid, and arbutin, known as tyrosinase inhibitors. Moreover, the inhibitory kinetics of calycosin on tyrosinase and their binding mechanisms are determined using molecular docking techniques, molecular dynamic simulations, and free energy analysis. The results indicate that calycosin has an obvious inhibitory effect on zebrafish pigmentation at the concentration of 7.5 μM, 15 μM, and 30 μM. The IC<sub>50</sub> of calycosin is 30.35 μM, which is lower than hydroquinone (37.35 μM), kojic acid (6.51 × 10<sup>3</sup> μM), and arbutin (3.67 × 10<sup>4</sup> μM). Furthermore, all the results of molecular docking, molecular dynamics simulations, and free energy analysis suggest that calycosin can directly bind to the active site of tyrosinase with very good binding affinity. The study indicates that the combination of computer molecular modeling and zebrafish in vivo assay would be feasible in confirming the result of the in vitro test and illustrating the target-binding information.
format	article
author	Nilupaier Tayier Ning-Yi Qin Li-Nan Zhao Yi Zeng Yu Wang Guang Hu Yuan-Qiang Wang
author_facet	Nilupaier Tayier Ning-Yi Qin Li-Nan Zhao Yi Zeng Yu Wang Guang Hu Yuan-Qiang Wang
author_sort	Nilupaier Tayier
title	Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
title_short	Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
title_full	Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
title_fullStr	Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
title_full_unstemmed	Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish
title_sort	theoretical exploring of a molecular mechanism for melanin inhibitory activity of calycosin in zebrafish
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/08efd68dd9854db5bbc5b6f0d1721eb8
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_version_	1718411056966008832

Theoretical Exploring of a Molecular Mechanism for Melanin Inhibitory Activity of Calycosin in Zebrafish

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