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Interactions of Cell-Penetrating Peptides with Membranes 171 FIGURE 8.1 Variations of the surface pressure with the mean molecular area of mixed DOPC- 1 monolayers at various peptide molar fractions (x P). (Adapted from Van Mau, N. et al., J. Membr. Biol., 167, 241, 1999. With permission.) of the membrane uptake of this peptide was undertaken using mainly monolayers AFM and FTIR. 57,58 8.2.2.8.1 Monolayer Study Because of its solubility properties, the peptide could be dissolved in the same volatile organic solvent mixture as the phospholipids (DOPC, DOPG, DPPC, and DPPG) and, hence, the peptide–lipid mixtures could be spread at the air–water interface. The various compression isotherms at various peptide molar fractions were recorded and are shown in Figures 8.1 and 8.2. Analysis of the isotherm was made by plotting the variation of the mean molecular area as a function of the molar fraction at a given surface pressure. In all cases the variations of the mean molecular area showed positive deviations from additivity (Figure 8.3 and insets of Figure 8.2). 109,110 Such behavior can be considered indicative of strong peptide–lipid interactions with expansion of the mean molecular area. However, the deviation from linearity is larger in DOPC and DOPG than in DPPC and DPPG, suggesting that the nature of the peptide–lipid interactions could strongly depend on the nature of the fatty acid. Further investigations, based now on FTIR, showed clearly that the peptide underwent a conformational transition, going from an α-helical form at low peptide molar fraction to a β-type structure at higher molar fractions. This conformational transition was detected by examination of the position of the Amide I band, the major component of which moves from 1655 cm –1 (wavenumber characteristic of an α-helix) to 1625 cm –1 (wavenumber characteristic of a sheet structure) 111,112 upon increasing the peptide molar fraction (Figure 8.4). This holds true, at least, when the peptide interacts with DOPG, but probably also for DOPC. However, a transition occurs at very low peptide molar fractions, probably
172 Cell-Penetrating Peptides: Processes and Applications FIGURE 8.2 (a) (b) (c)
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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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Page 210 and 211: Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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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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