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Microbial Membrane-Permeating Peptides and Their Applications 395 50. Lehrer, R.I. and Ganz, T., Antimicrobial peptides in mammalian and insect host defence, Curr. Opin. Immunol., 11, 23, 1999. 51. DeLucca, A.J. et al., Fungicidal activity of cecropin A, Antimicrob. Agents Chemother., 41, 481, 1997. 52. Hultmark, D. et al., Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia, Embo J., 2, 571, 1983. 53. Wu, M. and Hancock, R.E., Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane, J. Biol. Chem., 274, 29, 1999. 54. Lorian, V., Antibiotics in Laboratory Medicine, 4th ed., Williams & Wilkins, Baltimore, 1996. 55. Mason, D.J. et al., Antimicrobial action of rabbit leukocyte CAP18(106-137), Antimicrob. Agents Chemother., 41, 624, 1997. 56. Lehrer, R.I., Barton, A., and Ganz, T., Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry, J. Immunol. Methods, 108, 153, 1988. 57. Giacometti, A. et al., In-vitro activity and killing effect of polycationic peptides on methicillin-resistant Staphylococcus aureus and interactions with clinically used antibiotics, Diagn. Microbiol. Infect. Dis., 38, 115, 2000. 58. Linde, C.M. et al., In vitro activity of PR-39, a proline-arginine-rich peptide, against susceptible and multi-drug-resistant Mycobacterium tuberculosis, J. Antimicrob. Chemother., 47, 575, 2001. 59. Steinberg, D.A. et al., Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity, Antimicrob. Agents Chemother., 41, 1738, 1997. 60. Ahmad, I. et al., Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity, Biochim. Biophys. Acta, 1237, 109, 1995. 61. Welling, M.M. et al., Antibacterial activity of human neutrophil defensins in experimental infections in mice is accompanied by increased leukocyte accumulation, J. Clin. Invest., 102, 1583, 1998. 62. Bals, R. et al., Augmentation of innate host defense by ex<strong>press</strong>ion of a cathelicidin antimicrobial peptide, Infect. Immun., 67, 6084, 1999. 63. Kisich, K.O. et al., Antimycobacterial agent based on mRNA encoding human betadefensin 2 enables primary macrophages to restrict growth of Mycobacterium tuberculosis, Infect. Immun., 69, 2692, 2001. 64. Tsiodras, S. et al., Linezolid resistance in a clinical isolate of Staphylococcus aureus, Lancet, 358, 207, 2001. 65. Gonzales, R.D. et al., Infections due to vancomycin-resistant Enterococcus faecium resistant to linezolid, Lancet, 357, 1179, 2001. 66. Hancock, R.E., The bacterial outer membrane as a drug barrier, Trends Microbiol., 5, 37, 1997. 67. Wittung, P. et al., Phospholipid membrane permeability of peptide nucleic acid, FEBS Lett., 365, 27, 1995. 68. Good, L. and Nielsen, P.E., Inhibition of translation and bacterial growth by peptide nucleic acid targeted to ribosomal RNA, Proc. Natl. Acad. Sci. U.S.A., 95, 2073, 1998. 69. Good, L. et al., Antisense PNA effects in Escherichia coli are limited by the outermembrane LPS layer, Microbiology, 146, 2665, 2000. 70. Vaara, M. and Porro, M., Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria, Antimicrob. Agents Chemother., 40, 1801, 1996. 71. Cronan, J.E. and Rock, C.O., Escherichia coli and Salmlonella: Cellular and Molecular Biology, 2nd ed., American Society for Microbiology, Washington, D.C., 1996.
396 Cell-Penetrating Peptides: Processes and Applications 72. Breukink, E. et al., Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic, Science, 286, 2361, 1999. 73. Park, C.B. et al., Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions, Biochem. Biophys. Res. Commun., 244, 253, 1998. 74. Tsai, H. and Bobek, L.A., Human salivary histatins: promising anti-fungal therapeutic agents, Crit. Rev. Oral Biol. Med., 9, 480, 1998. 75. Skerlavaj, B., Romeo, D., and Gennaro, R., Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins, Infect. Immun., 58, 3724, 1990. 76. Couto, M.A., Harwig, S.S., and Lehrer, R.I., Selective inhibition of microbial serine proteases by eNAP-2, an antimicrobial peptide from equine neutrophils, Infect. Immun., 61, 2991, 1993.
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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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FIGURE 15.9 (Color Figure 15.9 foll
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Page 366 and 367: Cell-Penetrating Peptide Conjugatio
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Page 370 and 371: Cell-Penetrating Peptides as Vector
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Page 400 and 401: Microbial Membrane-Permeating Pepti
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Page 424 and 425: Index 403 pRB proteins, Tat-E1A bin
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