crc press - E-Lib FK UWKS

More documents

Recommendations

Info

Transportans 69 and still retain efficient uptake. Moreover, transportan can deliver proteins in a native, folded state of up to at least 150 kDa to the cytoplasm of living cells. ACKNOWLEDGMENTS This work was supported by grants from the EC Biotechnology Project BIO4-98-0227, Swedish Research Councils TFR and NFR, and Estonian Science Foundation (ESF4007). REFERENCES 1. Derossi, D. et al., The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem., 269, 10444, 1994. 2. Vivés, E., Brodin, P., and Lebleu, B., A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus, J. Biol. Chem., 272, 16010, 1997. 3. Elliott, G. and O’Hare, P., Intercellular trafficking and protein delivery by a herpesvirus structural protein, Cell, 88, 223, 1997. 4. Chaloin, L. et al., Conformations of primary amphipathic carrier peptides in membrane mimicking environments, Biochemistry, 36, 11179, 1997. 5. Pooga, M. et al., Cell penetration by transportan, FASEB J., 12, 67, 1998. 6. Oehlke, J. et al., Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior nonendocytically, Biochim. Biophys. Acta., 1414, 127, 1998. 7. Langel, Ü. et al., A galanin-mastoparan chimeric peptide activates the Na + ,K + -ATPase and reverses its inhibition by ouabain, Regul. Pept., 62, 47, 1996. 8. Land, T. et al., Linear and cyclic N-terminal galanin fragments and analogs as ligands at the hypothalamic galanin receptor, Int. J. Pept. Protein. Res., 38, 267, 1991. 9. Langel, Ü., Land, T., and Bartfai, T., Design of chimeric peptide ligands to galanin receptors and substance P receptors, Int. J. Pept. Protein. Res., 39, 516, 1992. 10. Consolo, S. et al., Galparan induces in vivo acetylcholine release in the frontal cortex, Brain Res., 756, 174, 1997. 11. Östenson, C-G. et al., Galparan: a powerful insulin-releasing chimeric peptide acting at a novel site, Endocrinology, 138, 3308, 1997. 12. Pooga, M. et al., Novel galanin receptor ligands, J. Pept. Res., 51, 65, 1998. 13. Heuser, J.E. and Anderson, R.G., Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation, J. Cell. Biol., 108, 389, 1989. 14. Lindgren, M. et al., Translocation properties of novel cell penetrating transportan and penetratin analogues, Bioconjug. Chem., 11, 619, 2000. 15. Soomets, U. et al., From galanin and mastoparan to galparan and transportan, Curr. Top. Pept. Protein. Res., 2, 83, 1997. 16. Higashijima, T. et al., Conformational change of mastoparan from wasp venom on binding with phospholipid membrane, FEBS Lett., 152, 227, 1983. 17. Higashijima, T. et al., Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins), J. Biol. Chem., 263, 6491, 1988. 18. Mousli, M. et al., G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides, Trends Pharmacol. Sci., 11, 358, 1990.
70 Cell-Penetrating Peptides: Processes and Applications 19. Zorko, M. et al., Differential regulation of GTPase activity by mastoparan and galparan, Arch. Biochem. Biophys., 349, 321, 1998. 20. Pooga, M. et al., Galanin-based peptides, galparan and transportan, with receptordependent and independent activities, Ann. N.Y. Acad. Sci., 863, 450, 1998. 21. Hällbrink, M. et al., Effects of vaso<strong>press</strong>in-mastoparan chimeric peptides on insulin release and G-protein activity, Regul. Pept., 82, 45, 1999. 22. Krishnakumari, V. and Nagaraj, R., Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogs, J. Pept. Res., 50, 88, 1997. 23. Soomets, U. et al., Deletion analogues of transportan, Biochim. Biophys. Acta, 1467, 165, 2000. 24. Meldal, M. and Breddam, K., Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsin, Anal. Biochem., 195, 141, 1991. 25. Nielsen, P.E. et al., Sequence-selective recognition of DNA by strand displacement with a thymine-substituted polyamide, Science, 254, 1497–1500, 1991. 26. Kumar, R. et al., The first analogues of LNA (locked nucleic acids): phosphorothioate- LNA and 2′-thio-LNA, Bioorg. Med. Chem. Lett., 8, 2219, 1998. 27. Summerton, J., Morpholino antisense oligomers: the case for an RNase H-independent structural type, Biochim. Biophys. Acta, 1489, 141, 1999. 28. Ray, A. and Nordén, B., Peptide nucleic acid (PNA): its medical and biotechnical applications and promise for the future, FASEB J., 14, 1041, 2000. 29. Pooga, M. et al., Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo, Nat. Biotechnol., 16, 857, 1998. 