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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.
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http://dx.doi.org/10.1038/s41429-018-0044-0 | DOI Listing |
Chembiochem
June 2025
Institut für Biotechnologie und Wirkstoff-Forschung gGmbH, Hanns-Dieter-Hüsch Weg 17, 55128, Mainz, Germany.
Bioactivity-guided isolation led to the identification of the cyclic lipodepsipeptide pleosporacin (1) from the mycelia extract of fungal strain Pleosporales sp. IBWF 020-21, a potent selective inhibitor of the fungal phytopathogen Botrytis cinerea. The structure and stereochemistry of 1 were elucidated by NMR and Marfey analysis, respectively.
View Article and Find Full Text PDFmBio
May 2025
Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (Leibniz-HKI), Jena, Germany.
is an environmental bacterium that can cause severe and fatal opportunistic infections in humans and animals. Although is characterized by its strong β-hemolytic activity, the molecular basis of this phenotype has remained elusive over the more than 15 years since the species was first described. Herein, we report a family of cyclic lipodepsipeptides, the jagaricins, that are responsible for the potent hemolytic activity of .
View Article and Find Full Text PDFProg Mol Biol Transl Sci
March 2025
Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL, United States.
Daptomycin is a cyclic lipodepsipeptide antibiotic that is a mainstay for the treatment of serious infections caused by Gram-positive bacteria, including methicillin-resistant Streptococcus aureus and vancomycin resistant enterococci. It is one of the so-called last-resort antibiotics that are used to tackle life-threatening infections that do not respond to first-line treatments. However, resistance to daptomycin is eroding its clinical efficacy motivating the design and/or discovery of analogues that overcome resistance.
View Article and Find Full Text PDFOrg Lett
March 2025
Friedrich Schiller University Jena, Institute for Organic Chemistry and Macromol. Chemistry, Humboldtstr. 10, D-07743 Jena, Germany.
The total synthesis of -derived cyclic lipodepsipeptide anikasin was achieved. Using a depsipeptide building block and balanced protecting groups on the branching d--Thr residue, the synthesis was established semiautomatically on a synthesizer. Buffered deprotections minimized side reactions and afforded synthetic anikasin and its enantiomer.
View Article and Find Full Text PDFJ Nat Prod
March 2025
Department of Pharmaceutical Sciences, College of Pharmacy, University of Illinois Chicago, Chicago, Illinois 60612, United States.
Menominin A () and B (), two cyclodepsipeptides containing a 3,8-dihydroxy-2-methyltetradecanoic acid residue, were isolated from the freshwater sponge-associated cyanobacterium, sp. UIC 10607, using bioactivity-guided and spectroscopic approaches. The planar structures of and were established using HRESIMS and one- and two-dimensional NMR experiments.
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