Two sulfur-containing heterodimers of a cytochalasan and a macrolide, sucurchalasins A and B ( and ), and four known cytochalasan monomers (-), as well as four known macrolide derivatives (-), were obtained from the endophytic fungus GDGJ-286. Sucurchalasins A and B ( and ) are the first cytochalasan heterodimers formed via a thioether bridge between cytochalasan and curvularin macrolide units. Their structures were elucidated by detailed analysis of NMR, LC-MS/MS, and X-ray crystallography. In bioassays, and exhibited cytotoxic effects on A2780 cells, with IC values of 3.9 and 8.3 μM, respectively. They also showed antibacterial activities against and with MIC values of 3.1 and 6.3 μg/mL, respectively.
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http://dx.doi.org/10.1021/acs.jnatprod.4c00489 | DOI Listing |
J Nat Prod
September 2024
State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources, Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources (Ministry of Education of China), Collaborative Innovation Center for Guangxi Ethnic Medicine, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, People's Republic of China.
Infect Drug Resist
October 2021
Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, Cd. México, 04510, México.
Background: Tuberculosis is an infectious disease caused by the bacillus . Compounds including a sulfur-containing scaffold have been shown to be key scaffolds in various antituberculosis agents. Interestingly, the 3-hydroxy-3-phenyl-prop-2-enedithioic acids have, to the best of our knowledge, not been previously described as antituberculosis agents.
View Article and Find Full Text PDFEur J Biochem
July 1991
Laboratorium für Mikrobiologie, Philipps Universität Marburg, Federal Republic of Germany.
L-Serine dehydratase with a specific activity of 15 nkat/mg protein was present in the anaerobic eubacterium Peptostreptococcus asaccharolyticus grown either on L-glutamate or L-serine. The enzyme was highly specific for L-serine with the lowest Km = 0.8 mM ever reported for an L-serine dehydratase.
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