کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1355810 | 981065 | 2012 | 7 صفحه PDF | دانلود رایگان |

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 IC50 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.
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 IC50 value of 0.8 nM. And 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.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry - Volume 20, Issue 15, 1 August 2012, Pages 4774–4780