Abstract
Calpain, a Ca2+-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.
Original language | English |
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Pages (from-to) | 131-135 |
Number of pages | 5 |
Journal | Neuroscience Research |
Volume | 47 |
Issue number | 1 |
DOIs | |
Publication status | Published - Sep 1 2003 |
Externally published | Yes |
Keywords
- Apoptosis
- Calpain
- Calpastatin
- Neuronal cell death
- Poly-arginine peptides
- Tat
ASJC Scopus subject areas
- Neuroscience(all)