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TABLE 4.2 Internalization of Peptide into Aortic Endothelial Cells and Fluorescein Leakage Peptide Peptide composition pmol internalized peptide/mg protein Fluorescein leakage related to that of I-exposed cells a H µ Φ (°) α-helix TFE SDS I KLALKLALKALK-AALKLA-NH2 228 ± 54 1.0 ± 0.38 –0.0161 0.3339 80 60 68 III KLALKLALKAL-KAALK-NH2 218 ± 23 3.13 ± 0.47 –0.0161 0.3339 80 52 61 IV KLALKALKAAL-KLA-NH2
80 Cell-Penetrating Peptides: Processes and Applications pmol/mgprotein 400 350 300 250 200 150 100 50 0 30 min peptide exposure 30 min peptide exposure with 30 min re-exchange IV VI FIGURE 4.5 Intact fractions of cell-associated peptide after exposing LKB Ez 7 cells for 30 min at 37°C to 50 µM IV and VI with and without exposure to fresh DPBSG for 30 min at 37°C prior to washing and treatment with diazotized 2-nitroaniline. Each bar represents the mean of three samples ± SD. comparable order as found with I was observed for the amphipathic peptides XI and XIII. For the nonamphipathic counterparts, XII and XIV, containing charged residues uniformly distributed around the helix, no internalization was detectable. The notion that the net positive charge is of lower importance for entry into the cell interior was further supported by the similar degree of internalization found for the Antennapedia peptide XV, 9 which possesses two positive side chains more than I (Table 4.2). Common quantitation protocols, as the HPLC approach applied here, presuppose removal of the vast excess of analyte in the incubation solution by a multiple wash process. The wash steps are normally performed in the cold in order to sup<strong>press</strong> bias of the results by energy-dependent efflux processes. Since, however, MAPs are able to cross the plasma membrane in the cold, the possibility could not be ruled out that the uptake results obtained might be biased by a rapid wash-out. Initial evidence that the inability to detect cellular uptake of the nonamphipathic peptides by the described HPLC protocol indeed reflected that only poor internalization combined with a rapid wash-out was provided by uptake experiments performed at 50 µM concentration using peptides IV and VI. Under such conditions clear internalization of these unstructured peptides, which were nontoxic even at this high concentration, 29 was detected by the HPLC protocol (Figure 4.5). Likewise, Figure 4.5 illustrates an extensive escape of these peptides from preloaded cells, whereas for the amphipathic parent, peptide I, no significant efflux was measurable under the same conditions. 10 This suggested that the low intracellular levels (relative to those of the external medium) achieved with peptides IV and VI are at least partially due to wash-out.
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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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26 Cell-Penetrating Peptides: Proce
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Page 94 and 95: Model Amphipathic Peptides 73 its D
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130 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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FIGURE 9.7 (Color Figure 9.7 follow
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FIGURE 9.8 The center of the figure
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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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