Microbial Membrane-Permeating Peptides and Their Applications 393 7. Carlsson, A. et al., Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription, Infect. Immun., 59, 3040, 1991. 8. 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. 9. Fickel, T.E. and Gilvarg, C., Transport of impermeant substances in E. coli by way of oligopeptide permease, Nat. New Biol., 241, 161, 1973. 10. Ames, B.N. et al., Illicit transport: the oligopeptide permease, Proc. Natl. Acad. Sci. U.S.A., 70, 456, 1973. 11. Payne, J.W., Drug delivery stystems: optimising the structure of peptide carriers for synthetic antimicrobial drugs, Drugs Exp. Clin. Res., 12, 585, 1986. 12. Nikaido, H., Prevention of drug access to bacterial targets: permeability barriers and active efflux, Science, 264, 382, 1994. 13. Alberts, B. et al., Molecular Biology of the Cell, Garland Publishing Inc., New York, 1994. 14. Broach, J.R., Pringle, J.R., and Jones, E.W., The Molecular and Cellular Biology of the Yeast Saccharomyces, Cold Spring Harbor Laboratory Press, New York, 1997. 15. Steiner, H. et al., Sequence and specificity of two antibacterial proteins involved in insect immunity, Nature, 292, 246, 1981. 16. Selsted, M.E. et al., Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages, J. Biol. Chem., 258, 14485, 1983. 17. Zasloff, M., Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor, Proc. Natl. Acad. Sci. U.S.A., 84, 5449, 1987. 18. Fearon, D.T. and Locksley, R.M., The instructive role of innate immunity in the acquired immune response, Science, 272, 50, 1996. 19. Hoffmann, J.A. et al., Phylogenetic perspectives in innate immunity, Science, 284, 1313, 1999. 20. Guina, T. et al., A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides, J. Bacteriol., 182, 4077, 2000. 21. Tang, Y.Q. et al., A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins, Science, 286, 498, 1999. 22. Derua, R., Gustafson, K.R. and Pannell, L.K., Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides, Biochem. Biophys. Res. Commun., 228, 632, 1996. 23. Gonzalez, C. et al., Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin, Proc. Natl. Acad. Sci. U.S.A., 97, 11221, 2000. 24. Maloy, W.L. and Kari, U.P., Structure-activity studies on magainins and other host defense peptides, Biopolymers, 37, 105, 1995. 25. Vunnam, S., Juvvadi, P., and Merrifield, R.B., Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine, J. Pept. Res., 49, 59, 1997. 26. Oren, Z. and Shai, Y., Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function, Biochemistry, 39, 6103, 2000.
394 Cell-Penetrating Peptides: Processes and Applications 27. Fernandez-Lopez, S. et al., Antibacterial agents based on the cyclic D,L-alpha-peptide architecture, Nature, 412, 452, 2001. 28. Shai, Y., Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membranelytic peptides, Biochim. Biophys. Acta, 1462, 55, 1999. 29. Huang, H.W., Action of antimicrobial peptides: two-state model, Biochemistry, 39, 8347, 2000. 30. Matsuzaki, K., Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes, Biochim. Biophys. Acta, 1462, 1, 1999. 31. Kobayashi, S. et al., Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor, Biochemistry, 39, 8648, 2000. 32. Zhang, L., Rozek, A., and Hancock, R.E., Interaction of cationic antimicrobial peptides with model membranes, J. Biol. Chem., 25, 25, 2001. 33. Guo, L. et al., Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides, Cell, 95, 189, 1998. 