Total synthesis and absolute stereochemistry of the proteasome inhibitors cystargolides A and B.
@article{TelloAburto2015TotalSA, title={Total synthesis and absolute stereochemistry of the proteasome inhibitors cystargolides A and B.}, author={Rodolfo Tello-Aburto and Liam P. Hallada and Doleshwar Niroula and Snezna Rogelj}, journal={Organic \& biomolecular chemistry}, year={2015}, volume={13 40}, pages={ 10127-30 } }
The absolute stereochemistry of the cystargolides was determined by total synthesis. Evaluation of synthetic cystargolides and derivatives showed that the natural (2S,3R) stereochemistry is essential for activity. Moreover, benzyl esters (-)-10 and (-)-15 were found to be about 100 times more potent, and to selectively kill MCF-7 cancerous cells.
7 Citations
Design, synthesis, and evaluation of cystargolide-based beta-lactones as potent proteasome inhibitors.
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- 2018
The cystargolide derivative 5k, structurally unique at both Py and P1, exhibited the most promising inhibitory activity for the β5 subunit of human proteasomes and was identified as a promising candidate for continued therapeutic studies.
Design, synthesis, and evaluation of cystargolide-based β-lactones as potent proteasome inhibitors.
- Biology, ChemistryEuropean journal of medicinal chemistry
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Natural product scaffolds as inspiration for the design and synthesis of 20S human proteasome inhibitors
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The following review discusses the efforts made in the field to isolate and identify natural products as inhibitors of the proteasome and some of the modifications made to natural products in order to discover more potent and selective inhibitors for potential disease treatment.
Built to bind: biosynthetic strategies for the formation of small-molecule protease inhibitors.
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This review summarizes the current knowledge on the biosynthesis of important and/or structurally interesting inhibitors of proteases and related enzymes to allow targeted genome mining for the discovery of new derivatives.
Chemically synthesized LYRM03 could inhibit the metastasis of human breast cancer MDA-MB-231 cells in vitro and in vivo.
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Global analysis of biosynthetic gene clusters reveals conserved and unique natural products in entomopathogenic nematode-symbiotic bacteria
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Evaluation of the bioactivity of the natural products expressed by the most prevalent cluster families explains the functional basis of bacterial natural products involved in bacteria–nematode–insect interactions.
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