Metal ion modulation of membrane permeability induced by a polypetide template

Journal of the American Chemical Society

Volumn 118, Issue 10, 1996, Pages 2505-2506

  Scrimin, Paolo ^a   Veronese, Andrea ^b   Tecilla, Paolo ^b   Tonellato, Umberto ^b   Monaco, Vania ^b   Formaggio, Fernando ^b   Crisma, Marco ^b   Toniolo, Claudio ^b  

^a UNIVERSITY OF TRIESTE   (Italy)

^b UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE;

ARTICLE; MEMBRANE BINDING; MEMBRANE PERMEABILITY; MODULATION;

EID: 0029998658     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9536173     Document Type: Article

References (41)

1. (a) Jaenicke, R. Ed. Protein Folding; Elsevier: Amsterdam. 1980.
2. (b) Creighton, T. E. Proteins - Structure and Molecular Properties; Freeman: New York, 1984.
3. (c) Montelione, G. T.; Scheraga, H. A. Acc. Chem. Res. 1989, 22, 70.
4. (a) Mutter, M.; Vuilleumier, S. Angew. Chem., Int. Ed. Engl. 1989, 28, 535.
5. (b) DeGrado, W. F.; Wasserman. Z. A.; Lear, J. D. Science 1989, 243, 622.
6. Mutter, M.; Tuchscherer, G. G.; Miller, C.; Altmann, K.-H.; Carey, R. I.; Wyss, D. F.; Labhardt, A. M.; Rivier, J. E. J. Am. Chem. Soc. 1992, 114, 1463.
7. (a) Ghadiri, M. R.; Fernholz, A. K. J. Am. Chem. Soc. 1990, 112, 9633.
8. (b) Ghadiri, M, R.; Soares, C.; Choi, C. J. Am. Chem. Soc. 1992, 114, 825.
9. (c) Ghadiri, M. R.; Soares, C.; Choi, C. J. Am. Chem. Soc. 1992, 114,4000.
10. Handel, T. M.; Williams, S. A.; DeGrado, W. F. Science 1993, 261, 879.
11. (a) Åkerfeldt, K. S.; Lear, J. D.; Wasserman, Z. R.; Chung, L. A.; DeGrado, W. F. Acc. Chem. Res. 1993, 26, 191.
12. (b) Stankovic, C. J.; Schreiber, S. L. Chemtracts: Org. Chem. 1991, 4, 1.
13. (c) Sansom, M. S. P. Prog. Biophys. Mol. Biol. 1991, 55, 139.
14. (d) Montai, M. Curr. Opin. Struct. Biol. 1995, 5, 501.
15. (e) Akerfeldt, K. S.; Kim, R. M.; Camac. D.; Groves, J. T.; Lear, J. D.; DeGrado, W. F. J. Am. Chem. Soc. 1992, 114, 9656.
16. (f) Grove, A.; Mutter, M.; Rivier, J. E.; Montai, M. J. Am. Chem. Soc. 1993, 115, 5919.
17. (g) Sasaki, T.; Kaiser, E. T. J. Am. Chem. Soc. 1989, 111, 380.
18. Stankovic, C. J.; Heinemann, S. H.; Delfino, J. M.; Sigworth, F. J.; Schreiber, S. L. Science 1989, 244, 813.
19. (a) Oiki, S.; Danho, W.; Montai, M. Proc. Nail. Acad. Sci. U.S.A. 1988, 85, 2393.
20. (b) Tosteson, M. T.; Auld, D. S.; Tosteson. D. C. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 707.
21. Benedetti, E.; Bavoso, A.; Di Blasio, B.; Pavone, V.; Pedone, C.; Toniolo, C.; Bonora, G. M. Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 7951.
22. (a) Pandey, R. C.; Cook, J. C., Jr.; Rinehart, K. L. J. Am. Chem. Soc. 1977, 99, 8469.
23. (b) Fox, R. O.; Richards, F. M. Nature 1982, 300, 325.
24. (a) Auvin-Guette, C.; Rebuffat, S.; Prigent, Y.; Bodo, B. J. Am. Chem. Soc. 1992. 114, 2170.
25. (b) Gurunath, R.; Balaram, P. Biopolymers 1995, 35, 21.
26. (c) Toniolo, C.; Peggion, C.; Crisma, M.; Formaggio, F.; Shui, X.; Eggleston, D. S. Nature Struct. Biol. 1994, 1, 908.
27. (a) Fujita, T.; Wada, S.; Iida, A.; Nishimura, T.; Kanai, M.; Toyama, N. Chem. Pharm. Bull. 1994, 42, 489.
28. (b) Monaco, V.; Formaggio, F.; Crisma, M.; Toniolo, C.; Shui, X.; Eggleston, D. S. Biopolymers, in press.
29. Le Doan, T.; El Hajji, M.; Rebuffat, S.; Rajesvari, M. R.; Bodo, B. Biochim. Biophys. Acta 1986, 858, 1.
30. Solution synthesis and characterization of the peptides discussed in this work are reported in the following: Toniolo, C.; Crisma, M.; Formaggio, F.; Peggion, C.; Monaco, V.; Goulard, C.; Rebuffat, S.; Bodo, B., in preparation.
31. All new compounds have been fully characterized: synthetic procedures and analytical data are in the supporting information.
32. Pirrone, L. Chemistry Degree Master Thesis, Department of Organic Chemistry, University of Padova, Padova, Italy, 1991.
33. Bodo, B.; Rebuffat, S.; Goulard, C.; Peggion, C.; Monaco, V.; Formaggio, F.; Crisma, M.; Toniolo, C. In Peptides 1994: Maia, H. L. S., Ed.; ESCOM: Leiden. 1995: p 749.
34. Prince, R. H. In Comprehensive Coordination Chemistry: Wilkinson, G., Gillard, R. D., McCleverty, A., Eds.; Pergamon Press: London. 1987: pp 937-938.
35. Scrimin, P.; Tecilla, P.; Tonellato, U.; Valle, G.; Veronese, A. J. Chem. Soc., Chem. Commun. 1995, 1163.
36. exc = 520 nm. Experiments were started by addition of the peptide as a methanolic solution, and the maximum amount of solvent added was 1.5% (v/v). Control experiments showed that this amount of methanol did not affect vesicles permeability. 100% CF content was determined by complete vesicles disruption with excess Triton X100.
37. Vesicles were prepared by sonication, and their size was analyzed by dynamic light scattering. Details are given in the supporting information.
38. -7 M), a discrete population of unbound peptide starts to form, suggesting an equilibrium between membrane-bound and unbound peptide.
39. -7 M, aggregates begin to form, as revealed by the increase of scattered light above these concentrations. These two concentrations may be taken as a rough estimate of the hydrophobicity of the two systems, which are very similar. This is hardly surprising, since 1 is triprotonated at pH = 7.4.
40. Similar results have been obtained connecting together two undecapeptides with the same sequence of trichogin via a succinimidoyl spacer (see ref 14).
41. CF release kinetics are not first order. This has been observed for alamethicin, too: Schwarz, G.; Robert, C. H. Biophys. J. 1990, 58, 577.