Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic L(i)K(j)(i=2j) peptides

Biochimica et Biophysica Acta - Biomembranes

Volumn 1416, Issue 1-2, 1999, Pages 176-194

  Castano, Sabine ^a   Desbat, Bernard ^b   Laguerre, Michel ^a   Dufourcq, Jean ^a  

^a CNRS   (France)

^b UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Helix at interface; Sheet at interface; Amphipathic peptide; Cytolytic peptide; FT IR spectroscopy; Lipid peptide interaction; Monolayer

Indexed keywords

ARTICLE; COMPUTER SIMULATION; CYTOLYSIS; HEMOLYSIS; IN VITRO STUDY; INFRARED SPECTROPHOTOMETRY; MODEL; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; THEORY;

AIR; AMINO ACID SEQUENCE; DANSYL COMPOUNDS; HEMOLYSIN PROTEINS; LIPIDS; MOLECULAR SEQUENCE DATA; PEPTIDES; PRESSURE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; WATER;

EID: 0032952095     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(98)00220-X     Document Type: Article

References (78)

1. R.M. Kini, H.J. Evans, Int. J. Peptide Protein Res. 34 (1989) 277-286.
2. W.F. De Grado, G.F. Musso, M. Lieber, E.T. Kaiser, F.J. Kézdy, Biophys. J. 37 (1982) 329-338.
3. M.T. Tosteson, S.J. Holmes, M. Razin, D.C. Tosteson, J. Membr. Biol. 87 (1985) 35-44.
4. C.E. Dempsey, Biochim. Biophys. Acta 1031 (1990) 143-161.
5. G. Colaccico, M.K. Basu, A.R. Buchelew, A.W.J. Berheimer, Biochim. Biophys. Acta 465 (1977) 378-390.
6. M. Bhakoo, T.H. Birkbeck, J.H. Freer, Biochemistry 21 (1982) 6883-6889.
7. G. Signor, S. Mammi, E. Peggion, H. Ringsdorf, A. Wagenknecht, Biochemistry 33 (1994) 6659-6670.
8. R. Maget-Dana, M. Ptak, Biophys. J. 73 (1997) 2527-2533.
9. L.K. Tamm, in: S. White (Ed.), Membrane Protein Structure, Oxford University Press, Oxford, 1994, pp. 283-313.
10. E. Schröder, K. Lübke, M. Lehmann, I. Beetz, Experientia 27 (1971) 764-765.
11. P. Bougis, H. Rochat, G. Piéroni, R. Verger, Biochemistry 20 (1981) 4915-4920.
12. P. Ash, R.C. Hider, A.A. Menez, A.G. Wunderer, Biochim. Biophys. Acta 669 (1981) 231-235.
13. M. Grandbois, J. Dufourcq, C. Salesse, Thin Solid Films 284 (1996) 743-747.
14. G. Saberwal, R. Nagaraj, Biochim. Biophys. Acta 1197 (1994) 109-131.
15. T. Kiyota, S. Lee, G.V. Sugihara, Biochemistry 35 (1996) 13196-13204.
16. I. Cornut, K. Büttner, J.L. Dasseux, J. Dufourcq, FEBS Lett. 349 (1994) 29-33.
17. I. Cornut, B. Desbat, J.M. Turlet, J. Dufourcq, Biophys. J. 70 (1996) 305-312.
18. M. Dathe, T. Wieprecht, H. Nikolenko, L. Handel, M.L. Maloy, D.L. Mc Donald, M. Beyerman, M. Bienert, FEBS Lett. 403 (1997) 208-212.
19. S. Castano, B. Desbat, I. Cornut, P. Méléard, J. Dufourcq, Lett. Peptide Sci. 4 (1997) 195-200.
