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Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.

Tyrosinase inhibitors are of far-ranging importance in cosmetics, medicinal products, and food industries. Peru is a diverse country with a wide variety of plants that may contain excellent anti-tyrosinase inhibitors. In the present study, the tyrosinase inhibitory properties of 50 medicinal plant e...

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Autores principales: Guillen Quispe, Yanymee Nimesia, Hwang, Seung Hwan, Wang, Zhiqiang, Lim, Soon Sung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155296/
https://www.ncbi.nlm.nih.gov/pubmed/28273864
http://dx.doi.org/10.3390/molecules22030402
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author Guillen Quispe, Yanymee Nimesia
Hwang, Seung Hwan
Wang, Zhiqiang
Lim, Soon Sung
author_facet Guillen Quispe, Yanymee Nimesia
Hwang, Seung Hwan
Wang, Zhiqiang
Lim, Soon Sung
author_sort Guillen Quispe, Yanymee Nimesia
collection PubMed
description Tyrosinase inhibitors are of far-ranging importance in cosmetics, medicinal products, and food industries. Peru is a diverse country with a wide variety of plants that may contain excellent anti-tyrosinase inhibitors. In the present study, the tyrosinase inhibitory properties of 50 medicinal plant extracts from Peru were investigated using tyrosinase assay. Among plant extracts, those that showed an inhibition rate >50% were Hypericum laricifolium Juss., Taraxacum officinale F.H.Wigg., and Muehlenbeckia vulcanica Meisn., with H. laricifolium Juss. showing the greatest anti-tyrosinase activity. Although H. laricifolium Juss. has been widely used as a medicinal plant by Peruvians, little is known regarding its bioactive components and effects on tyrosinase activity. For this reason, we attempted to discover tyrosinase inhibitors in H. laricifolium Juss. for the first time. The bioactive components were separated by Sephadex LH-20 chromatography and eluted with 100% methanol. Eight compounds were discovered and characterized by high-performance liquid chromatography coupled with diode array detection (HPLC-DAD): protocatechuic acid, p-hydroxybenzoic acid, chlorogenic acid, vanilic acid, caffeic acid, kaempferol 3-O-glucuronide, quercetin, and kaempferol. In addition, the concentration of these compounds required for 50% inhibition (IC(50)) of tyrosinase activity were evaluated. Quercetin exhibited the strongest tyrosinase inhibition (IC(50) 14.29 ± 0.3 μM). Therefore, the Peruvian plant H. laricifolium Juss. could be a novel source for anti-tyrosinase activity.
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spelling pubmed-61552962018-11-13 Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss. Guillen Quispe, Yanymee Nimesia Hwang, Seung Hwan Wang, Zhiqiang Lim, Soon Sung Molecules Article Tyrosinase inhibitors are of far-ranging importance in cosmetics, medicinal products, and food industries. Peru is a diverse country with a wide variety of plants that may contain excellent anti-tyrosinase inhibitors. In the present study, the tyrosinase inhibitory properties of 50 medicinal plant extracts from Peru were investigated using tyrosinase assay. Among plant extracts, those that showed an inhibition rate >50% were Hypericum laricifolium Juss., Taraxacum officinale F.H.Wigg., and Muehlenbeckia vulcanica Meisn., with H. laricifolium Juss. showing the greatest anti-tyrosinase activity. Although H. laricifolium Juss. has been widely used as a medicinal plant by Peruvians, little is known regarding its bioactive components and effects on tyrosinase activity. For this reason, we attempted to discover tyrosinase inhibitors in H. laricifolium Juss. for the first time. The bioactive components were separated by Sephadex LH-20 chromatography and eluted with 100% methanol. Eight compounds were discovered and characterized by high-performance liquid chromatography coupled with diode array detection (HPLC-DAD): protocatechuic acid, p-hydroxybenzoic acid, chlorogenic acid, vanilic acid, caffeic acid, kaempferol 3-O-glucuronide, quercetin, and kaempferol. In addition, the concentration of these compounds required for 50% inhibition (IC(50)) of tyrosinase activity were evaluated. Quercetin exhibited the strongest tyrosinase inhibition (IC(50) 14.29 ± 0.3 μM). Therefore, the Peruvian plant H. laricifolium Juss. could be a novel source for anti-tyrosinase activity. MDPI 2017-03-04 /pmc/articles/PMC6155296/ /pubmed/28273864 http://dx.doi.org/10.3390/molecules22030402 Text en © 2017 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Guillen Quispe, Yanymee Nimesia
Hwang, Seung Hwan
Wang, Zhiqiang
Lim, Soon Sung
Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title_full Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title_fullStr Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title_full_unstemmed Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title_short Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss.
title_sort screening of peruvian medicinal plants for tyrosinase inhibitory properties: identification of tyrosinase inhibitors in hypericum laricifolium juss.
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155296/
https://www.ncbi.nlm.nih.gov/pubmed/28273864
http://dx.doi.org/10.3390/molecules22030402
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