34. Friedrich, C. et al., Salt-resistant alpha-helical cationic antimicrobial peptides, Antimicrob. Agents Chemother., 43, 1542, 1999. 35. Tossi, A., Sandri, L., and Giangaspero, A., Amphipathic, alpha-helical antimicrobial peptides, Biopolymers, 55, 4, 2000. 36. Naider, F. and Becker, J. M., Peptide transport in Candida albicans: implications for the development of antifungal agents, Curr. Top. Med. Mycol., 2, 170, 1988. 37. Hancock, R.E.W., Drug Transport in Antimicrobial and Anticancer Chemotherapy, Marcel Dekker, New York, 1994. 38. Sandvig, K. and van Deurs, B., Endocytosis and intracellular transport of ricin: recent discoveries, FEBS Lett., 452, 67, 1999. 39. Falnes, P.O. and Sandvig, K., Penetration of protein toxins into cells, Curr. Opin. Cell Biol., 12, 407, 2000. 40. Sandvig, K. and van Deurs, B., Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives, Embo J., 19, 5943, 2000. 41. Westerhoff, H.V. et al., Magainins and the disruption of membrane-linked free-energy transduction, Proc. Natl. Acad. Sci. U.S.A., 86, 6597, 1989. 42. Yang, L. et al., Crystallization of antimicrobial pores in membranes: magainin and protegrin, Biophys. J., 79, 2002, 2000. 43. Kragol, G. et al., The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding, Biochemistry, 40, 3016, 2001. 44. Sharma, S. and Khuller, G., DNA as the intracellular secondary target for antibacterial action of human neutrophil peptide-I against Mycobacterium tuberculosis H37Ra, Curr. Microbiol., 43, 74, 2001. 45. Helmerhorst, E.J. et al., The cellular target of histatin 5 on Candida albicans is the energized mitochondrion, J. Biol. Chem., 274, 7286, 1999. 46. Debono, M. and Gordee, R.S., Antibiotics that inhibit fungal cell wall development, Annu. Rev. Microbiol., 48, 471, 1994. 47. Lupetti, A. et al., Candidacidal activities of human lactoferrin peptides derived from the N terminus, Antimicrob. Agents Chemother., 44, 3257, 2000. 48. Boman, H.G. et al., Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids, FEBS Lett., 259, 103, 1989. 49. Andreu, D. et al., Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity, FEBS Lett., 296, 190, 1992.
- Page 2 and 3:
CELL- PENETRATING PEPTIDES Processe
- Page 4 and 5:
Pharmacology and Toxicology: Basic
- Page 7 and 8:
Library of Congress Cataloging-in-P
- Page 9 and 10:
to the handbook are prominent resea
- Page 11 and 12:
REFERENCES 1. Green, M. and Loewens
- Page 14 and 15:
Contributors Mats Andersson Microbi
- Page 16 and 17:
Erin T. Pelkey Department of Chemis
- Page 18 and 19:
Contents Section I Classes of Cell-
- Page 20:
Chapter 16 Cell-Penetrating Peptide
- Page 24 and 25:
1 CONTENTS 0-8493-1141-1/02/$0.00+$
- Page 26 and 27:
The Tat-Derived Cell-Penetrating Pe
- Page 28 and 29:
The Tat-Derived Cell-Penetrating Pe
- Page 30 and 31:
The Tat-Derived Cell-Penetrating Pe
- Page 32 and 33:
The Tat-Derived Cell-Penetrating Pe
- Page 34 and 35:
The Tat-Derived Cell-Penetrating Pe
- Page 36 and 37:
The Tat-Derived Cell-Penetrating Pe
- Page 38 and 39:
The Tat-Derived Cell-Penetrating Pe
- Page 40 and 41:
The Tat-Derived Cell-Penetrating Pe
- Page 42:
The Tat-Derived Cell-Penetrating Pe
- Page 45 and 46:
24 Cell-Penetrating Peptides: Proce
- Page 47 and 48:
26 Cell-Penetrating Peptides: Proce
- Page 49 and 50:
28 Cell-Penetrating Peptides: Proce
- Page 51 and 52:
30 Cell-Penetrating Peptides: Proce
