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Index 401 structure prediction, 187–222 toxicity, 245–261 uptake kinetics, 277–293 Melittin, 236–238, 240 Membrane-associated fraction (MAF), determination of, 282–283 Membrane effect comparison, of CPPs and other peptides, 236–238 Membrane interactions, 163–183 conclusions and perspectives, 180–181 internalization, 177–180 vesicular, 177 via receptor, 177–179 origin of toxicity, 179–180 principles and background, 164–165 structural determinations, 165–177 analytical methods: conformational identifications, 166–168 circular dichroism, 167 diffraction, 168 Fourier transform infrared spectroscopy, 167–168 NMR, 166–167, 232–233 bilayers, 169 fluorescence, 169–177 electron paramagnetic resonance (EPR) spectroscopy, 177 multidisciplinary monolayer-based approach, 177–177 phospholipid interactions, 168–169 lipid-containing air–water interface, 169 lipid-free air–water interface, 168 monolayer approach, 168 unfolding for conjugate CPP–protein, 179 Membrane-mimetic solvents, 228–229, 233–236 Membrane proteins, structure prediction modeling, 204–206 Membrane targeting and transport (MTT) system, 301–302 Membrane translocating sequence (MTS) peptides, 115–140 arginine–proline-rich translocating peptides, 129–130 attaching cargo and targeting domains, 124–127 cationic translocating peptides, 127–129 commonly used, 127 future perspectives, 130–132 h-region signal sequence and, 117–122 applications of SN50 peptide, 119 development of SN50 peptide, 117–119 in integrin β 3, 122 kFGF and translocation of other cargoes, 119–122 mechanism of membrane translocation, 122–124 in nucleic acid delivery, 354–356 proline-rich peptides as translocating, 130 signal hypothesis, 116–117 Micelles, 228–229, 234–235 positioning, 234–235 structure induction, 234 Microbial membrane-permeating peptides, 377–396 applications, 388–392 as anti-infective agents, 388–389 as delivery vehicle, 389–392 experimental methods, 385–388 antimicrobial activity assays, 385–386 cell uptake assays, 386–388 cell permeabilization assays, 386–388 fluorescence microscopy and FACS, 386 mechanisms of action, 382–385 cell-killing, 383–385 cell type-specific activities, 385 dual peptide activities, 384–385 intracellular target inhibition, 384 membrane leakage, 383–384 cell uptake, 382–383 cell permeation by cationic peptides, 382–383 receptor-mediated peptide transport and endocytosis, 383 principles and background, 378–382 composition and structure, 380–382 origins and discovery, 380 Microdilution assay, 385–386 Microscopy confocal laser scanning (CLSM), 281 fluorescence, 267–269, 386, see also Fluorescence studies Model amphipathic peptides (MAPs), 71–92, see also MAPs Modeling, structure prediction, 187–222 conclusions, 215–218 methods, 190–202 atomic surface hydrophobicity (first restraint), 191–193 charge simulation (third restraint), 194–197 description of water–bilayer interface, 190–191 lipid perturbation (second restraint), 193–194 molecular hydrophobicity potential (MHP), 199–202 Monte Carlo procedure, 198 Pex2Dstat files, 198–199 procedure, 197–198
402 Cell-Penetrating Peptides: Processes and Applications principles and background, 188–190 results, 202–215 charged bilayer model, 210–215 efficiency of Monte Carlo method, 202–206 hydrophobic peptides, 202–204 membrane proteins, 204–206 penetratin, 206–207 uncharged membrane model, 207–210 Molecular hydrophobicity potential (MHP), 199–202 Monte Carlo method, in structure prediction modeling, 187–222, see also Structure prediction modeling M28 peptide, 202 M13 procoat proteins, 302 MTT assay, 251 N NFAT transcription factor, 118 N-tail phenomenon, 305 Nuclear factor-kappa B (NF-κB) SN50 subunit, 118–119 Nuclear localization sequence (NLS), see Signal sequence-based CPPs Nuclear localization signal, in nucleic acid delivery, 354–356 Nuclear magnetic resonance (NMR) biophysical studies, 232–233 of membrane interactions, 166–167 Nucleic acid delivery, 347–363 delivery strategies, 349 peptide vectors for oligonucleotide delivery, 350–360 amphiphilic peptide similar to KALA, 357 KALA peptide, 356–357 KFFKFFKFFK peptide, 357 MTS–NLS, 354–356 penetratin, 350–351 polylysine and loligomers, 357–358 pVEC, 356 Tat, 351–354 transportan, 354 principles and background, 347–348 transport of naked oligonucleotides, 348–349 O Oligonucleotides, penetratin and, 46 Oligopeptides, penetratin and, 46 P Penetratin, 127–128, 131, 224, 225, 238–239 delivery, 31–40 AntpHD internalization of polypeptides, 34–35 chemical drug, 38 of entire proteins, 38 of peptide nucleic acids (PNAs), 37–38 principles of cargo–vector linkage, 31 vectorization with AntpHD, 31–34 vectorization with penetratin peptides in vitro, 35–37 experimental procedures, 40–47 AntpHD and penetratin, 40–42 AntpHD and penetratin-coupled cargoes, 42–46 comments, 46–47 homeoprotein-derived peptidic vectors, 24–26 antennapedia homeodomain, 24–25 AntpHD mutant behavior, 25 penetratin-1 peptide, 25–26 internalization, 26–30 blood–brain barrier and, 39–40 direct perfusion in CNS, 39 internalization, immune system, 39 in vivo with penatratin-derived vectors, 39–40 peptide–lipid interactions, 28–29 peptides in blood vessels, 39 proposed models, 29–30 structural parameters and translocation, 26–28 membrane-associated fraction, 283 in nucleic acid delivery, 350–351 quantification of bioactivity, 274 structure prediction modeling, 206–207 toxicity, 253–254 translocation studies, 238–239 Penetratin/penetratin analogues, uptake kinetics, 289 Peptide nucleic acids (PNAs) penetratin and, 46 transportan and, 60–61 Permeability, see Cell membrane permeability Pex2Dstat files, 198–199 Phospholipid interactions, 168–169 lipid-containing air–water interface, 169 lipid-free air–water interface, 168 monolayer approach, 168 Phospholipids, for model studies, 226 PiHD (XcpA) signal peptidases, 307 PilD (XcpA) signal peptidases, 307 Plasmodium CS proteins, 130 Polylysine, 163 in nucleic acid delivery, 357–358 Polytopic membrane proteins, 305 Porins, 204–206 p130 proteins, Tat-E1A binding of, 370
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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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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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Cell-Penetrating Peptides as Vector
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