Orientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay

Biophysical Journal

Volumn 76, Issue 4, 1999, Pages 2121-2141

  Nicol, François ^a,b   Nir, Shlomo ^c   Szoka Jr , Francis C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b CNRS   (France)

^c HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AVIDIN; BIOTIN; LIPOSOME; PEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BILAYER MEMBRANE; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CONFORMATIONAL TRANSITION; FLUORESCENCE; PEPTIDE ANALYSIS; PHOSPHOLIPID VESICLE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

EID: 0033058273     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77368-6     Document Type: Article

References (59)

1. Barranger-Mathys, M., and D. S. Cafiso. 1996. Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling. Biochemistry. 35:498-505.
2. Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
3. Batenburg, A. M., and B. de Kruijff. 1988. Modulation of membrane surface curvature by peptide-lipid interactions. Biosci. Rep. 8:299-307.
4. Bechinger, B., Y. Kim, L. E. Chirlian, J. Gesell, J. M. Neumann, M. Motal, J. Tomich, M. Zasloff, and S. J. Opella. 1991. Orientation of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy. J. Biol. NMR. 1:167-173.
5. Benachir, T., and M. Lafleur. 1995. Study of vesicle leakage induced by melittin. Biochim. Biophys. Acta. 1235:452-460.
6. Bentz, J., and S. Nir. 1981. Aggregation of colloidal particles modeled as a dynamical process. Proc. Natl. Acad. Sci. USA. 78:1634-1637.
7. Biwersi, J., N. Emans, and A. S. Verkman. 1996. Cystic fibrosis transmembrane conductance regulator activation stimulates endosome fusion in vivo. Proc. Natl. Acad. Sci. USA. 93:12484-12489.
8. Blatz, P. J., and A. V. Toblosky. 1945. Note on kinetics of virus-cell aggregation and fusion. Biophys. J. 49:77-80.
9. Boman, H. G. 1994. Antimicrobial peptides. Chairman's opening remarks. Ciba Foundation Symposium. 186:1-4.
10. Brachais, L., H. Duclohier, C. Mayer, D. Davoust, and G. Molle. 1995. Influence of proline-14 substitution on the secondary structure in a synthetic analogue of alamethicin. Biopolymers. 36:547-558.
11. Cafiso, D. S. 1994. Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Ann. Rev. Biophys. Biomol. Struct. 23: 141-165.
12. Cornut, I., E. Thiaudière, and J. Dufourcq. 1993. The amphipathic helix in cytotoxic peptides. In The Amphipathic Helix. R. M. Epand, editor. CRC Press, Boca Raton, FL. 173-219.
13. De Grado, W. F., Z. R. Wasserman, and J. D. Lear. 1989. Protein design, a minimalist approach. Science. 243:622-628
14. Ellens, H., J. Bentz, and F. C. Szoka, Jr. 1984. pH-induced destabilization of phosphatidylethanolamine-containing liposomes: role of bilayer contact. Biochemistry. 23:1532-1538.
15. Emans, N., J. Biwersi, and A. S. Verkman. 1995. Imaging of endosome fusion in BHK fibroblasts based on a novel fluorimetric avidin-biotin binding assay. Biophys. J. 69:716-728.
16. Epand, R. M., Y. Shai, J. P. Segrest, and G. M. Anantharamaiah. 1995. Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers. 37:319-338.
17. Fattal, E., S. Nir, P. A. Parente, and F. C. Szoka, Jr. 1994. Pore forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry. 33:6721-6731.
18. Gazit, E., A. Boman, H. G. Boman, and Y. Shai. 1995. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry. 34:11479-11488.
19. Goormaghtigh, E., J. De Meutter, F. C. Szoka, Jr., V. Cabiaux, R. A. Parente, and J. M. Ruysschaert. 1991. Secondary structure and orientation of the amphipathic peptide GALA in lipid structures. An infrared-spectroscopic approach. Eur. J. Biochem. 195:421-429.
20. He, K., S. J. Ludtke, D. L. Worcester, and H. W. Huang. 1995. Antimicrobial peptide pores detected by neutron in-plane scattering. Biochemistry. 34:15614-15618.
21. He, K., S. J. Ludtke, D. L. Worcester, and H. W. Huang. 1996. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70:2659-2666.
22. Hillenkamp, F., M. Karas, R. Beavis, and B. T. Chait. 1991. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 63:1193A-1203A.
23. Kaduk, C., H. Duclohier, M. Dathe, H. Wenschuh, M. Beyermann, G. Molle, and M. Bienert. 1997. Influence of proline position upon the ion channel activity of alamethicin. Biophys. J. 72:2151-2159.
24. Karolin, J., L. B. A. Johansson, L. Standberg, and T. Ny. 1994. Fluorescence and adsorption spectroscopic properties of dipyrrometheneboron difluoride (BODIPY) derivatives in liquids, lipid membranes, and proteins. J. Am. Chem. Soc. 116:7801-7806.
25. Lear, J. D., Wasserman, Z. R., and DeGrado, W. F. 1988. Synthetic amphipathic peptide models for protein ion channels. Science. 240: 1177-1181.
26. Ludtke, S. J., K. S. He, Y. Wu, and H. W. Huang. 1994. Cooperative membrane insertion of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta. 1190:181-184.
27. Ludtke, S. J., K. S. He, W. T. Heller, T. A. Harroun, L. Yang, and H. W. Huang. 1996. Membrane pores induced by magainin. Biochemistry. 35:13723-13728.