- Page 53 and 54:
32 Cell-Penetrating Peptides: Proce
- Page 55 and 56:
34 Cell-Penetrating Peptides: Proce
- Page 57 and 58:
36 Cell-Penetrating Peptides: Proce
- Page 59 and 60:
38 Cell-Penetrating Peptides: Proce
- Page 61 and 62:
40 Cell-Penetrating Peptides: Proce
- Page 63 and 64:
42 Cell-Penetrating Peptides: Proce
- Page 65 and 66:
44 Cell-Penetrating Peptides: Proce
- Page 67 and 68:
46 Cell-Penetrating Peptides: Proce
- Page 69 and 70:
48 Cell-Penetrating Peptides: Proce
- Page 71 and 72:
50 Cell-Penetrating Peptides: Proce
- Page 74 and 75:
3 Transportans Margus Pooga, Mattia
- Page 76 and 77:
Transportans 55 Indeed, galparan is
- Page 78 and 79:
Transportans 57 especially the endo
- Page 80 and 81:
Transportans 59 In the penetration
- Page 82 and 83:
Transportans 61 A 21-mer antisense
- Page 84 and 85:
Transportans 63 Commonly, the prote
- Page 86 and 87:
Transportans 65 antibiotin antibodi
- Page 88 and 89:
Transportans 67 For cross-linking o
- Page 90 and 91:
Transportans 69 and still retain ef
- Page 92 and 93:
4 CONTENTS 0-8493-1141-1/02/$0.00+$
- Page 94 and 95:
Model Amphipathic Peptides 73 its D
- Page 96 and 97:
Model Amphipathic Peptides 75 pmol/
- Page 98 and 99:
TABLE 4.1 Internalization of Peptid
- Page 100 and 101:
TABLE 4.2 Internalization of Peptid
- Page 102 and 103:
Model Amphipathic Peptides 81 relat
- Page 104 and 105:
Model Amphipathic Peptides 83 relat
- Page 106 and 107:
Model Amphipathic Peptides 85 relat
- Page 108 and 109:
Model Amphipathic Peptides 87 A cat
- Page 110 and 111:
Model Amphipathic Peptides 89 At th
- Page 112 and 113:
Model Amphipathic Peptides 91 16. H
- Page 114 and 115:
5 CONTENTS 0-8493-1141-1/02/$0.00+$
- Page 116 and 117:
Signal Sequence-Based Cell-Penetrat
- Page 118 and 119:
Signal Sequence-Based Cell-Penetrat
- Page 120 and 121:
Signal Sequence-Based Cell-Penetrat
- Page 122 and 123:
Signal Sequence-Based Cell-Penetrat
- Page 124 and 125:
Signal Sequence-Based Cell-Penetrat
- Page 126 and 127:
Signal Sequence-Based Cell-Penetrat
- Page 128 and 129:
Signal Sequence-Based Cell-Penetrat
- Page 130 and 131:
Signal Sequence-Based Cell-Penetrat
- Page 132 and 133:
Signal Sequence-Based Cell-Penetrat
- Page 134:
Signal Sequence-Based Cell-Penetrat
- Page 137 and 138:
116 Cell-Penetrating Peptides: Proc
- Page 139 and 140:
118 Cell-Penetrating Peptides: Proc
- Page 141 and 142:
120 Cell-Penetrating Peptides: Proc
- Page 143 and 144:
122 Cell-Penetrating Peptides: Proc
- Page 145 and 146:
124 Cell-Penetrating Peptides: Proc
- Page 147 and 148:
126 Cell-Penetrating Peptides: Proc
- Page 149 and 150:
128 Cell-Penetrating Peptides: Proc
- Page 151 and 152:
130 Cell-Penetrating Peptides: Proc
- Page 153 and 154:
132 Cell-Penetrating Peptides: Proc
- Page 155 and 156:
134 Cell-Penetrating Peptides: Proc
- Page 157 and 158:
136 Cell-Penetrating Peptides: Proc
- Page 159 and 160:
138 Cell-Penetrating Peptides: Proc
- Page 161 and 162:
140 Cell-Penetrating Peptides: Proc
- Page 163 and 164:
142 Cell-Penetrating Peptides: Proc
- Page 165 and 166:
144 Cell-Penetrating Peptides: Proc
- Page 167 and 168:
146 Cell-Penetrating Peptides: Proc
- Page 169 and 170:
148 Cell-Penetrating Peptides: Proc
- Page 171 and 172:
150 Cell-Penetrating Peptides: Proc
- Page 173 and 174:
152 Cell-Penetrating Peptides: Proc
- Page 175 and 176:
154 Cell-Penetrating Peptides: Proc
- Page 177 and 178:
