Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain

Hai Yan Wu, Kazuhito Tomizawa, Masayuki Matsushita, Yun Fei Lu, Sheng Tian Li, Hideki Matsui

Research output: Contribution to journalArticle

31 Citations (Scopus)


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 languageEnglish
Pages (from-to)131-135
Number of pages5
JournalNeuroscience Research
Issue number1
Publication statusPublished - Sep 1 2003



  • Apoptosis
  • Calpain
  • Calpastatin
  • Neuronal cell death
  • Poly-arginine peptides
  • Tat

ASJC Scopus subject areas

  • Neuroscience(all)

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