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Hydrophobic Membrane Translocating Sequence Peptides 139 146. Agerberth, B. et al., Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides, Eur. J. Biochem., 202, 849, 1991. 147. Cabiaux, V. et al., Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide, Eur. J. Biochem., 224, 1019, 1994. 148. Casteels, P. et al., Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera), Eur. J. Biochem., 187, 381, 1990. 149. Casteels, P. et al., Apidaecins: antibacterial peptides from honeybees, EMBO. J., 8, 2387, 1989. 150. Gennaro, R., Skerlavaj, B., and Romeo, D., Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils, Infect. Immun., 57, 3142, 1989. 151. Frank, R.W. et al., Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils, J. Biol. Chem., 265, 18871, 1990. 152. Boman, H.G., Agerberth, B., and Boman, A., Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine, Infect. Immun., 61, 2978, 1993. 153. Gallo, R.L. and Huttner, K.M., Antimicrobial peptides: an emerging concept in cutaneous biology, J. Invest. Dermatol., 111, 739, 1998. 154. Bevins, C.L., Antimicrobial peptides as agents of mucosal immunity, Ciba. Found. Symp., 186, 250, 1994. 155. Shi, J. et al., Antibacterial activity of a synthetic peptide (PR-26) derived from PR- 39, a proline-arginine-rich neutrophil antimicrobial peptide, Antimicrob. Agents Chemother., 40, 115, 1996. 156. Miao, Z. and Tam, J.P., Bidirectional tandem pseudoproline ligations of proline-rich helical peptides, J. Am. Chem. Soc., 122, 4253, 2000. 157. Scocchi, M., Romeo, D., and Zanetti, M., Molecular cloning of Bac7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils, FEBS Lett., 352, 197, 1994. 158. Sadler, K. and Tam, J.P., Unpublished results. 159. Singh, D. et al., Penetration and intracellular routing of nucleus-directed peptidebased shuttles (loligomers) in eukaryotic cells, Biochemistry, 37, 5798, 1998. 160. Arnold, L.J., Jr. et al., Antineoplastic activity of poly(L-lysine) with some ascites tumor cells, Proc. Natl. Acad. Sci. U.S.A., 76, 3246, 1979. 161. Nussenzweig, V. and Nussenzweig, R.S., Circumsporozoite proteins of malaria parasites, Cell, 42, 401, 1985. 162. Hugel, F.U., Pradel, G., and Frevert, U., Release of malaria circumsporozoite protein into the host cell cytoplasm and interaction with ribosomes, Mol. Biochem. Parasitol., 81, 151, 1996. 163. Frevert, U. et al., Malaria circumsporozoite protein inhibits protein synthesis in mammalian cells, EMBO. J., 17, 3816, 1998. 164. Mota, M.M. et al., Migration of Plasmodium sporozoites through cells before infection, Science, 291, 141, 2001. 165. Eichinger, D.J. et al., Circumsporozoite protein of Plasmodium berghei: gene cloning and identification of the immunodominant epitopes, Mol. Cell Biol., 6, 3965, 1986. 166. Lum, B.L. et al., Molecular targets in oncology: implications of the multidrug resistance gene, Pharmacotherapy, 13, 88, 1993. 167. Boukerche, H. et al., A new Mr 55,000 surface protein implicated in melanoma progression: association with a metastatic phenotype, Cancer Res., 60, 5848, 2000.
140 Cell-Penetrating Peptides: Processes and Applications 168. Tendler, A., Kaufman, H.L., and Kadish, A.S., Increased carcinoembryonic antigen ex<strong>press</strong>ion in cervical intraepithelial neoplasia grade 3 and in cervical squamous cell carcinoma, Hum. Pathol., 31, 1357, 2000. 169. Hewett, P.W., Identification of tumour-induced changes in endothelial cell surface protein ex<strong>press</strong>ion: an in vitro model, Int. J. Biochem. Cell. Biol., 33, 325, 2001. 170. Lango, M.N., Shin, D.M., and Grandis, J.R., Targeting growth factor receptors: integration of novel therapeutics in the management of head and neck cancer, Curr. Opin. Oncol., 13, 168, 2001. 171. Fraile-Ramos, A. et al., The human cytomegalovirus US28 protein is located in endocytic vesicles and undergoes constitutive endocytosis and recycling, Mol. Cell Biol., 12, 1737, 2001. 172. Doms, R.W. and Trono, D., The plasma membrane as a combat zone in the HIV battlefield, Genes Dev., 14, 2677, 2000.
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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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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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264 Cell-Penetrating Peptides: Proc
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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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