Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius

Two new stilbene derivatives, named strebluses C and D, were isolated from the EtOAc-soluble fraction of the stems of Streblus ilicifolius (Moraceae). Its absolute configuration was elucidated based on NMR spectroscopic data interpretation and optical rotation calculation. Streblus C possesses stron...

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Autores principales: Nguyen, Nhan T., Dang, Phu H., Nguyen, Hai X., Do, Truong N. V., Le, Tho H., Le, Tuyen Q. H., Nguyen, Mai T. T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2021
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8266447/
https://www.ncbi.nlm.nih.gov/pubmed/34306141
http://dx.doi.org/10.1155/2021/5561176
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author Nguyen, Nhan T.
Dang, Phu H.
Nguyen, Hai X.
Do, Truong N. V.
Le, Tho H.
Le, Tuyen Q. H.
Nguyen, Mai T. T.
author_facet Nguyen, Nhan T.
Dang, Phu H.
Nguyen, Hai X.
Do, Truong N. V.
Le, Tho H.
Le, Tuyen Q. H.
Nguyen, Mai T. T.
author_sort Nguyen, Nhan T.
collection PubMed
description Two new stilbene derivatives, named strebluses C and D, were isolated from the EtOAc-soluble fraction of the stems of Streblus ilicifolius (Moraceae). Its absolute configuration was elucidated based on NMR spectroscopic data interpretation and optical rotation calculation. Streblus C possesses strong tyrosinase inhibitory activity with an IC(50) value of 0.01 μM. Docking studies of 1 and 2 with oxy-tyrosinase were carried out to analyze their interactions. The analysis of the docked poses confirmed that 1 showed better binding affinity for oxy-tyrosinase than that of 2.
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spelling pubmed-82664472021-07-22 Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius Nguyen, Nhan T. Dang, Phu H. Nguyen, Hai X. Do, Truong N. V. Le, Tho H. Le, Tuyen Q. H. Nguyen, Mai T. T. Evid Based Complement Alternat Med Research Article Two new stilbene derivatives, named strebluses C and D, were isolated from the EtOAc-soluble fraction of the stems of Streblus ilicifolius (Moraceae). Its absolute configuration was elucidated based on NMR spectroscopic data interpretation and optical rotation calculation. Streblus C possesses strong tyrosinase inhibitory activity with an IC(50) value of 0.01 μM. Docking studies of 1 and 2 with oxy-tyrosinase were carried out to analyze their interactions. The analysis of the docked poses confirmed that 1 showed better binding affinity for oxy-tyrosinase than that of 2. Hindawi 2021-07-01 /pmc/articles/PMC8266447/ /pubmed/34306141 http://dx.doi.org/10.1155/2021/5561176 Text en Copyright © 2021 Nhan T. Nguyen et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Nguyen, Nhan T.
Dang, Phu H.
Nguyen, Hai X.
Do, Truong N. V.
Le, Tho H.
Le, Tuyen Q. H.
Nguyen, Mai T. T.
Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title_full Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title_fullStr Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title_full_unstemmed Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title_short Tyrosinase Inhibitors from the Stems of Streblus Ilicifolius
title_sort tyrosinase inhibitors from the stems of streblus ilicifolius
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8266447/
https://www.ncbi.nlm.nih.gov/pubmed/34306141
http://dx.doi.org/10.1155/2021/5561176
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