The taming of the cell penetrating domain ofthe HIV Tat: Myths and realities

被引:137
作者
Chauhan, Ashok
Tikoo, Akshay
Kapur, Arvinder K.
Singh, Mahavir
机构
[1] Johns Hopkins Univ, Dept Neurol, Richard Johnson Div Neuroimmunol & Neurol Infect, Baltimore, MD 21287 USA
[2] Dept Biotechnol, Jaipur, Rajasthan, India
[3] Univ Wisconsin, Dept Pediat, Madison, WI USA
[4] Univ Louisville, Dept Physiol & Biophys, Sch Med, Louisville, KY 40202 USA
[5] Potentia Pharmaceut Inc, Biotechnol & Cell Biol, Louisville, KY 40202 USA
关键词
protein transduction domain (PTD); nuclear export signal (NES) analysis; nuclear/nucleolar HIV Tat; cytoplasmic protein delivery; Lysosomotropic agent; transcellular-PTD;
D O I
10.1016/j.jconrel.2006.10.031
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Protein transduction with cell penetrating peptides over the past several years has been shown to be an effective way of delivering proteins in vitro and now several reports have also shown valuable in vivo applications in correcting disease states. An impressive bioinspired phenomenon of crossing biological barriers came from HIV transactivator Tat protein. Specifically, the protein transduction domain of HIV Tat has been shown to be a potent pleiotropic peptide in protein delivery. Various approaches such as molecular modeling, arginine guarridinium head group structural strategy, multimerization of PTD sequence and phage display system have been applied for taming of the PTD. This has resulted in identification of PTD variants which are efficient in cell membrane penetration and cytoplasmic delivery. In spite of these state of the art technologies, the dilemma of low protein transduction efficiency and target specific delivery of PTD fusion proteins remains unsolved. Moreover, some misconceptions about PTD of Tat in the literature require considerations. We have assembled critical information on secretory, plasma membrane penetration and transcellular properties of Tat and PTD using molecular analysis and available experimental evidences. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:148 / 162
页数:15
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