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Omuralide and Vibralactone: Differences in the Proteasome‐ β‐Lactone‐γ‐Lactam Binding Scaffold Alter Target Preferences
Author(s) -
List Anja,
Zeiler Evelyn,
Gallastegui Nerea,
Rusch Marion,
Hedberg Christian,
Sieber Stephan A.,
Groll Michael
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201308567
Subject(s) - proteasome , protease , chemistry , scaffold , biochemistry , hela , ubiquitin , lactam , enzyme , stereochemistry , gene , computer science , cell , database
Despite their structural similarity, the natural products omuralide and vibralactone have different biological targets. While omuralide blocks the chymotryptic activity of the proteasome with an IC 50 value of 47 nM, vibralactone does not have any effect at this protease up to a concentration of 1 m M . Activity‐based protein profiling in HeLa cells revealed that the major targets of vibralactone are APT1 and APT2.