Cystargamide B, a cyclic lipodepsipeptide with protease inhibitory activity from Streptomyces sp
| Autor: | Atchareeya A-nuegoonpipat, Takeshi Kurosu, Takuya Nihira, Mitsuki Yoshida, Kazuyoshi Ikuta, Yasuhiro Igarashi, Ousana Boonlucksanawong, Shigeru Kitani, Watanalai Panbangred |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Magnetic Resonance Spectroscopy Stereochemistry medicine.medical_treatment Molecular Conformation Spectrometry Mass Fast Atom Bombardment Streptomyces 03 medical and health sciences Residue (chemistry) Zingiberaceae Depsipeptides Drug Discovery medicine Kaempferia galanga Protease Inhibitors Pharmacology chemistry.chemical_classification Protease biology Fatty acid Nuclear magnetic resonance spectroscopy Dengue Virus Fast atom bombardment biology.organism_classification Amino acid 030104 developmental biology chemistry Rhizome |
| Zdroj: | The Journal of Antibiotics. 71:662-666 |
| ISSN: | 1881-1469 0021-8820 |
| DOI: | 10.1038/s41429-018-0044-0 |
| Popis: | We identified a new cyclic lipodepsipeptide, cystargamide B (1), from the mycelial extract of a Kaempferia galanga rhizome-derived actinomycete strain, Streptomyces sp. PB013. The planar structure was elucidated based on high resolution fast-atom bombardment mass spectrometry (HRFABMS) spectroscopy and one-dimensional (1D) and two-dimensional (2D) nuclear magnetic resonance (NMR) spectroscopic data. The absolute configurations of the constituent amino acids were determined using advanced Marfey's method. Cystargamide B (1) includes rare structural units: a 5-hydroxytryptophan residue and a 2,3-epoxy fatty acid side chain. Notably, cystargamide B (1) inhibited the protease activity of the NS2B/NS3 complex from dengue virus. |
| Databáze: | OpenAIRE |
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