Interactions of Cell-Penetrating Peptides with Membranes 185 83. Silvestro, L. and Axelsen, P.H., Fourier transform infrared linked analysis of conformational changes in annexinV upon membrane binding, Biochemistry, 38, 113, 1999. 84. Burger, K.N.J. et al., The interaction of synthetic analogs of the N-terminal fusion sequence of influenza virus with a lipid monolayer. Comparison of fusion-active and fusion-defective analogs, Biochim. Biophys. Acta, 1065, 121, 1991. 85. Briggs, M.S. et al., Conformations of signal peptides induced by lipids suggest initial steps in protein export, Science, 233, 206, 1986. 86. Lindblom, G. and Quist, P.-O., Protein and peptide interactions with lipids: structure, membrane function and new methods, Curr. Opin. Colloid Interface Sci., 3, 499, 1998. 87. Taylor, S.E. et al., Structure of a fusion peptide analogue at the air–water interface, determined from surface activity, infrared spectroscopy and scanning force microscopy, Biophys. Chem., 87, 63, 2000. 88. Elmore, D.L. and Dluhy, R.A., Application of 2D IR correlation analysis to phase transitions in Langmuir monolayer films, Colloids Surf. A: Physicochem. Eng. Aspects, 171, 225, 2000. 89. Cortijo, M. et al., Intrinsic protein–lipid interactions. Infrared spectroscopic studies of gramicidin A, bacteriorhodopsin and Ca 2+ -ATPase in biomembranes and reconstituted systems, J. Mol. Biol., 157, 597, 1982. 90. Dempsey, C.E., The actions of melittin on membranes, Biochim. Biophys. Acta, 1031, 143, 1990. 91. Latal, A. et al., Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids, Eur. J. Biochem., 248, 938, 1997. 92. Cummings, C.E. et al., Structural and functional studies of a synthetic peptide mimicking a proposed membrane inserting region of a Bacillus thuringiensis δ-endotoxin, Mol. Membr. Biol., 11, 87, 1994. 93. Tamm, L.K. and Tatulian, S.A., Infrared spectroscopy of proteins and peptides in lipid bilayers, Q. Rev. Biophys., 30, 365, 1997. 94. Baty, D. et al., A 136-amino-acid-residue COOH-terminal fragment of colicin A is endowed with ionophoric activity, Eur. J. Biochem., 30, 409, 1990. 95. Pécheur, I. et al., Protein-induced fusion can be modulated by target membrane lipids through a structural switch at the level of the fusion peptide, J. Biol. Chem., 275, 3936, 2000. 96. Vié, V. et al., Lipid-induced pore formation of the Bacillus thuringiensis Cry1Aa insecticidal toxin, J. Membr. Biol., 180, 195, 2001. 97. Lakowicz, J.R., in Principles of Florescence Spectroscopy, Plenum Press, New York, 1986. 98. Kenworthy, A.K., Petranova, N., and Edidin, M., High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes, Mol. Biol. Cell, 11, 1645, 2000. 99. Lakey, J.H. et al., Membrane insertion of the pore-forming domain of colicin A. A spectroscopic study, Eur. J. Biochem., 196, 599, 1991. 100. Edidin, M., Lipid microdomains in cell surface membranes, Curr. Opin. Struct. Biol., 7, 528, 1997. 101. Zazadzinski, J.A. et al., Langmuir–Blodgett films, Science, 263, 1726, 1994. 102. Mou, J.D., Czalkowsky, M., and Shao, Z., Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers, Biochemistry, 35, 3222, 1996. 103. ten Grotenhuis, E.R. et al., Phase behavior of stratum corneum lipids in mixed Langmuir–Blodgett monolayers, Biophys. J., 71, 1389, 1996.
186 Cell-Penetrating Peptides: Processes and Applications 104. Vié, V. et al., Distribution of ganglioside G M1 between two-components, two phase phosphatidylcholine monolayers, Langmuir, 14, 4574, 1998. 105. Czajkowsky, D.M. et al., Direct visualization of surface charge in aqueous solution, Ultramicroscopy, 74, 1, 1998. 106. Gliss, C. et al., Direct detection of domains in phospholipid bilayers by grazing incidence diffraction of neutrons and atomic force microscopy, Biophys. J., 74, 2443, 1998. 107. Hollars, C.W. and Dunn, R.C., Submicron structure of L-α-dipalmitoylphosphatidylcholine monolayers and bilayers probed with confocal, atomic force, and near field microscopy, Biophys. J., 75, 342, 1998. 108. Hui, S.W. et al., The structure and stability of phospholipid bilayers by atomic force microscopy, Biophys. J., 68, 171, 1995. 109. Gaines, G.L., Mixed monolayers, in Insoluble Monolayers at Liquid–Gas Interfaces, Prigogine, I., Ed., Interscience, New York, 281, 1966. 110. Crisp, D.J., A two dimensional phase rule. I. Derivation of a two-dimensional phase rule for planar interface. II. Some applications of a two dimensional phase rule for a single surface, in Surface Chemistry, Butterworths, London, 17, 1949. 111. Arrondo, J.L.R. et al., Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy, Prog. Biophys. Mol. Biol., 59, 23, 1993. 112. Dong, A., Huang, P., and Caughey, W.S., Protein secondary structures in water from second-derivative amide I infrared spectra, Biochemistry, 29, 3303, 1990. 113. Taneva, S. and Keough, K.M.W., Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air–water interface. I. Monolayers of pulmonary surfactant protein SP-B and phospholipids, Biophys. J., 66, 1137, 1994. 114. Berlose, J.P. et al., Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments, Eur. J. Biochem., 242, 372, 1996. 115. van der Goot, F.G. et al., A “molten-globule” membrane insertion intermediate of the pore-forming domain of colicin A, Nature, 354, 408, 1991. 116. Bychkova, V.E., Pain, R.H., and Ptitsyn, O.B., The “molten globule” state is involved in the translocation of proteins across membranes? FEBS Lett., 238, 231, 1988. 117. Beven, L. et al., Effect on mollicutes of peptides comprising a signal peptide or a fusion peptide and a nuclear localization sequence (NLS): a comparison with melittin, Biochim. Biophys. Acta, 1329, 357, 1997. 118. Chaloin, L. et al., Ionic channels formed by primary amphipathic peptides, Biochim. Biophys. Acta, 1375, 52, 1998.
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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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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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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 83 relat
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Model Amphipathic Peptides 85 relat
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Model Amphipathic Peptides 87 A cat
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Model Amphipathic Peptides 91 16. H
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Toxicity and Side Effects of Cell-P
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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 Peptide Conjugatio
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptides as Vector
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TABLE 16.1 Examples of Transport of
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Cell-Penetrating Peptides as Vector
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CPP 2 Cargo or mRNA CAP Antisense A
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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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