Abstract:
:4-Hydroxyderricin is a heat labile bioactive chalcone isolated from the plant Angelica keiskei. It received attention due to its antibiotic potency against several strains of bacteria including pathogens such as Staphylococcus aureus. Despite these promising pharmacological properties, the exact mode of action or the biological targets are still unknown. Here we report the synthesis and the application of a 4-hydroxyderricin probe for activity-based protein profiling (ABPP) in S. aureus. Due to the heat sensitivity of the natural product we utilize a chemical tool for the mild and selective enrichment of labile probe-protein conjugates and report seryl-tRNA synthetase (STS) to be covalently modified by our probe. This modification results in inhibition of the amino acylation of tRNAs catalyzed by S. aureus STS which is an essential enzymatic pathway for bacterial viability.
journal_name
Mol Biosystjournal_title
Molecular bioSystemsauthors
Battenberg OA,Yang Y,Verhelst SH,Sieber SAdoi
10.1039/c2mb25446hsubject
Has Abstractpub_date
2013-03-01 00:00:00pages
343-51issue
3eissn
1742-206Xissn
1742-2051journal_volume
9pub_type
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