Arginine Carrier Peptide Bearing Ni(II) Chelator to Promote Cellular Uptake of Histidine-Tagged Proteins

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• 作者：Shiroh Futaki ; Miki Niwa ; Ikuhiko Nakase ; Akiko Tadokoro ; Youjun Zhang ; Makoto Nagaoka ; Naoya Wakako ; and Yukio Sugiura
• 刊名：Bioconjugate Chemistry
• 出版年：2004
• 出版时间：May 2004
• 年：2004
• 卷：15
• 期：3
• 页码：475 - 481
• 全文大小：270K
• 年卷期：v.15,no.3(May 2004)
• ISSN：1520-4812

文摘

Arginine-rich peptide-mediated protein delivery into living cells is a novel technology for controllingcell functions with therapeutic potential. In this report, a novel approach for the intracellular deliveryof histidine-tagged proteins was introduced where a Ni(II) chelate of octaarginine peptide bearingnitrilotriacetic acid [R8-NTA-Ni(II)] was used as a membrane-permeable carrier molecule. Significantinternalization of histidine-tagged enhanced green fluorescent protein (EGFP) into HeLa cells wasobserved by confocal microscopic observation in the presence of R8-NTA-Ni(II). Nuclear condensationcharacteristic in apoptotic cell death was also induced in the cells treated with a histidine-taggedapoptosis-inducing peptide [pro-apoptotic domain peptide (PAD)], indicating that the cargo moleculesreally went through the membrane to reach the cytosol. The apoptosis-inducing activity of the peptidethus delivered was compared with that of the PAD peptide covalently connected with the octaargininepeptide.