Structure Prediction of CPPs and Iterative Development of Novel CPPs 219 ACKNOWLEDGMENTS Olivier Bouffioux has been supported by the Ministère de la Région Wallonne, contract # 97/13649. Frédéric Basyn thanks the National Funds for Scientific Research of Belgium (FNRS) (Télévie) for financial support. René Rezsohazy is postdoctoral researcher at the National Funds for Scientific Research of Belgium. Robert Brasseur is research director at the National Funds for Scientific Research of Belgium. This work was supported by the European Community biotech contract BIO4-98-0227 and by the Interuniversity Poles of Attraction Program — Belgian State, Prime Minister’s Office — Federal Office for Scientific, Technical, and Cultural Affairs PAI contract # P4/03. REFERENCES 1. Banerjee–Basu, S., Ryan, J.F., and Baxevanis, A.D., The homeodomain resource: a prototype database for a large protein family, Nucleic Acids Res., 28, 329, 2000. 2. Krumlauf, R., Hox genes in vertebrate development, Cell, 78, 191, 1994. 3. Wolberger, C., Homeodomain interactions, Curr. Opin. Struct. Biol., 6, 62, 1996. 4. Passner, J.M. et al., Structure of a DNA-bound ultrabithorax-extradenticle homeodomain complex, Nature, 397, 714, 1999. 5. Piper, D.E. et al., Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation, Cell, 96, 587, 1999. 6. Niessing, D. et al., Homeodomain position 54 specifies transcriptional vs. translational control by Bicoid, Mol. Cell, 5, 395, 2000. 7. Schnabel, C.A. and Abate–Shen, C., Re<strong>press</strong>ion by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues, Mol. Cell Biol., 16, 2678, 1996. 8. Zhang, H., Catron, K.M., and Abate–Shen, C., A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional re<strong>press</strong>ion, Proc. Natl. Acad. Sci. U.S.A., 93, 1764, 1996. 9. Zhang, N. et al., Three distinct domains in the HOX-11 homeobox oncoprotein are required for optimal transactivation, Oncogene, 13, 1781, 1996. 10. Kim, Y.H. et al., Homeodomain-interacting protein kinases, a novel family of core<strong>press</strong>ors for homeodomain transcription factors, J. Biol. Chem, 273, 25875, 1998. 11. Li, X., Murre, C., and McGinnis, W., Activity regulation of a Hox protein and a role for the homeodomain in inhibiting transcriptional activation, EMBO J., 18, 198, 1999. 12. Zappavigna, V. et al., HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation, EMBO J., 15, 4981, 1996. 13. Zappavigna, V., Sartori, D., and Mavilio, F., Specificity of HOX protein function depends on DNA–protein and protein–protein interactions, both mediated by the homeodomain, Genes Dev., 8, 732, 1994. 14. Ohneda, K. et al., The homeodomain of PDX-1 mediates multiple protein–protein interactions in the formation of a transcriptional activation complex on the insulin promoter, Mol. Cell Biol., 20, 900, 2000. 15. Zhang, H. et al., Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism, Mol. Cell Biol., 17, 2920, 1997.
220 Cell-Penetrating Peptides: Processes and Applications 16. Le Roux, I. et al., Neurotrophic activity of the Antennapedia homeodomain depends on its specific DNA-binding properties, Proc. Natl. Acad. Sci. U.S.A., 90, 9120, 1993. 17. Derossi, D. et al., The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem, 269, 10444, 1994. 18. Joliot, A. et al., Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein, Curr. Biol., 8, 856, 1998. 19. Maizel, A. et al., A short region of its homeodomain is necessary for Engrailed nuclear export and secretion, Development, 126, 3183, 1999. 20. Chatelin, L. et al., Transcription factor hoxa-5 is taken up by cells in culture and conveyed to their nuclei, Mech. Dev., 55, 111, 1996. 21. Prochiantz, A., Messenger proteins: homeoproteins, TAT and others, Curr. Opin. Cell Biol., 12, 400, 2000. 22. Derossi, D. et al., Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent, J. Biol. Chem, 271, 18188, 1996. 23. 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. 24. Drin, G. et al., Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity, Eur. J. Biochem., 268, 1304, 2001. 25. Scheller, A. et al., Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides, Eur. J. Biochem., 267, 6043, 2000. 26. Pooga, M. et al., Cell penetration by transportan, FASEB J., 12, 67, 1998. 27. Pooga, M. et al., Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo, Nat. Biotechnol., 16, 857, 1998. 28. Prochiantz, A., Getting hydrophilic compounds into cells: lessons from homeopeptides, Curr. Opin. Neurobiol., 6, 629, 1996. 29. Schwarze, S.R., Hruska, K.A., and Dowdy, S.F., Protein transduction: unrestricted delivery into all cells? Trends Cell Biol., 10, 290, 2000. 30. Williams, E.J. et al., Selective inhibition of growth factor-stimulated mitogenesis by a cell-permeable Grb2-binding peptide, J. Biol. Chem, 272, 22349, 1997. 31. Ducarme, P., Rahman, M., and Brasseur, R., IMPALA: a simple restraint field to simulate the biological membrane in molecular structure studies, Proteins, 30, 357, 1998. 32. La Rocca, P., Shai, Y., and Sansom, M.S., Peptide-bilayer interactions: simulations of dermaseptin B, an antimicrobial peptide, Biophys. Chem., 76, 145, 1999. 33. Vogt, B. et al., The topology of lysine-containing amphipathic peptides in bilayers by circular dichroism, solid-state NMR, and molecular modeling, Biophys. J., 79, 2644, 2000. 34. Lins, L. and Brasseur, R., The hydrophobic effect in protein folding, FASEB J., 9, 535, 1995. 35. Basyn, F. et al., Prediction of membrane protein orientation in lipid bilayer: a theoretical approach, J. Mol. Graph. Model., 20, 235, 2001. 36. Wiener, M.C. and White, S.H., Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure, Biophys. J., 61, 437, 1992. 37. Bradshaw, J.P. et al., Oblique membrane insertion of viral fusion peptide probed by neutron diffraction, Biochemistry, 39, 6581, 2000. 38. Saiz, L. and Klein, M.L., Structural properties of a highly polyunsaturated lipid bilayer from molecular dynamics simulations, Biophys. J., 81, 204, 2001.
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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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Transportans 55 Indeed, galparan is
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Transportans 65 antibiotin antibodi
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Model Amphipathic Peptides 73 its D
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Cell-Penetrating Peptide Conjugatio
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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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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