Membrane-permeable arginine-rich peptides and the translocation mechanisms

被引:359
作者
Futaki, S [1 ]
机构
[1] Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan
[2] JST, PRESTO, Kawaguchi, Saitama 3320012, Japan
关键词
HIV-1; tat; oligoarginine; penetratin; cell permeable peptide; protein transduction; drug delivery;
D O I
10.1016/j.addr.2004.10.009
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The intracellular delivery of proteins and other bioactive molecules using membrane-permeable carrier peptide vectors opens the possibility of establishing novel methods of elucidating and controlling cell functions with therapeutic potentials. One of the most typical peptide vectors is a short, arginine-rich peptide segment derived from the human immunodeficiency virus (HIV)-1 Tat protein. We have shown that not only the Tat peptide, but also various arginine-rich oligopeptides possess very similar characteristics in translocation and abilities as a delivery vector. This review summarizes the structures of these peptide vectors, especially the Tat and other arginine-rich peptides, and the current understanding of their internalization mechanisms. (c) 2004 Elsevier B.V All rights reserved.
引用
收藏
页码:547 / 558
页数:12
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