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  • Title: Arginine carrier peptide bearing Ni(II) chelator to promote cellular uptake of histidine-tagged proteins.
    Author: Futaki S, Niwa M, Nakase I, Tadokoro A, Zhang Y, Nagaoka M, Wakako N, Sugiura Y.
    Journal: Bioconjug Chem; 2004; 15(3):475-81. PubMed ID: 15149174.
    Abstract:
    Arginine-rich peptide-mediated protein delivery into living cells is a novel technology for controlling cell functions with therapeutic potential. In this report, a novel approach for the intracellular delivery of histidine-tagged proteins was introduced where a Ni(II) chelate of octaarginine peptide bearing nitrilotriacetic acid [R8-NTA-Ni(II)] was used as a membrane-permeable carrier molecule. Significant internalization of histidine-tagged enhanced green fluorescent protein (EGFP) into HeLa cells was observed by confocal microscopic observation in the presence of R8-NTA-Ni(II). Nuclear condensation characteristic in apoptotic cell death was also induced in the cells treated with a histidine-tagged apoptosis-inducing peptide [pro-apoptotic domain peptide (PAD)], indicating that the cargo molecules really went through the membrane to reach the cytosol. The apoptosis-inducing activity of the peptide thus delivered was compared with that of the PAD peptide covalently connected with the octaarginine peptide.
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