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Membrane cell-penetrating peptides

Already in 1965, Ryser and Hancock provided evidence that histones and polyamino acids could greatly enhance albumin uptake by cultured tumor cells (6). More recently, several polybasic peptides (so-called protein transduction domains, PTDs or cell-penetrating peptides, CPPs) have been shown to efficiently mediate uptake of nucleic acids, bioactive peptides, phage particles, and liposomes into a wide variety of mammalian cells. The initially proposed ability of CPPs to penetrate plasma membranes via a temperature-independent, non-endocytotic pathway was later shown to be a fixation artifact, and it is currently widely accepted that CPP-mediated macromolecular delivery follows energy-dependent endocytotic pathways that in most cases depend on the expression of cell-surface heparan sulfate proteoglycans (HSPGs) (7). [Pg.5]

Micelles of various kinds have proven to be useful as mimetics for investigating the high-resolution structure of bound peptides. These include studies of several cell-penetrating peptides (14,15) as well as membrane-disrupting peptides including antimicrobial peptides (16). [Pg.133]

Magzoub, M., L.E.G. Eriksson, and A. Graslund (2003) Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles. Biophys. Chem. 103, 271-288. [Pg.137]

Thoren, P, D. Persson, E. Esbjomer, M. Goksor, B. Lincoln, and B. Norden (2004) Membrane binding and translocation of cell-penetrating peptides. Biochemistry 43, 3471-3489. [Pg.137]

Cell-penetrating peptides (CPPs) can internalize into cells without disturbing the membrane potential and, therefore, are an attractive research target for drug delivery. These peptides are also short, cationic, and usually amphiphilic, and are able to bring a functional cargo into the cell [24, 31-33], There is no mechanism unanimously agreed upon,... [Pg.465]

Afonin, S., Frey, A., Bayerl, S., et al. (2006) The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes. Chemphyschem, 7, 2134—2142. [Pg.492]

Foged C, Nielsen HM. Cell penetrating peptides for drag delivery across membrane barriers. Expert Opin Drag Deliv 2008 5(1) 105-117. [Pg.292]

The control of inverse transition temperatures by sequence manipulation and biocompatibility of ELPs make them useful polymers for drug delivery. Cultured cancer cells and solid tumors in animal models uptake fluorescently labeled ELPs in a thermally responsive manner (48,49). Two major limitations in cancer therapy have been the inability of therapeutic molecules to cross the cell membrane and the target-specificity of the compounds. To overcome these limitations cell-penetrating, peptides (CPP) have been fused with ELPs (CPP-ELP) to develop thermally responsive therapeutics with the ability to translocate the cell membrane (Figure 3B). CPPs can assist in the transportation of hydrophilic compounds (small molecules, oglionucleotides and peptides) across the cell membrane (50). Fusing ELPs to a variety of CPPs have revealed that the peptide sequence of penetratin demonstrates the most efficient cellular uptake (51). Further, these CPP-ELPs have been fused to a c-Myc inhibitory peptide known to target and inhibit cancer. As proof of principle, these fusion proteins inhibits proliferation of cultured cancer cell lines in a thermally responsive manner (52). [Pg.46]

Cell-penetrating peptides (CPPs), Trojan horse peptides, protein transduction domains, peptides of different stmctural classes that are capable to cross the plasma membranes of mammalian cells in an... [Pg.67]

Free Energy of Cell-Penetrating Peptide through Lipid Bilayer Membrane Coarse-Grained Model Simulation... [Pg.503]


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