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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

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.[1]

References

  1. Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain. Wu, H.Y., Tomizawa, K., Matsushita, M., Lu, Y.F., Li, S.T., Matsui, H. Neurosci. Res. (2003) [Pubmed]
 
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