20. G. Raghunathan, P. Seetharamulu, B.R. Brooks, H.R. Guy, Proteins 8 (1990) 213-225.
21. Y. Shai, Trends Biochem. Sci. 20 (1995) 460-464.
22. B. Bechinger, J. Membr. Biol. 156 (1997) 197-211.
23. B. Bechinger, M. Zasloff, S.J. Opella, Protein Sci. 2 (1993) 2077-2084.
24. K. Matsuzaki, O. Murase, H. Tokuda, S. Funakoshi, N. Fujii, K. Miyajima, Biochemistry 33 (1994) 3342-3349.
25. H. Vogel, F. Jähnig, V. Hofmann, J. Stümpel, Biochim. Biophys. Acta 733 (1983) 201-209.
26. J.W. Brauner, R. Mendelsohn, F.G. Prendergast, Biochemistry 26 (1987) 8151-8158.
27. Y.P. Zhang, R.N.A.H. Lewis, R.S. Hodges, R.N. McElhaney, Biophys. J. 68 (1995) 847-857.
28. R. Brasseur, J. Biol. Chem. 266 (1991) 16120-16127.
29. S. Frey, L.K. Tamm, Biophys. J. 60 (1991) 922-930.
30. R. Mendelsohn, J.W. Brauner, A. Gericke, Annu. Rev. Phys. Chem. 46 (1995) 305-334.
31. R.A. Dluhy, J. Phys. Chem. 90 (1986) 1373-1379.
32. C.R. Flack, J.W. Brauner, J.W. Taylor, R.C. Baldwin, R. Mendelsohn, Biophys. J. 67 (1994) 402-410.
33. A. Gericke, C.R. Flach, R. Mendelsohn, Biophys. J. 73 (1997) 492-499.
34. D. Blaudez, J.M. Turlet, J. Dufourcq, D. Bard, T. Buffeteau, B. Desbat, J. Chem. Soc. Faraday Trans. 92 (1996) 525-530.
35. B. Pastrana-Rios, S. Taneva, K.M.W. Keough, A.J. Mautone, R. Mendelsohn, Biophys. J. 69 (1995) 2531-2540.
36. M. Boncheva, H. Vogel, Biophys. J. 73 (1997) 1056-1072.
37. C.R. Flach, F.G. Prendergast, R. Mendelsohn, Biophys. J. 70 (1996) 539-546.
38. S. Castano, I. Cornut, K. Büttner, J.L. Dasseux, J. Dufourcq, Biochim. Biophys. Acta 1416 (1999) 161-175.
39. E. Perez-Paya, J. Dufourcq, L. Braco, C. Abad, Biochim. Biophys. Acta 1323 (1997) 223-236.
40. A.F. Mingotaud, C. Mingotaud, L.K. Patterson, Handbook of Monolayers, Vol. 2, Harcourt Brace Jovanovitch, San Diego, CA, 1992.
41. D. Blaudez, T. Buffeteau, J.C. Cornut, B. Desbat, N. Escafre, M. Pezolet, J.M. Turlet, Thin Solid Films 242 (1994) 146-150.
42. G. Sessa, J.H. Freer, G. Colacicco, G. Weismann, J. Biol. Chem. 244 (1969) 3575-3582.
43. V.S. Gevod, K.S. Birdi, Biophys. J. 45 (1984) 1079-1083.
44. T. Miyazawa, Infrared Spectra and Helical Conformations, Marcel Dekker, New York, 1967.
45. B. Pastrana, A.J. Mautone, R. Mendelsohn, Biochemistry 30 (1991) 10058-10064.
46. E. Goormaghtigh, V. Cabiaux, J.M. Ruysschaert, in: H.J. Hilderson, G.B. Ralston (Eds.), Subcellular Biochemistry: Physicochemical Methods in the Study of Biomembranes, Vol. 23, Plenum Press, New York, 1994, pp. 405-450.
47. F. Dousseau, M. Pezolet, Biochemistry 29 (1990) 8771-8779.
48. J.L.R. Arrondo, A. Muga, M.J. Castresana, F.M. Goni, Prog. Biophys. Mol. Biol. 59 (1993) 23-56.
49. P.H. Axelsen, B.K. Kaufman, R.N. MacElhaney, R.N.A.H. Lewis, Biophys. J. 69 (1995) 2770-2781.
