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Biophysical Studies of Cell-Penetrating Peptides 243 30. Santini, C.-L. et al., Translocation of jellyfish green fluorescent protein via the tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock, J. Biol. Chem., 276, 8159, 2001. 31. Rigler, R., Fluorescence correlations, single molecule detection and large number screening. Applications in biotechnology, J. Biotechnol., 41, 177, 1995. 32. Circular Dichroism and the Conformational Analysis of Biomolecules, Fasman, G.D., Ed., Plenum Press, New York, 1996. 33. Yang, L. et al., Barrel-stave model or toroidal model? A case study on melittin pores, Biophys. J., 81, 1475, 2001. 34. Tamm, L.K. and Tatulian, S.A., Infrared spectroscopy of proteins and peptides in lipid bilayers, Q. Rev. Biophys., 30, 365, 1997. 35. Wüthrich, K., The second decade — into the third millenium, Nat. Struct. Biol. NMR, Suppl. 5, 492, 1998. 36. Ferentz, A.E. and Wagner, G., NMR spectroscopy: a multifaceted approach to macromolecular structure, Q. Rev. Biophys., 33, 29, 2000. 37. Pervushin, K., Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology, Q. Rev. Biophys., 33, 161, 2000. 38. Biological Magnetic Resonance, Vol. 14, Spin Labeling, The Next Mellennium, Berliner, L.J., Ed., Plenum Press, New York, 1998. 39. Lindberg, M. and Gräslund, A., The position of the cell-penetrating peptide penetratin in SDS micelles determined by NMR, FEBS Lett., 497, 39, 2001. 40. Öhman, A. et al., NMR study of the conformation and localization of porcine galanin in SDS micelles. Comparison with an inactive analog and a galanin receptor antagonist, Biochemistry, 37, 9169, 1998. 41. Damberg, P., Jarvet, J., and Gräslund, A., Micellar systems as solvents in peptide and protein structure determination, Meth. Enzymol., 339, 271, 2001. 42. Lindberg, M. et al., Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR, Biochemistry, 40, 3141, 2001. 43. Drin, G. et al., Translocation of the pAntp peptide and its amphipathic analogue AP- 2AL, Biochemistry, 40, 1824, 2001. 44. Magzoub, M. et al., Interaction and structure induction of cell-penetrating peptides in the presence of phosholipid vesicles, Biochim. Biophys. Acta, 1572, 77, 2001. 45. Magzoub, M., Eriksson, L.E.G., and Gräslund, A., Conformational states of the cellpenetrating peptide penetratin when interacting with phospholipid vesicles. Effects of surface charge and peptide concentration, Biochim. Biophys. Acta, in <strong>press</strong>. 46. Vivès, E., Brodin, P., and Lebleu, B., A truncated HIV-1 tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus, J. Biol. Chem., 272, 16010, 1997. 47. Matsuzaki, K., Magainins as paradigm for the mode of action of pore forming polypeptides, Biochim. Biophys. Acta, 1376, 391, 1998. 48. Matzuzaki, K., Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes, Biochim. Biophys. Acta, 1462, 1, 1999. 49. Shai, Y., Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell nonselective membrane-lytic peptides, Biochim. Biophys. Acta, 1462, 44, 1999. 50. Shai, Y. and Oren, Z., From “carpet” mechanism to de novo designed diastereomeric cell-selective antimicrobial peptides, Peptides, 22, 1629, 2001. 51. Tossi, A., Sandri, L., and Giangaspero, A., Amphipathic, α-helical antimicrobial peptides, Biopolymers, 55, 4, 2000.
244 Cell-Penetrating Peptides: Processes and Applications 52. Huang, H.W., Action of antimicrobial peptides: two-state model, Biochemistry, 39, 8347, 2000. 53. Yang, L. et al., Crystallization of antimicrobial pores in membranes: magainin and protegrin, Biophys. J., 79, 2002, 2000. 54. Kobayashi, S. et al., Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor, Biochemistry, 39, 8648, 2000. 55. Park, C.B., Kim, H.S., and Kim, S.C., Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions, Biochem. Biophys. Res. Commun., 244, 253, 1998. 56. Thorén, P.E.G. et al., The Antennapedia peptide penetratin translocates across lipid bilayers — the first direct observation, FEBS Lett., 482, 265, 2000. 57. Drin, G. et al., Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity, Eur. J. Biochem., 268, 1304, 2001. 58. Persson, D., Thorén, P.E.G., and Nordén, B., Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles, FEBS Lett., 505, 307, 2001. 59. Futaki, S. et al., Arginine-rich peptides, J. Biol. Chem., 276, 5836, 2001. 60. Ludtke, S., He, K., and Huang, H., Membrane thinning caused by magainin 2, Biochemistry, 34, 16764, 1995.
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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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1 CONTENTS 0-8493-1141-1/02/$0.00+$
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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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Structure Prediction of CPPs and It
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Kinetics of Uptake of Cell-Penetrat
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Cell-Penetrating Peptide Conjugatio
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FIGURE 15.9 (Color Figure 15.9 foll
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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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