Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 9, 2006, Pages 1483-1498

  Salditt, Tim ^a   Li, Chenghao ^a   Spaar, Alexander ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; MAGAININ 1;

ANTIMICROBIAL ACTIVITY; CONFORMATION; ENVIRONMENTAL FACTOR; LIPID MEMBRANE; LIQUID; METHODOLOGY; NEUTRON; PRIORITY JOURNAL; PROTEIN STRUCTURE; RADIATION SCATTERING; REVIEW; STRUCTURE ANALYSIS;

LIPIDS; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; X-RAYS;

EID: 33748940257     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.08.002     Document Type: Review

References (99)

1. Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156 (1997) 197-211
2. Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462 (1999) 157-183
3. Biggin P.C., and Sansom M.S. Interactions of α-helices with lipid bilayers: a review of simulation studies. Biophys. Chem. 76 (1999) 161-183
4. H.W. Huang, Action of antimicrobial peptides: two-state model. Biochemistry 39 8347.
5. Marsh D. Peptide models for membrane channels. Biochem. J. 315 (1996) 345-361
6. Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462 (1999) 1-10
7. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
8. Sitaram N., and Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity. Biochim. Biophys. Acta 1462 (1999) 29-54
9. Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1376 (1998) 391-400
10. Nagle J.F., and Tristram-Nagle S. Structure of lipid bilayers. Biochim. Biophys. Acta 1469 (2000) 159
11. White S.H., and Hristova K. Peptides in lipid bilayers: determination of location by absolute-scale X-ray refinement. In: Katsaras J., and Gutberlet T. (Eds). Lipid Bilayers: Structure and Interactions (2000), Springer Verlag
12. Hallock K.J., Wildmann K.H., Lee D.K., and Ramamoorthy A. An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies. Biophys. J. 82 (2002) 2499-2503
13. Ramamoorthy A., Thennarasu S., Lee D.K., Tan A., and Maloy L. Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide msi-843. Biophys. J. 91 (2006) 116-206
14. Hallock K.J., Lee D.K., and Ramamoorthy A. Msi-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84 (2003) 3052-3060
15. Losche M. Surface-sensitive X-ray and neutron scattering characterization of planar lipid model membranes and lipid/peptide interactions. Curr. Top. Membr. 52 (2002) 117
16. Seul M., and Sammon M.J. Preparation of surfactant multilayer films on solid substrates by deposition from organic solution. Thin Solid Films 185 (1990) 287
17. β phases in a hydrated phosphatidylcholine multimembrane. Phys. Rev. Lett. 60 (1988) 813
18. Mennicke U., and Salditt T. Preparation of solid-supported lipid bilayers by spin-coating. Langmuir 18 (2002) 8172
19. Cafiso D.S. Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 141-165
20. Kessel A., and Ben-Tal N. Energetics of peptide-membrane systems. In: Simon S.A., and McIntosh T.J. (Eds). Current Topics in Membranes (2002), Academic Press
21. Sansom M.S.P. Alamethicin and related peptaibols-Model ion channels. Eur. Biophys. J. 22 (1993) 105-124
22. Duclohier H., and Wroblewski H. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184 (2001) 1-12
23. Fox R.O., and Richards F.M. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution. Nature 300 (1982) 325-330
24. Aguilella V.M., and Bezrukov S.M. Alamethicin channel conductance modified by lipid charge. Eur. Biophys. J. 30 (2001) 233-241
25. Boheim G. Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol. 19 (1974) 277-303
26. Hall J.E. Voltage-dependent lipid flip-flop induced by alamethicin. Biophys. J. 33 (1981) 373-381
27. Schwarz G., and Savko P. Structural and dipolar properties of the voltage-dependent pore former alamethicin in octanol/dioxane. Biophys. J. 39 (1982) 211-219
28. Vodyanoy I., Hall J.E., and Balasubramanian T.M. Alamethicin-induced current-voltage curve asymmetry in lipid bilayers. Biophys. J. 42 (1983) 71-82
29. Woolley G.A., Biggin P.C., Schultz A., Lien L., Jaikaran D.C.J., Breed J., Crowhurst K., and Sansom M.S.P. Intrinsic rectification of ion flux in alamethicin channels: Studies with an alamethicin dimer. Biophys. J. 73 (1997) 770-778
30. Galaktionov S.G., and Marshall G.R. Effects of electric field on alamethicin bound at the lipid-water interface: a molecular mechanics study. Biophys. J. 65 (1993) 608-617
31. Jayasinghe S., Barrenger-Mathys M., Ellena J.F., Franklin C., and Cafiso D.S. Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesicles. Biophys. J. 74 (1998) 3023-3030
32. Kessel A., Cafiso D.S., and Ben-Tal N. Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects. Biophys. J. 78 (2000) 571-583
33. Kessel A., Schulten K., and Ben-Tal N. Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer. Biophys. J. 79 (2000) 2322-2330
