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New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne

Five new sesterterpenoids, compounds 1–5, have been isolated from the sponge Hippospongia lachne off Yongxing Island in the South China Sea. The structures of compounds 1–5 were elucidated through extensive spectroscopic analysis, including HRMS, 1D, and 2D NMR experiments. The stereochemistry, incl...

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Detalles Bibliográficos
Autores principales: Piao, Shu-Juan, Jiao, Wei-Hua, Yang, Fan, Yi, Yang-Hua, Di, Ying-Tong, Han, Bing-Nan, Lin, Hou-Wen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4113817/
https://www.ncbi.nlm.nih.gov/pubmed/25007159
http://dx.doi.org/10.3390/md12074096
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author Piao, Shu-Juan
Jiao, Wei-Hua
Yang, Fan
Yi, Yang-Hua
Di, Ying-Tong
Han, Bing-Nan
Lin, Hou-Wen
author_facet Piao, Shu-Juan
Jiao, Wei-Hua
Yang, Fan
Yi, Yang-Hua
Di, Ying-Tong
Han, Bing-Nan
Lin, Hou-Wen
author_sort Piao, Shu-Juan
collection PubMed
description Five new sesterterpenoids, compounds 1–5, have been isolated from the sponge Hippospongia lachne off Yongxing Island in the South China Sea. The structures of compounds 1–5 were elucidated through extensive spectroscopic analysis, including HRMS, 1D, and 2D NMR experiments. The stereochemistry, including absolute configurations of these compounds, was determined by spectroscopic, chemical, and computational methods. Compounds 1 and 5 showed moderate protein tyrosine phosphatase 1B (PTP1B) inhibitory activities with IC(50) values of 5.2 μM and 8.7 μM, respectively, more potent than previously reported hippolides.
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spelling pubmed-41138172014-07-29 New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne Piao, Shu-Juan Jiao, Wei-Hua Yang, Fan Yi, Yang-Hua Di, Ying-Tong Han, Bing-Nan Lin, Hou-Wen Mar Drugs Article Five new sesterterpenoids, compounds 1–5, have been isolated from the sponge Hippospongia lachne off Yongxing Island in the South China Sea. The structures of compounds 1–5 were elucidated through extensive spectroscopic analysis, including HRMS, 1D, and 2D NMR experiments. The stereochemistry, including absolute configurations of these compounds, was determined by spectroscopic, chemical, and computational methods. Compounds 1 and 5 showed moderate protein tyrosine phosphatase 1B (PTP1B) inhibitory activities with IC(50) values of 5.2 μM and 8.7 μM, respectively, more potent than previously reported hippolides. MDPI 2014-07-08 /pmc/articles/PMC4113817/ /pubmed/25007159 http://dx.doi.org/10.3390/md12074096 Text en © 2014 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 license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Piao, Shu-Juan
Jiao, Wei-Hua
Yang, Fan
Yi, Yang-Hua
Di, Ying-Tong
Han, Bing-Nan
Lin, Hou-Wen
New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title_full New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title_fullStr New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title_full_unstemmed New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title_short New Hippolide Derivatives with Protein Tyrosine Phosphatase 1B Inhibitory Activity from the Marine Sponge Hippospongia lachne
title_sort new hippolide derivatives with protein tyrosine phosphatase 1b inhibitory activity from the marine sponge hippospongia lachne
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4113817/
https://www.ncbi.nlm.nih.gov/pubmed/25007159
http://dx.doi.org/10.3390/md12074096
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