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
Current Protein & Peptide Science
Title: Modulation of Cellular Function by TAT Mediated Transduction of Full Length Proteins
Volume: 4 Issue: 2
Author(s): Jehangir S. Wadia and Steven F. Dowdy
Affiliation:
Keywords: Modulation, macromolecules, poly-Arginine, protein transduction domains (PTDs), peptides
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.
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Cite this article as:
Wadia S. Jehangir and Dowdy F. Steven, Modulation of Cellular Function by TAT Mediated Transduction of Full Length Proteins, Current Protein & Peptide Science 2003; 4 (2) . https://dx.doi.org/10.2174/1389203033487289
DOI https://dx.doi.org/10.2174/1389203033487289 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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