Rugulactone is a natural product isolated from the plant . It has shown very important biological activity as an inhibitor of the nuclear factor κB (NF-κB) activation pathway. A new chemoenzymatic approach towards the synthesis of rugulactone is presented here. The chirality, induced to the key intermediate by a stereoselective enzymatic reduction utilizing NADPH-dependent ketoreductase, is described in detail.
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http://dx.doi.org/10.3390/molecules23030640 | DOI Listing |
Biomedicines
January 2025
Department of Chemistry and Biochemistry, Augusta University, Augusta, GA 30912, USA.
Natural cyclic peptides, a diverse class of bioactive compounds, have been isolated from various natural sources and are renowned for their extensive structural variability and broad spectrum of medicinal properties. Over 40 cyclic peptides or their derivatives are currently approved as medicines, underscoring their significant therapeutic potential. These compounds are employed in diverse roles, including antibiotics, antifungals, antiparasitics, immune modulators, and anti-inflammatory agents.
View Article and Find Full Text PDFChembiochem
January 2025
Institut Pasteur, Department of Structural Biology and Chemistry, 28 Rue du Dr. Roux, 75015, Paris, FRANCE.
Access to synthetic oligonucleotides is crucial for applications in diagnostics, therapeutics, synthetic biology, and nanotechnology. Traditional solid phase synthesis is limited by sequence length and complexities, low yields, high costs and poor sustainability. Similarly, polymerase-based approaches such as in vitro transcription and primer extension reactions do not permit any control on the positioning of modifications and display poor substrate tolerance.
View Article and Find Full Text PDFChembiochem
January 2025
National Glycoengineering Research Center, Shandong Provincial Key Laboratory of Glycochemistry and Glycobiology, Shandong University, Qingdao, Shandong, 266237, P. R China.
Nucleotide sugars (NSs) are essential building blocks for the enzymatic assembly of glycans. In this study, we established a preparation and recycling avenue to the biocatalysts for the enzymatic synthesis of NSs. This approach involves fusing two enzymes into a bifunctional chimera and using elastin-like polypeptides (ET64) as a purification tag, which allows for easy recovery of these biocatalysts without the need for chromatography.
View Article and Find Full Text PDFChem Rev
January 2025
Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York 14853, United States.
Cells contain thousands of different lipids. Their rapid and redundant metabolism, dynamic movement, and many interactions with other biomolecules have justly earned lipids a reputation as a vexing class of molecules to understand. Further, as the cell's hydrophobic metabolites, lipids assemble into supramolecular structures─most commonly bilayers, or membranes─from which they carry out myriad biological functions.
View Article and Find Full Text PDFOrg Lett
January 2025
Biomimetic Catalysis, Catalysis Research Center, TUM School of Natural Sciences, Technical University of Munich, Lichtenbergstrasse 4, 85748 Garching, Germany.
Inspired by natural cryptic halogenation in -bond formation, this study developed a synthetic approach combining biocatalytic bromination with transition-metal-catalyzed cross-coupling. Using the cyanobacterial VHPO, a robust and sustainable bromination-arylation cascade was created. Genetic modifications allowed enzyme immobilization, enhancing the compatibility between biocatalysis and chemocatalysis.
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