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Glidobactin A is a natural product belonging to the syrbactin class of proteasome inhibitors, originally isolated from the bacterium *Polyangium brachysporum*. It is a macrocyclic peptide-like molecule that acts as a potent and irreversible inhibitor of the eukaryotic 20S proteasome. Specifically, it targets the chymotrypsin-like activity of the proteasome by covalently binding to the catalytic N-terminal threonine residues. Preclinical research has demonstrated that glidobactin A induces apoptosis and autophagy in various cancer models, including neuroblastoma, multiple myeloma, and ovarian cancer. Its structural scaffold serves as a platform for the development of novel proteasome inhibitors with potential therapeutic applications in oncology.
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