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The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase

The enzyme tyrosinase plays a key role in the early stages of melanin biosynthesis. This study evaluated the inhibitory activity of anthocyanidin (1) and anthocyanins (2–6) on the catalytic reaction. Of the six derivatives examined, 1–3 showed inhibitory activity with IC(50) values of 3.7 ± 0.1, 10....

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Autores principales: Yang, Seo Young, Kim, Jang Hoon, Su, Xiangdong, Kim, Jeong Ah
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458148/
https://www.ncbi.nlm.nih.gov/pubmed/36080469
http://dx.doi.org/10.3390/molecules27175703
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author Yang, Seo Young
Kim, Jang Hoon
Su, Xiangdong
Kim, Jeong Ah
author_facet Yang, Seo Young
Kim, Jang Hoon
Su, Xiangdong
Kim, Jeong Ah
author_sort Yang, Seo Young
collection PubMed
description The enzyme tyrosinase plays a key role in the early stages of melanin biosynthesis. This study evaluated the inhibitory activity of anthocyanidin (1) and anthocyanins (2–6) on the catalytic reaction. Of the six derivatives examined, 1–3 showed inhibitory activity with IC(50) values of 3.7 ± 0.1, 10.3 ± 1.0, and 41.3 ± 3.2 μM, respectively. Based on enzyme kinetics, 1–3 were confirmed to be competitive inhibitors with K(i) values of 2.8, 9.0, and 51.9 μM, respectively. Molecular docking analysis revealed the formation of a binary encounter complex between 1–3 and the tyrosinase catalytic site. Luteolinidin (1) and petunidin 3-O-glucoside (2) may serve as tyrosinase inhibitors to block melanin production.
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spelling pubmed-94581482022-09-09 The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase Yang, Seo Young Kim, Jang Hoon Su, Xiangdong Kim, Jeong Ah Molecules Article The enzyme tyrosinase plays a key role in the early stages of melanin biosynthesis. This study evaluated the inhibitory activity of anthocyanidin (1) and anthocyanins (2–6) on the catalytic reaction. Of the six derivatives examined, 1–3 showed inhibitory activity with IC(50) values of 3.7 ± 0.1, 10.3 ± 1.0, and 41.3 ± 3.2 μM, respectively. Based on enzyme kinetics, 1–3 were confirmed to be competitive inhibitors with K(i) values of 2.8, 9.0, and 51.9 μM, respectively. Molecular docking analysis revealed the formation of a binary encounter complex between 1–3 and the tyrosinase catalytic site. Luteolinidin (1) and petunidin 3-O-glucoside (2) may serve as tyrosinase inhibitors to block melanin production. MDPI 2022-09-04 /pmc/articles/PMC9458148/ /pubmed/36080469 http://dx.doi.org/10.3390/molecules27175703 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Yang, Seo Young
Kim, Jang Hoon
Su, Xiangdong
Kim, Jeong Ah
The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title_full The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title_fullStr The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title_full_unstemmed The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title_short The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase
title_sort luteolinidin and petunidin 3-o-glucoside: a competitive inhibitor of tyrosinase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458148/
https://www.ncbi.nlm.nih.gov/pubmed/36080469
http://dx.doi.org/10.3390/molecules27175703
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