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Biophysical Studies of Cell-Penetrating Peptides 241 complicated and unlikely as a pore model. Whether any of the CPPs are able to promote a transverse diffusion (flip-flop) of some phospholipids remains to be studied. There is today no simple correlation between any degree of secondary structure induced in various model systems and the permeability efficiency of CPPs in cellular systems. Translocation of a charged CPP and a cargo across an intact membrane is energetically very unfavorable, even in the presence of proper transmembrane potential. The CPP effect will depend on biophysical phenomena, not easily accounted for by structures, or molecular simulations in a short time window (~nsec). The function of the CPP tag could perhaps be as a magic agent to destabilize the membrane locally. Electrostatic perturbations within the membrane, primarily in the outer leaflet, may cause lateral rearrangement of acidic lipids. Besides membrane surface potential, interfacial dipole potential could be influenced. A discreteness-ofcharge phenomenon may also be created, as suggested for studies on hepta-lysine. 28 A thinning of the membrane like the one reported with magainin, 60 combined with a reduction of local surface tension, may allow CPPs to intercalate the membrane. An intimate and flexible sealing between peptide side groups and lipid head groups will reduce leakage until the CPP slips snugly through and pulls the concomitant cargo inside. After this transient permeation the membrane must rapidly recover and heal. The detailed structural and thermodynamic description of such a hypothetic process remains to be worked out. From the biophysical point of view, to elucidate the mechanisms involved in CPP translocation and transport is still a challenge. ACKNOWLEDGMENT Work on this project in the authors’ laboratory is supported by the Swedish Science Council. REFERENCES 1. Derossi, D., Chassaing, G., and Prochiantz, A., Trojan peptides: the penetratin system for intracellular delivery, Trends Cell Biol., 8, 84, 1998. 2. Lindgren, M. et al., Cell-penetrating peptides, Trends Pharm. Sci., 21, 99, 2000. 3. Schwarze, S.R., Hruska, K.A., and Dowdy, S.F., Protein transduction: unrestricted delivery into all cells? Trends Cell Biol., 10, 290, 2000. 4. Derossi, D. et al., The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem., 269, 10444, 1994. 5. Derossi, D. et al., Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent, J. Biol. Chem., 271, 18188, 1996. 6. Berlose, J.-P. et al., Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments, Eur. J. Biochem., 242, 372, 1996. 7. Kilk, K. et al., Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the Islet-1 homeodomain. Comparison with the penetratin peptide, Bioconjugate Chem., 12, 911, 2001. 8. Pooga, M. et al., Cell penetration by transportan, FASEB J., 12, 67, 1998.
242 Cell-Penetrating Peptides: Processes and Applications 9. Green, M. and Loewenstein, P.M., Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein, Cell, 55, 1179, 1988. 10. Frankel, A.D. and Pabo, C.O., Cellular uptake of the tat protein from human immunodeficiency virus, Cell, 55, 1189, 1998. 11. Lin, Y.-Z., Yao, S., and Hawiger, J., Role of the nuclear localization sequence in fibroblast growth factor-1-stimulated mitogenic pathways, J. Biol. Chem., 271, 5305, 1996. 12. Chaloin, L. et al., Conformations of primary amphipathic carrier peptides in membrane mimicking environments, Biochemistry, 36, 11179, 1997. 13. Vidal, P. et al., Interactions of primary amphipathic vector peptides with membranes. Conformational consequences and influence on cellular localization, J. Membr. Biol., 162, 259, 1998. 14. Prochiantz, A., Getting hydrophilic compounds into cells: lessons from homeopeptides, Curr. Opin. Neurobiol., 6, 629, 1996. 15. Soomets, U. et al., Deletion analogues of transportan, Biochim. Biophys. Acta, 1467, 165, 2000. 16. Handbook of Nonmedical Applications of Liposomes, Volume IV: From Gene Delivery and Diagnostics to Ecology, Lasic, D.D. and Yechezkel, B., Eds., CRC Press, Boca Raton, FL, 1996. 17. Jin, A.J. et al., Light scattering characterization of extruded lipid vesicles, Eur. Biophys. J., 28, 187, 1999. 18. Fischer, A., Oberholzer, T., and Luisi, P.L., Giant vesicles as models to study the interactions between membranes and proteins, Biochim. Biophys. Acta, 1467, 177, 2000. 19. Sanders, C.R. and Schwonek, J.P., Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoyl-phosphatidylcholine by solid-state NMR, Biochemistry, 31, 8898, 1992. 20. Prosser, R.S., Hwang, J.S., and Vold, R.R., Magnetically aligned phospholipid bilayers with positive ordering: a new model membrane system, Biophys. J., 74, 2405, 1998. 21. Sternin, E., Nizza, D., and Gawrisch, K., Temperature dependence of DMPC/DHPC mixing in a bicellar solution and its structural implications, Langmuir, 17, 2610, 2001. 