Modulation of Cellular Function by TAT Mediated Transduction of Full Length Proteins

Authors: Wadia J.S.; Dowdy S.F.

Source: Current Protein and Peptide Science, Volume 4, Number 2, April 2003 , pp. 97-104(8)

Publisher: Bentham Science Publishers

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Abstract:

Due to the barrier imposed by the cell membrane, delivery of macromolecules in excess of 500 Daltons directly into cells remains problematic. However, proteins, which have been evolutionarily selected to perform specific functions, are therefore an attractive therapeutic agent to treat a variety of human diseases. In practice, the direct intracellular delivery of these proteins has, until recently, been difficult to achieve due primarily to the bioavailability barrier of the plasma membrane, which effectively prevents the uptake of the majority of peptides and prote ins by limiting their passive entry. However, recent wor k using small c ationic pe ptide s, termed protein transduction domains (PTDs), derived from nucleic acid binding proteins, such as HIV TAT protein or the Dros. m. transcription factor Antp. or synthetic poly-Arginine, have now been shown to deliver a myriad of molecules, including synthetic small molecules, peptides and proteins, into animal models in vivo. Here, we focus on the delivery of biologically active, full length proteins to treat pre-clinical disease models.

Keywords: Modulation; macromolecules; poly-Arginine; protein transduction domains (PTDs); peptides

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/1389203033487289

Publication date: 2003-04-01