50. E. Goormaghtigh, V. Cabiaux, J.M. Ruysschaert, Eur. J. Biochem. 193 (1990) 409-420.
51. W.K. Surewicz, T.M. Stepanick, A.G. Szabo, H.H. Mantsch, J. Biol. Chem. 263 (1988) 786-790.
52. W.K. Surewicz, H.H. Mantsch, D. Chapman, Biochemistry 32 (1993) 389-394.
53. S. Krimm, J. Bandekar, Adv. Protein Chem. 38 (1986) 181-364.
54. P.I. Haris, D. Chapman, Trends Biochem. Sci. 17 (1992) 328-333.
55. S.A. Tatulian, L.R. Jones, L.G. Reddy, D.L. Stokes, L.K. Tamm, Biochemislry 34 (1995) 4448-4456.
56. S. Krimm, W.C. Reisdorf, Faraday Discuss. 99 (1994) 181-197.
57. F.N. Fu, D.B. De Oliveira, W.R. Trumble, H.K. Sarkar, B.R. Singh, Appl. Spectrosc. 48 (1994) 1432-1441.
58. T. Buffeteau, B. Desbat, Appl. Spectrosc. 43 (1989) 1027-1032.
59. D. Marsh, Biophys. J. 72 (1997) 2710-2718.
60. R.A. Demel, W.S.M.G. van Kessel, R.F.A. Zwaal, B. Roelfsen, L.L.M. van Deenen, Biochim. Biophys. Acta 406 (1975) 97.
61. S.H. Portlock, Y. Lee, J. Tomich, L.K. Tamm, J. Biol. Chem. 267 (1992) 11017-11022.
62. E. Goormaghtigh, V. Cabiaux, J.M. Ruysschaert, in: H.J. Hilderson, G.B. Ralston (Eds.), Subcellular Biochemistry: Physicochemical Methods in the Study of Biomembranes, Vol. 23, Plenum Press, New York, 1994, pp. 363-403.
63. W.F. De Grado, J.D. Lear, J. Am. Chem. Soc. 107 (1985) 7684-7689.
64. J.H. Freer, T.H. Birkbeck, M. Bhakoo, in: J.E. Alouf (Ed.), Bacterial Protein Toxins, Academic Press, London, 1984, pp. 181-189.
65. D.J. Ciesla, D.E. Gilbert, J. Feigon, J. Am. Chem. Soc. 113 (1991) 3957-3961.
66. J. Dufourcq, W. Neri, N. Henry-Toulme, FEBS Lett. 421 (1998) 7-11.
67. M. Narita, Y. Tomotake, S. Isohawa, T. Matsuzawa, T. Miyauchi, Macromolecules 17 (1984) 1903-1906.
68. K.H. Altmann, A. Florsheimer, M. Mutter, Int. J. Peptide Protein Res. 27 (1986) 314-319.
69. S. Ono, S. Lee, H. Mihara, Y. Aoyagi, T. Kato, N. Yamasaki, Biochim. Biophys. Acta 1022 (1990) 237-244.
70. D. Eisenberg, R.M. Weiss, T.C. Terwilliger, Nature 299 (1982) 371-374.
71. K.E. Krebs, M.C. Phillips, FEBS Lett. 175 (1984) 263-266.
72. S.J. Opella, J. Gesell, B. Bechinger in: R.M. Epand (Ed.), The Amphipathic Helix, CRC Press, Boca Raton, FL, 1993, pp. 87-106.
73. R.E. Dickerson, I. Geis, The Structure and Action of Proteins, Harper and Row, New York, 1969.
74. J.A. Reynaud, J.P. Grivet, D. Sy, Y. Trudelle, Biochemistry 32 (1993) 4997-5008.
75. S.H. White, W.C. Winley, Curr. Opin. Struct. Biol. 4 (1994) 79-86.
76. T.E. Creighton, Proteins, Structure and Molecular Properties, W.H. Freeman and Company, New York, 1996.
77. B.H. Bull, K. Breese, Arch. Biochem. Biophys. 161 (1974) 665-670.
78. S.P. Ho, W.F. De Grado, J. Am. Chem. Soc. 109 (1987) 6751-6758.