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.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1038/s41429-018-0044-0 | DOI Listing |
J Nat Prod
December 2024
Natural Products Research Institute, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.
New lipodepsipeptides, octaminomycins C and D ( and ), were discovered in an engineered sp. strain overexpressing the LysR transcriptional regulator family. The structures of and were elucidated by comprehensive analysis of their UV, HRMS, and NMR data.
View Article and Find Full Text PDFACS Omega
November 2024
Department of Pharmaceutical Sciences, Center for Biomolecular Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois 60612, United States.
We established a university-community partnership with the Boys and Girls Clubs of Chicago (BGCC)-named b-to involve middle school students in antibiotic discovery research. In the course of working with a cohort of students from the BGCC, one student isolated a bacterium from a goose feces sample that produced a new cyclic lipodepsipeptide, which was characterized as orfamide N. Orfamide N is composed of ten mixed D/L-amino acids and a ()-3-hydroxyhexadec-9-enoic acid residue.
View Article and Find Full Text PDFCommun Biol
November 2024
State Key Laboratory of Microbial Metabolism and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Rd., Shanghai, 200240, China.
Menaquinone (MK) in bacterial membrane is an attractive target for the development of novel therapeutic agents. Mining the untapped chemical diversity encoded by Gram-negative bacteria presents an opportunity to identify additional MK-binding antibiotics (MBAs). By MK-binding motif searching of bioinformatically predicted linear non-ribosomal peptides from 14,298 sequenced genomes of 45 underexplored Gram-negative bacterial genera, here we identify a novel MBA structural family, including silvmeb and pseudomeb, using structure prediction-guided chemical synthesis.
View Article and Find Full Text PDFACS Cent Sci
September 2024
Biomedicine Discovery Institute, Infection Program and Department of Pharmacology and Infection Program and Department of Microbiology, Monash University, Melbourne, VIC 3800, Australia.
A significant increase in life-threatening infections caused by Gram-negative "superbugs" is a serious threat to global health. With a dearth of new antibiotics in the developmental pipeline, antibiotics with novel mechanisms of action are urgently required to prevent a return to the preantibiotic era. A key strategy to develop novel anti-infective treatments is to discover new natural scaffolds with distinct mechanisms of action.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
November 2024
School of Biological Sciences, Victoria University of Wellington, 6012, Wellington, New Zealand.
Historically, small molecules biosynthesised by bacteria have been an excellent source for antibacterial drugs. Today, however, the rediscovery of known compounds is a significant hurdle to developing new antimicrobials. Here we use a genome mining and synthetic biology approach to discover the ambocidins: calcium-dependent lipodepsipeptides that are active against drug-resistant Gram-positive pathogens.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!