156 Cell-Penetrating Peptides: Proc
- Page 179 and 180:
158 Cell-Penetrating Peptides: Proc
- Page 181 and 182:
160 Cell-Penetrating Peptides: Proc
- Page 184 and 185:
8 CONTENTS 0-8493-1141-1/02/$0.00+$
- Page 186 and 187:
Interactions of Cell-Penetrating Pe
- Page 188 and 189:
Interactions of Cell-Penetrating Pe
- Page 190 and 191:
Interactions of Cell-Penetrating Pe
- Page 192 and 193:
Interactions of Cell-Penetrating Pe
- Page 194 and 195:
Interactions of Cell-Penetrating Pe
- Page 196 and 197:
Interactions of Cell-Penetrating Pe
- Page 198 and 199:
Interactions of Cell-Penetrating Pe
- Page 200 and 201:
Interactions of Cell-Penetrating Pe
- Page 202 and 203:
Interactions of Cell-Penetrating Pe
- Page 204 and 205:
Interactions of Cell-Penetrating Pe
- Page 206 and 207:
Interactions of Cell-Penetrating Pe
- Page 208 and 209:
9 CONTENTS 0-8493-1141-1/02/$0.00+$
- Page 210 and 211:
Structure Prediction of CPPs and It
- Page 212 and 213:
Structure Prediction of CPPs and It
- Page 214 and 215:
Structure Prediction of CPPs and It
- Page 216 and 217:
Structure Prediction of CPPs and It
- Page 218 and 219:
Structure Prediction of CPPs and It
- Page 220 and 221:
Structure Prediction of CPPs and It
- Page 222 and 223:
Structure Prediction of CPPs and It
- Page 224 and 225:
Structure Prediction of CPPs and It
- Page 226 and 227:
Structure Prediction of CPPs and It
- Page 228 and 229:
FIGURE 9.7 (Color Figure 9.7 follow
- Page 230 and 231:
FIGURE 9.8 The center of the figure
- Page 232 and 233:
Structure Prediction of CPPs and It
- Page 234 and 235:
Structure Prediction of CPPs and It
- Page 236 and 237:
Structure Prediction of CPPs and It
- Page 238 and 239:
Structure Prediction of CPPs and It
- Page 240 and 241:
Structure Prediction of CPPs and It
- Page 242 and 243:
Structure Prediction of CPPs and It
- Page 244 and 245:
10 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 246 and 247:
Biophysical Studies of Cell-Penetra
- Page 248 and 249:
Biophysical Studies of Cell-Penetra
- Page 250 and 251:
Biophysical Studies of Cell-Penetra
- Page 252 and 253:
Biophysical Studies of Cell-Penetra
- Page 254 and 255:
Biophysical Studies of Cell-Penetra
- Page 256 and 257:
Biophysical Studies of Cell-Penetra
- Page 258 and 259:
Biophysical Studies of Cell-Penetra
- Page 260 and 261:
Biophysical Studies of Cell-Penetra
- Page 262 and 263:
Biophysical Studies of Cell-Penetra
- Page 264 and 265:
Biophysical Studies of Cell-Penetra
- Page 266 and 267:
11 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 268 and 269:
Toxicity and Side Effects of Cell-P
- Page 270 and 271:
Toxicity and Side Effects of Cell-P
- Page 272 and 273:
Toxicity and Side Effects of Cell-P
- Page 274 and 275:
Toxicity and Side Effects of Cell-P
- Page 276 and 277:
Toxicity and Side Effects of Cell-P
- Page 278 and 279:
Toxicity and Side Effects of Cell-P
- Page 280 and 281:
Toxicity and Side Effects of Cell-P
- Page 282:
Toxicity and Side Effects of Cell-P
- Page 285 and 286:
264 Cell-Penetrating Peptides: Proc
- Page 287 and 288:
266 Cell-Penetrating Peptides: Proc
- Page 289 and 290:
268 Cell-Penetrating Peptides: Proc
- Page 291 and 292:
270 Cell-Penetrating Peptides: Proc
- Page 293 and 294:
272 Cell-Penetrating Peptides: Proc
- Page 295 and 296:
274 Cell-Penetrating Peptides: Proc
- Page 298 and 299:
13 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 300 and 301:
Kinetics of Uptake of Cell-Penetrat
- Page 302 and 303:
Kinetics of Uptake of Cell-Penetrat
- Page 304 and 305:
Kinetics of Uptake of Cell-Penetrat
- Page 306 and 307:
Kinetics of Uptake of Cell-Penetrat
- Page 308 and 309:
Kinetics of Uptake of Cell-Penetrat
- Page 310 and 311:
Kinetics of Uptake of Cell-Penetrat
- Page 312 and 313:
Kinetics of Uptake of Cell-Penetrat
- Page 314:
Kinetics of Uptake of Cell-Penetrat
- Page 317 and 318:
296 Cell-Penetrating Peptides: Proc
- Page 319 and 320:
298 Cell-Penetrating Peptides: Proc
- Page 321 and 322:
300 Cell-Penetrating Peptides: Proc
- Page 323 and 324:
302 Cell-Penetrating Peptides: Proc
- Page 325 and 326:
304 Cell-Penetrating Peptides: Proc
- Page 327 and 328:
306 Cell-Penetrating Peptides: Proc
- Page 329 and 330:
308 Cell-Penetrating Peptides: Proc
- Page 331 and 332:
310 Cell-Penetrating Peptides: Proc
- Page 333 and 334:
312 Cell-Penetrating Peptides: Proc
- Page 335 and 336:
314 Cell-Penetrating Peptides: Proc
- Page 337 and 338:
316 Cell-Penetrating Peptides: Proc
- Page 339 and 340:
318 Cell-Penetrating Peptides: Proc
- Page 341 and 342:
320 Cell-Penetrating Peptides: Proc
- Page 343 and 344:
322 Cell-Penetrating Peptides: Proc
- Page 345 and 346:
324 Cell-Penetrating Peptides: Proc
- Page 348 and 349:
15 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 350 and 351:
Cell-Penetrating Peptide Conjugatio
- Page 352 and 353:
Cell-Penetrating Peptide Conjugatio
- Page 354 and 355:
Cell-Penetrating Peptide Conjugatio
- Page 356 and 357:
Cell-Penetrating Peptide Conjugatio
- Page 358 and 359:
Cell-Penetrating Peptide Conjugatio
- Page 360 and 361:
Cell-Penetrating Peptide Conjugatio
- Page 362 and 363:
FIGURE 15.9 (Color Figure 15.9 foll
- Page 364 and 365: Cell-Penetrating Peptide Conjugatio
- Page 366 and 367: Cell-Penetrating Peptide Conjugatio
- Page 368 and 369: 16 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 370 and 371: Cell-Penetrating Peptides as Vector
- Page 372 and 373: Cell-Penetrating Peptides as Vector
- Page 374 and 375: TABLE 16.1 Examples of Transport of
- Page 376 and 377: Cell-Penetrating Peptides as Vector
- Page 378 and 379: Cell-Penetrating Peptides as Vector
- Page 380 and 381: CPP 2 Cargo or mRNA CAP Antisense A
- Page 382 and 383: Cell-Penetrating Peptides as Vector
- Page 384: Cell-Penetrating Peptides as Vector
- Page 387 and 388: 366 Cell-Penetrating Peptides: Proc
- Page 389 and 390: 368 Cell-Penetrating Peptides: Proc
- Page 391 and 392: 370 Cell-Penetrating Peptides: Proc
- Page 393 and 394: 372 Cell-Penetrating Peptides: Proc
- Page 395 and 396: 374 Cell-Penetrating Peptides: Proc
- Page 398 and 399: 18 CONTENTS 0-8493-1141-1/02/$0.00+
- Page 400 and 401: Microbial Membrane-Permeating Pepti
- Page 402 and 403: Microbial Membrane-Permeating Pepti
- Page 404 and 405: Microbial Membrane-Permeating Pepti
- Page 406 and 407: Microbial Membrane-Permeating Pepti
- Page 408 and 409: Microbial Membrane-Permeating Pepti
- Page 410 and 411: Microbial Membrane-Permeating Pepti
- Page 412 and 413: Microbial Membrane-Permeating Pepti
- Page 416 and 417: Microbial Membrane-Permeating Pepti
- Page 418 and 419: Index A Abaecin, 129 Abz radiolabel
- Page 420 and 421: Index 399 Diffraction, 168 Disulphi
- Page 422 and 423: Index 401 structure prediction, 187
- Page 424 and 425: Index 403 pRB proteins, Tat-E1A bin
- Page 426 and 427: Index 405 lipid perturbation (secon