28. Lúneberg, J., I. Martin, F. Núbler, J. M. Ruysschaert, and A. Herrmann. 1995. Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:27606-27614.
29. Matsuzaki, K., O. Murase, H. Toduka, S. Funakoshi, N. Fujii, and K. Miyajima. 1994. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry. 33:3342-3349.
30. Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemists. 34:12553-12559.
31. Matsuzaki, K., S. Yoneyama, O. Murase, and K. Miyajima. 1996. Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry. 35:8450-8456.
32. Matsuzaki, K., S. Yoneyama, and K. Miyajima. 1997a. Pore formation and translocation by melittin. Biophys. J. 73:831-838.
33. Matsuzaki, K., A. Nakamura, O. Murase, K. Sugishita, N. Fujii, and K. Miyajima. 1997b. Modulation of magainin 2-lipid bilayer interactions by peptide charge. Biochemistry. 36:2104-2111.
34. Nicol, F., S. Nir, and F. C. Szoka, Jr. 1996. Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH sensitive peptide. Biophys. J. 71:3288-3301.
35. Nir, S., J. Bentz, J. Wilschut, and N. Düzgünes. 1983. Aggregation and fusion of phospholipid vesicles. Prog. Surf. Sci. 13:1-124.
36. Nir, S., R. Peled, and K. Lee. 1994. Analysis of particle uptake by cells: binding to several receptors, equilibration time, endocytosis. Colloids Surf. 89:45-57.
37. Parente, R. A., S. Nir, and F. C. Szoka, Jr. 1988. pH-dependent fusion of phosphatidylcholine small vesicles. Induction by a synthetic amphipathic peptide. J. Biol. Chem. 263:4724-4730
38. Parente, R. A., S. Nir, and F. C. Szoka, Jr. 1990a. Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA. Biochemistry. 29: 8720-8728.
39. Parente, R. A., Nadasdi L., N. K. Subbarao, and F. C. Szoka, Jr. 1990b. Association of a pH-sensitive peptide with membrane vesicles: role of amino acid sequence. Biochemistry. 29:8713-8719.
40. Pugliese, L., A. Coda, M. Malcovati, and M. Bolognesi. 1993. Three dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution. J. Mol. Biol. 231:698-710.
41. Qiu, X.-Q., K. S. Jakes, A. Finkelstein, and S. L. Slatin. 1994. Site-directed biotinylation of colicin Ia. J. Biol. Chem., 269:7483-7488.
42. Qiu, X.-Q., K. S. Jakes, P. K. Kienker, A. Finkelstein, and S. L. Slatin. 1996. Major transmembrane movement associated with colicin Ia channel gating. J. Gen. Physiol. 107:313-328.
43. Rapaport, D., R. Peled, S. Nir, and Y. Shai. 1996. Reversible surface aggregation in pore formation by pardaxin. Biophys. J. 70:2502-2512.
44. Rex, S. and G. Schwarz. 1998. Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles. Biochemistry. 37:2336-2345.
45. Sansom, M. S. P. 1991. The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55:139-235.
46. Schwarz, G., and A. Arbuzova. 1995. Pore kinetics reflected in the dequenching of a lipid vesicle entrapped fluorescent dye. Biochim. Biophys. Acta. 1239:51-57.
47. Shai, Y. 1994. Pardaxin: channel formation by a shark repellent peptide from fish. Toxicology. 87:109-129.
48. Slatin, S. L., X.-Q. Qiu, K. S. Jakes, and A. Finkelstein. 1994. Identification of a translocated protein segment in a voltage-dependent channel. Nature. 371:158-161.
49. Smith, R., F. Separovic, T. J. Milne, A. Whittaker, F. Bennett, B. A. Cornell, and A. Makriyannis. 1994. Structure and orientation of the pore-forming peptide, melittin, in lipid bilayers. J. Mol. Biol. 241: 456-466.
50. Smoluchowski. 1917. Versuch einer mathematischen Theorie der Koagulations kinetik Koloider Losungen. Z. Phys. Chem. Stochiom. Verv.. 92:129-168.
51. Spach, G., Merle, Y., and Molle, G. 1985. Peptides amphiphiles et canaux transmembranes. J. Chim. Phys. 82:719.
52. Subbarao, N. K., R. A. Parente, F. C. Szoka, Jr., L. Nadasdi, and K. Pongracz. 1987. pH-dependent bilayer destabilization by an amphipathic peptide. Biochemistry. 26:2964-2972.
53. Subbarao, N. K., C. J. Fielding, R. L. Hamilton, and F. C. Szoka, Jr. 1988. Lecithin:cholesterol acyltransferase activation by synthetic amphipathic peptides. Proteins 3:187-198.
54. Szoka, F. C., Jr., and D. Papahadjopoulos. 1978. Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation. Proc. Natl. Acad. Sci. USA. 75:4194-4198.
55. Terwilliger, T. C., L. Weissman, and D. Eisenberg. 1982. The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities. Biophys. J. 37:353-361.
56. Tomich, J. M. 1993. Amphipathic helices in channel-forming structures. In The Amphipathic Helix. R. M. Epand. editor. CRC Press, Boca Raton. FL. 221-254.
57. Tytler, E. M., J. P. Segrest, R. M. Epand, S. Q. Nie, R. F. Epand, V. K. Mishra, Y. V. Venkatachalapathi, and G. M. Anantharamaiah. 1993. Reciprocal effects of alipoprotein and lytic peptide analogs on membranes. Cross-sectional molecular shapes of amphipathic alpha helices control membrane stability. J. Biol. Chem. 268:22112-22118.
58. Vogel, H., and F. Jahnig. 1986. The structure of melittin in membranes. Biophys. J. 50:573-582.
59. Wu, Y., H. W. Huang, and G. A. Olah. 1990. Method of oriented circular dichroism. Biophys. J. 57:797-806.