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Synthesis of a new cell penetrating calpain inhibitor (calpeptin).

Abstract：

:N-terminal of Leu-norleucinal or Leu-methioninal was modified to obtain a cell penetrative peptide inhibitor against calpain. Benzyloxycarbonyl (Z) derivatives had less active against papain than phenylbutyryl derivatives and leupeptin. Z-Leu-nLeu-H (calpeptin) was more sensitive to calpain I than Z-Leu-Met-H and leupeptin. Calpeptin was most potent among synthesized inhibitors in terms of preventing the Ca2+-ionophore induced degradation of actin binding protein and P235 in intact platelets. After 30 min incubation with intact platelets, calpeptin completely abolished calpain activity in platelets but no effect was observed in case of leupeptin. Calpeptin also inhibited 20K phosphorylation in platelets stimulated by thrombin, ionomycin or collagen. Thus calpeptin was found to be a useful cell-penetrative calpain inhibitor.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tsujinaka T,Kajiwara Y,Kambayashi J,Sakon M,Higuchi N,Tanaka T,Mori T

doi

10.1016/s0006-291x(88)81355-x

subject

Has Abstract

pub_date

1988-06-30 00:00:00

pages

1201-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)81355-X

journal_volume

153

pub_type

杂志文章

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