Front Cover: Activation, Structure, Biosynthesis and Bioactivity of Glidobactin‐like Proteasome Inhibitors from Photorhabdus laumondii (ChemBioChem 9/2021)

Glidobactin‐like proteasome inhibitors are regarded as promising candidates for anticancer drug development. We report the largest subset of glidobactin‐like proteasome inhibitors, which were produced and identified after the silent biosynthetic gene cluster plu1881–1877 had been activated in the na...

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Published inChembiochem : a European journal of chemical biology Vol. 22; no. 9; p. 1494
Main Authors Zhao, Lei, Le Chapelain, Camille, Brachmann, Alexander O., Kaiser, Marcel, Groll, Michael, Bode, Helge B.
Format Journal Article
LanguageEnglish
Published 04.05.2021
Subjects
biosynthesis
drug design
glidobactins
proteasome inhibitors
structure–activity relationships
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Summary:Glidobactin‐like proteasome inhibitors are regarded as promising candidates for anticancer drug development. We report the largest subset of glidobactin‐like proteasome inhibitors, which were produced and identified after the silent biosynthetic gene cluster plu1881–1877 had been activated in the native host Photorhabdus laumondii. Crystal‐structure analysis of the new glidobactin derivatives in complex with yeast proteasome core particle (yCP) suggests that the inhibition occurs primarily by covalent and irreversible binding of the inhibitors to the β5 subunit of the yCP. More information can be found in the full paper by H. B. Bode et al.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.202100174