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Interactions of Cell-Penetrating Peptides with Membranes 175 FIGURE 8.5 Variation of the transition surface <strong>press</strong>ure as a function of the lipid molar fraction (x P). The data are provided from Figure 8.1. The dashed vertical bar shows the limits of the phase transitions. (Adapted from Van Mau, N. et al., J. Membr. Biol., 167, 241, 1999. With permission.) The phase separation deduced by analysis of the com<strong>press</strong>ion isotherms was confirmed by direct observations using AFM imaging on transferred monolayers. Figure 8.6 reveals strong changes on lipid-embedded particles when the peptide molar ratio is varied. The clear domains (Figure 8.6C) confirm the existence of peptide-induced phase separation; evolution of the shape of the particle is in accordance with a conformational change of the peptide with formation of mixed particles compatible with the FTIR observations. 8.2.2.8.2 Influence of the Sequence Cell positioning: membrane associated or nuclear — Within the SP–NLS peptides (Table 8.1) and FP–NLS (Table 8.2), several variants have been synthesized. While single K to S mutations in the NLS sequences do not modify the final nuclear localization, removal of the W-S-Q-P linker can strongly modify the final cellular localization. For the SP–NLS peptides, the presence of this linker has no influence on final localization, 47 however, its absence in the FP-NLS series leads to a peptide that has a membrane-associated localization. 48 The origin of these different behaviors according to the nature of the hydrophobic sequence is still not clear and no rational explanation has been provided up till now, although some preliminary data suggest that the peptide–peptide interactions involving the N-terminal hydrophobic domain could play an important role. Comparison between FP- and SP-NLS: a possible role of the conformation — A comparative study of peptides of the two series made on model membrane systems also provided some unexpected information. Using vesicles made of pure phospholipids
176 Cell-Penetrating Peptides: Processes and Applications FIGURE 8.6 2 × 2 µm AFM scans of transferred peptide 1 -containing DOPC monolayers. x P = 0, 0.01, 0.05, 0.1, and 0.25 for A, B, C, D, and E, respectively. (Adapted from Van Mau, N. et al., J. Membr. Biol., 167, 241, 1999. With permission.) (DOPC or DOPG), fluorescence measurements based on the Trp residues revealed that the SP–NLS peptide penetrates indifferently into neutral and negatively charged lipidic media, 47 while the FP–NLS peptide penetrates only in the negatively charged lipids. The same conclusion was obtained on the basis of monolayer experiments
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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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Biophysical Studies of Cell-Penetra
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Toxicity and Side Effects of Cell-P
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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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