Abstract
The linear depsipeptide grassystatin A, a valuable probe for the study of cathepsin E function, has been synthesized by a [4+6] strategy. It exhibited specific inhibitory activity against cathepsin E with an IC(50) value of 0.8 nM. Our studies indicated that inhibition of cathepsin E did not have an impact on ovalbumin antigen processing and peptide presentation, unique from studies of other aspartic protease inhibitors.
Copyright © 2012 Elsevier Ltd. All rights reserved.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cathepsin E / antagonists & inhibitors*
-
Cathepsin E / metabolism
-
Dose-Response Relationship, Drug
-
Female
-
Male
-
Mice
-
Mice, Transgenic
-
Molecular Structure
-
Peptides / chemical synthesis
-
Peptides / chemistry
-
Peptides / pharmacology*
-
Protease Inhibitors / chemical synthesis
-
Protease Inhibitors / chemistry
-
Protease Inhibitors / pharmacology*
-
Structure-Activity Relationship
Substances
-
Peptides
-
Protease Inhibitors
-
grassystatin A
-
Cathepsin E