30. Sei, S. et al., Identification of a key target sequence to block human immunodeficiency virus type 1 replication within the gag-pol transframe domain, J. Virol., 74, 4621, 2000. 31. Schwarze, S.R., Hruska, K.A., and Dowdy, S.F., Protein transduction: unrestricted delivery into all cells? Trends Cell. Biol., 10, 290, 2000. 32. Tsien, R.Y., The green fluorescent protein, Annu. Rev. Biochem., 67, 509, 1988. 33. Schwarze, S.R. et al., In vivo protein transduction: delivery of a biologically active protein into the mouse, Science, 285, 1569, 1999. 34. Peeters, J.M. et al., Comparison of four bifunctional reagents for coupling peptides to proteins and the effect of the three moieties on the immunogenicity of the conjugates, J. Immunol. Methods, 120, 133, 1989. 35. Bernatowicz, M.S., Matsueda, R., and Matsueda, G.R., Preparation of Boc-[S- (3-nitro-2-pyridinesulfenyl)]-cysteine and its use for unsymmetrical disulfide bond formation, Int. J. Pept. Protein. Res., 28, 107, 1986. 36. Lindberg, M. et al., Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR, Biochemistry, 40, 3141, 2001. 37. Brasseur, R., Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations, J. Biol. Chem., 266, 16120, 1991. 38. Pooga, M. et al., Cellular translocation of proteins by transportan, FASEB J., 15, 1400, 2001.
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:
Page 30 and 31:
Page 32 and 33:
Page 34 and 35:
Page 36 and 37:
Page 38 and 39:
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 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 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 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 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:
Page 145 and 146:
Page 147 and 148:
Page 149 and 150:
Page 151 and 152:
Page 153 and 154:
Page 155 and 156:
Page 157 and 158:
Page 159 and 160:
Page 161 and 162:
Page 163 and 164:
Page 165 and 166:
Page 167 and 168:
Page 169 and 170:
Page 171 and 172:
Page 173 and 174:
Page 175 and 176:
Page 177 and 178:
Page 179 and 180:
Page 181 and 182:
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:
Page 190 and 191:
Page 192 and 193:
Page 194 and 195:
Page 196 and 197:
Page 198 and 199:
Page 200 and 201:
Page 202 and 203:
Page 204 and 205:
Page 206 and 207:
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:
Page 214 and 215:
Page 216 and 217:
Page 218 and 219:
Page 220 and 221:
Page 222 and 223:
Page 224 and 225:
Page 226 and 227:
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:
Page 234 and 235:
Page 236 and 237:
Page 238 and 239:
Page 240 and 241:
Page 242 and 243:
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:
Page 250 and 251:
Page 252 and 253:
Page 254 and 255:
Page 256 and 257:
Page 258 and 259:
Page 260 and 261:
Page 262 and 263:
Page 264 and 265:
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:
Page 272 and 273:
Page 274 and 275:
Page 276 and 277:
Page 278 and 279:
Page 280 and 281:
Page 282:
Page 285 and 286:
Page 287 and 288:
Page 289 and 290:
Page 291 and 292:
Page 293 and 294:
Page 295 and 296:
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:
Page 304 and 305:
Page 306 and 307:
Page 308 and 309:
Page 310 and 311:
Page 312 and 313:
Page 314:
Page 317 and 318:
Page 319 and 320:
Page 321 and 322:
Page 323 and 324:
Page 325 and 326:
Page 327 and 328:
Page 329 and 330:
Page 331 and 332:
Page 333 and 334:
Page 335 and 336:
Page 337 and 338:
Page 339 and 340:
Page 341 and 342:
Page 343 and 344:
Page 345 and 346:
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:
Page 354 and 355:
Page 356 and 357:
Page 358 and 359:
Page 360 and 361:
Page 362 and 363:
FIGURE 15.9 (Color Figure 15.9 foll
Page 364 and 365:
Page 366 and 367:
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:
Page 374 and 375:
TABLE 16.1 Examples of Transport of
Page 376 and 377:
Page 378 and 379:
Page 380 and 381:
CPP 2 Cargo or mRNA CAP Antisense A
Page 382 and 383:
Page 384:
Page 387 and 388:
Page 389 and 390:
Page 391 and 392:
Page 393 and 394:
Page 395 and 396:
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:
Page 404 and 405:
Page 406 and 407:
Page 408 and 409:
Page 410 and 411:
Page 412 and 413:
Page 414 and 415:
Page 416 and 417:
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
show all

crc press - E-Lib FK UWKS

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?