RRC ID 1398
Author Futaki S, Niwa M, Nakase I, Tadokoro A, Zhang Y, Nagaoka M, Wakako N, Sugiura Y.
Title Arginine carrier peptide bearing Ni(II) chelator to promote cellular uptake of histidine-tagged proteins.
Journal Bioconjug. Chem.
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.
Volume 15(3)
Pages 475-81
Published 2004-5
DOI 10.1021/bc034181g
PMID 15149174
MeSH Apoptosis / drug effects Arginine / chemistry* Cell Survival / drug effects Drug Carriers / chemical synthesis Drug Carriers / chemistry Drug Carriers / pharmacokinetics* Drug Design Green Fluorescent Proteins / chemistry Green Fluorescent Proteins / genetics Green Fluorescent Proteins / metabolism HeLa Cells Histidine / chemistry* Humans Nickel / chemistry* Nitrilotriacetic Acid / chemical synthesis Nitrilotriacetic Acid / chemistry Nitrilotriacetic Acid / pharmacokinetics Oligopeptides / chemistry* Peptides / chemical synthesis Peptides / chemistry Peptides / pharmacokinetics*
IF 4.349
Times Cited 46
Human and Animal Cells HeLa