The ubiquitous calpains, μ- and m-calpain, are implicated in a variety of vital (patho)physiological processes and therefore cell-permeable specific inhibitors represent important tools for defining the role of calpains in cells and animal models. A synthetic N-acetylated 27-mer peptide derived from exon B of the human calpastatin inhibitory domain 1 is known to be the most potent and selective reversible inhibitor of calpains. To improve the membrane permeability of this peptidic inhibitor, it was N-terminally extended with or disulfide-linked to the C-terminal 7-mer fragment of penetratin, a well-established vector for cell membrane translocation of bioactive compounds. Despite the shorter penetratin sequence, both constructs showed increased cell permeability and retained their full calpain inhibitory potency. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
A new cell-permeable calpain inhibitor / Fiorino, Ferdinando; Shirley Gil, Parrado; Irmgard Assfalg, Machleidt; Werner, Machleidt; Luis, M. o. r. o. d. e. r.. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - ELETTRONICO. - 13:1(2007), pp. 70-73. [10.1002/psc.790]
A new cell-permeable calpain inhibitor.
FIORINO, FERDINANDO;
2007
Abstract
The ubiquitous calpains, μ- and m-calpain, are implicated in a variety of vital (patho)physiological processes and therefore cell-permeable specific inhibitors represent important tools for defining the role of calpains in cells and animal models. A synthetic N-acetylated 27-mer peptide derived from exon B of the human calpastatin inhibitory domain 1 is known to be the most potent and selective reversible inhibitor of calpains. To improve the membrane permeability of this peptidic inhibitor, it was N-terminally extended with or disulfide-linked to the C-terminal 7-mer fragment of penetratin, a well-established vector for cell membrane translocation of bioactive compounds. Despite the shorter penetratin sequence, both constructs showed increased cell permeability and retained their full calpain inhibitory potency. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.