22. Glover, K.J. et al., Structural evaluation of phospholipid bicelles for solution-state studies of membrane-associated biomolecules, Biophys. J., 81, 2163-2001. 23. Struppe, J., Whiles, J.A., and Vold, R.R., Acidic phospholipid bicelles: a versatile model membrane system, Biophys. J., 78, 281, 2000. 24. Vold, R.R., Prosser, R.S., and Deese, A.J., Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides, J. Biomol. NMR, 9, 329, 1997. 25. Kuprin, S. et al., Nonideality of water-hexafluoropropanol mixtures as studied by X-ray small angle scattering, Biochem. Biophys. Res. Commun., 217, 1151, 1995. 26. Grahame, D.C., The electrical double layer and the theory of electrocapillarity, Chem. Rev., 41, 441, 1947. 27. Peitzsch, R.M. et al., Calculations of the electrostatic potential adjacent to model phospholipid bilayers, Biophys. J., 68, 729, 1995. 28. Murray, D. et al., Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experiment, Biophys. J., 77, 3176, 1999. 29. Lakowicz, J.R., Principles of Fluorescence Spectroscopy, 2nd ed., Kluwer Academic/Plenum Publishers, New York, 1999.
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CELL- PENETRATING PEPTIDES Processe
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Pharmacology and Toxicology: Basic
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Library of Congress Cataloging-in-P
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to the handbook are prominent resea
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REFERENCES 1. Green, M. and Loewens
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Contributors Mats Andersson Microbi
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Erin T. Pelkey Department of Chemis
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Contents Section I Classes of Cell-
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Chapter 16 Cell-Penetrating Peptide
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The Tat-Derived Cell-Penetrating Pe
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24 Cell-Penetrating Peptides: Proce
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3 Transportans Margus Pooga, Mattia
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Transportans 55 Indeed, galparan is
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Transportans 57 especially the endo
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Transportans 59 In the penetration
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Transportans 61 A 21-mer antisense
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Transportans 63 Commonly, the prote
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Transportans 65 antibiotin antibodi
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Transportans 67 For cross-linking o
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Transportans 69 and still retain ef
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Model Amphipathic Peptides 73 its D
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Model Amphipathic Peptides 75 pmol/
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TABLE 4.1 Internalization of Peptid
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TABLE 4.2 Internalization of Peptid
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Model Amphipathic Peptides 81 relat
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Model Amphipathic Peptides 87 A cat
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Model Amphipathic Peptides 89 At th
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Model Amphipathic Peptides 91 16. H
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Signal Sequence-Based Cell-Penetrat
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116 Cell-Penetrating Peptides: Proc
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Interactions of Cell-Penetrating Pe
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Structure Prediction of CPPs and It
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Kinetics of Uptake of Cell-Penetrat
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Kinetics of Uptake of Cell-Penetrat
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptides as Vector
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TABLE 16.1 Examples of Transport of
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CPP 2 Cargo or mRNA CAP Antisense A
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Microbial Membrane-Permeating Pepti
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Index A Abaecin, 129 Abz radiolabel
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Index 399 Diffraction, 168 Disulphi
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Index 401 structure prediction, 187
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Index 403 pRB proteins, Tat-E1A bin
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Index 405 lipid perturbation (secon
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