Cationic cell-penetrating peptides

Duchardt, F., Fotin-Mleczek, M., Schwarz, H., Fischer, R., Brock, R. A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 2007, 8, 848-66. 

Drin, G., et al. 2003. Studies on the internalisation mechanism of cationic cell-penetrating peptides. J Biol Chem 278 31192. 

VP22 Tat FGFs Penetratin Cationic Cell-Penetrating Peptides ... 

Drin, G., Cottin, S., Blanc, E., Rees, A.R. and Temsamani, J. (2003) Smdies on the internalization mechanism of cationic cell-penetrating peptides. Journal of Biological Chemistry, 278(33), 31192-201. 

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,... 

In a conceptual paper, Matile et al. described that CT-DNA can be activated by amphiphilic cations such as guanidiniocalixarenes 7 to act as a cation transporter in bulk and Upid bilayer membranes and showed that this unusual activity of DNA can be of interest for the development of biosensors (Fig. 24.32). In light of the chargebalancing effect of cell-penetrating peptides as anion transporters across lipid membranes, this discovery demonstrates that the multifunctionality of polyion-counterion complexes is general and occurs with low-basicity polyanions exactly as with low-acidity polycations [100]. 

Kwon et al. used NMR to investigate domain formation in membranes (phosphatidylethanolamine (POPE) and anionic l-palmitoyl-2-oleoyl-s -gZycero-3-phosphatidylglycerol (POPG)) with to cationic peptides. The antimicrobial peptides were (AMP(3)) of the beta-hairpin family of protegrin-1 (PG-1), and two cell-penetrating peptides (CPPs), HIV TAT and penetratin. The NMR showed the extent of the interaction between the bilayers and the peptides. 

Cell-penetrating peptides (CPPs) are a class of short, often cationic peptides that have the capability to translocate across cellular membranes, and although the translocation most likely involves several pathways, they interact directly with membranes, as well as with model bilayers. A review focuses on solution NMR as a tool for investigating CPP-lipid interactions. Structural propensities and cell-penetrating capabilities can be derived from a combination of CPP solution structures and studies of the effect that the peptides have on bilayers and the localization in a bilayer. 

For DNA and RNA delivery to the central nervous system (CNS), numerous nonviral nanosystems can be employed [10], These include cationic and stealth liposomes, cationic polymers, dendrimers, cyclodextrin, and cell-penetrating peptides (CPPs). In general terms, all these synthetic vectors lack of a cytotropism, i.e., they do not specifically target a single type/subtype of cell, and display different degrees of cytotoxicity. 

In this context, it is worthy to note that the already mentioned Baa behaves as a new cell-penetrating unit, because its presence permits the deliveiy into cells of both cationic and anionic peptides, which are not able to cross the membrane by themselves, further increasing the potentiality of fullerene derivatives (Yang et al., 2007a). 

Terrone, D., S. Leung, W. Sang, L. Roudaia, and J. Silvius (2003) Penetratin and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential. Biochemistry 42, 13787-13799. 

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