HIV-1 TAT (48-60) is a cell-penetrating peptide derived from the human immunodeficient virus (HIV)-1 Tat protein residue 48-60. It has been used to deliver exogenous macromolecules into cells in a non-disruptive way.
Studies show that exogenous Tat protein is able to translocate through the plasma membrane and to reach the nucleus to transactivate the viral genome. The HIV-1 TAT (48-60) peptide, which contains the basic domain of the full length peptide only, retains the full translocation activity and even appears more efficient in terms of nuclear localization when compared with the other active peptides at the standard dose of 1 mM[1]. Cell-penetrating peptides are regarded as promising vectors for intracellular delivery of large, hydrophilic molecules. An apparently endocytotic uptake of HIV-1 TAT (48-60) is observed by confocal laser scanning microscopy[2]. HIV-1 TAT (48-60) induces the formation of rodlike, presumably inverted micelles in DMPC, which may represent intermediates during the translocation across eukaryotic membranes[3].
[1]. Vivès E, et al. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem. 1997 Jun 20;272(25):16010-7. [2]. Thorén PE, et al. Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells. Biochem Biophys Res Commun. 2003 Jul 18;307(1):100-7. [3]. Afonin S, et al. The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes. Chemphyschem. 2006 Oct 13;7(10):2134-42.