Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102)
Abstract Two new cyclopentapeptides, xylapeptide A (1) with an uncommon L-pipecolinic acid moiety, and xylapeptide B (2) having a common L-proline residue were identified from an associated fungus Xylaria sp. isolated from the Chinese medicinal plant Sophora tonkinensis. Their planar structures were...
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2017
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oai:doaj.org-article:54f1a2416b1b442fa0a247efb28f8cde2021-12-02T15:04:59ZXylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102)10.1038/s41598-017-07331-42045-2322https://doaj.org/article/54f1a2416b1b442fa0a247efb28f8cde2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07331-4https://doaj.org/toc/2045-2322Abstract Two new cyclopentapeptides, xylapeptide A (1) with an uncommon L-pipecolinic acid moiety, and xylapeptide B (2) having a common L-proline residue were identified from an associated fungus Xylaria sp. isolated from the Chinese medicinal plant Sophora tonkinensis. Their planar structures were elucidated by a comprehensive analysis of NMR and MS spectroscopic spectra. The absolute configurations were determined by Marfey’s method and single-crystal X-ray diffraction (Cu Kα) analysis. Xylapeptide A (1) is the first example of cyclopentapeptide with L-Pip of terrestrial origin and showed strong antibacterial activity against Bacillus subtilis and B. cereus with MIC value of 12.5 μg/mL.Wei-Feng XuXue-Mei HouFei-Hua YaoNa ZhengJun LiChang-Yun WangRui-Yun YangChang-Lun ShaoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017) |
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Medicine R Science Q Wei-Feng Xu Xue-Mei Hou Fei-Hua Yao Na Zheng Jun Li Chang-Yun Wang Rui-Yun Yang Chang-Lun Shao Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
description |
Abstract Two new cyclopentapeptides, xylapeptide A (1) with an uncommon L-pipecolinic acid moiety, and xylapeptide B (2) having a common L-proline residue were identified from an associated fungus Xylaria sp. isolated from the Chinese medicinal plant Sophora tonkinensis. Their planar structures were elucidated by a comprehensive analysis of NMR and MS spectroscopic spectra. The absolute configurations were determined by Marfey’s method and single-crystal X-ray diffraction (Cu Kα) analysis. Xylapeptide A (1) is the first example of cyclopentapeptide with L-Pip of terrestrial origin and showed strong antibacterial activity against Bacillus subtilis and B. cereus with MIC value of 12.5 μg/mL. |
format |
article |
author |
Wei-Feng Xu Xue-Mei Hou Fei-Hua Yao Na Zheng Jun Li Chang-Yun Wang Rui-Yun Yang Chang-Lun Shao |
author_facet |
Wei-Feng Xu Xue-Mei Hou Fei-Hua Yao Na Zheng Jun Li Chang-Yun Wang Rui-Yun Yang Chang-Lun Shao |
author_sort |
Wei-Feng Xu |
title |
Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
title_short |
Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
title_full |
Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
title_fullStr |
Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
title_full_unstemmed |
Xylapeptide A, an Antibacterial Cyclopentapeptide with an Uncommon L-Pipecolinic Acid Moiety from the Associated Fungus Xylaria sp. (GDG-102) |
title_sort |
xylapeptide a, an antibacterial cyclopentapeptide with an uncommon l-pipecolinic acid moiety from the associated fungus xylaria sp. (gdg-102) |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/54f1a2416b1b442fa0a247efb28f8cde |
work_keys_str_mv |
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