34. Tieleman D.P., Sansom M.S.P., and Berendsen H.J.C. Alamethicin helices in a bilayer and in solution: molecular dynamics simulations. Biophys. J. 76 (1999) 40-49
35. Tieleman D.P., Berendsen H.J.C., and Sansom M.S.P. Surface binding of alamethicin stabilizes its helical structure: molecular dynamics simulations. Biophys. J. 76 (1999) 3186-3191
36. Baumann G., and Mueller P. A molecular model of membrane excitability. J. Supramol. Struct. 2 (1974) 538-557
37. Boheim G., Hanke W., and Jung G. Alamethicin pore formation: voltage-dependent flip-flop of α-helix dipoles. Biophys. Struct. Mech. 9 (1983) 181-191
38. Ehrenstein G., and Lecar H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10 (1977) 1-34
39. Cantor R.S. Size distribution of barrel-stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile. Biophys. J. 82 (2002) 2520-2525
40. He K., Ludtke S.J., Worcester D.L., and Huang H.W. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70 (1996) 2659-2666
41. Biggin P.C., Breed J., Son H.S., and Sansom M.S. Simulation studies of alamethicin-bilayer interactions. Biophys. J. 72 (1997) 627-636
42. La Rocca P., Biggin P.C., Tieleman D.P., and Sansom M.S.P. Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta 1462 (1999) 185-200
43. Tieleman D.P., Berendsen H.J.C., and Sansom M.S.P. Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces. Biophys. J. 80 (2001) 331-346
44. Tieleman D.P., Berendsen H.J.C., and Sansom M.S.P. An alamethicin channel in a lipid bilayer: molecular dynamics simulations. Biophys. J. 76 (1999) 1757-1769
45. Tieleman D.P., Hess B., and Sansom M.S.P. Analysis and evaluation of channel models: simulations of alamethicin. Biophys. J. 83 (2002) 2393-2407
46. T.A. Harroun, W.T. Heller, L. Yang, T.M. Weiss, H.W. Huang, Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis. Biophys. J., 77:2648
47. 15N solid state nuclear magnetic resonance. Biophys. J. 81 (2001) 1684-1698
48. B'éven L., Helluin O., Molle G., Duclohier H., and Wr'óblewski H. Correlation between anti-bacterial activity and pore sizes of two classes of voltage-dependent channel-forming peptides. Biochim. Biophys. Acta 1421 1 (1999) 53-63
49. Ionov R., El-Abed A., Angelova A., Goldmann M., and Peretti P. Asymmetrical ion-channel model inferred from two-dimensional crystallization of a peptide antibiotic. Biophys. J. 78 (2000) 3026-3035
50. He K., Ludtke S.J., Heller W.T., and Huang H.W. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71 (1996) 2669-2679
51. Woolley G.A., and Wallace B.A. Temperature dependence of the interaction of alamethicin helices in membranes. Biochemistry 32 (1993) 9819-9825
52. 13C-labelling of alamethicin, an ion-channel-forming peptide. Eur. J. Biochem. 243 (1997) 283-291
53. Zasloff M. Frog Skin peptides. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 5449
54. Wade D., Boman A., Wahlin B., Drain C.M., Andreu D., Boman H.G., and Merrifield R.B. All-D amino acid channel-forming antibiotic peptides. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 4761
55. T. Wieprecht, PhD Dissertation, Math-Naturwiss. Fakultät I Humboldt Universität Berlin.
56. Ludtke S., He J., Wu Y., and Huang H.W. Cooperative membrane insertation of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta 1190 (1994) 181-184
57. Ludtke S., He K., and Huang H.W. Membrane thinning caused by magainin 2. Biochemistry 34 (1995) 16764-16769
58. Ludtke S.J., He K., Heller W.T., Harroun T.A., Yang L., and Huang H.W. Membrane pores induced by magainin. Biochemistry 35 (1996) 13723-13728
59. Li C., Constantin D., and Salditt T. Biomimetic membranes of lipid-peptide model systems prepared on solid support. J. Phys. Cond. Mat. 16 (2004) S2439-S2453
60. Nagle J.F., and Katsaras J. Absence of a vestigial vapor pressure paradox. Phys. Rev., E 59 (1999) 7018
61. Vogel M., Münster C., Fenzl W., and Salditt T. Thermal unbinding of highly oriented phospholipid membranes. Phys. Rev. Lett. 84 (2000) 390
62. Pabst G., Katsaras J., and Raghunathan V.A. Enhancement of steric repulsion with temperature in oriented lipid multilayers. Phys. Rev. Lett. 88 (2002) 101-128
63. Brotons G., Salditt T., Dubois M., and Zemb Th. Highly oriented, charged multil-amellar membranes osmotically stressed by a polyelectrolyte of same sign. Langmuir 19 (2003) 8235-8244
64. Salditt T., Münster C., Lu J., Vogel M., Fenzl W., and Souvorov A. Specular and diffuse scattering of highly aligned phospholipid membranes. Phys. Rev., E 60 (1999) 7285
65. Spaar A., and Salditt T. Short range order of hydrocarbon chains in fluid phospholipid bilayers studied by X-ray diffraction from highly oriented membranes. Biophys. J. 85 (2003) 1576-1584
66. C. Li, Strukturanalyse von Antibiotischen Peptides in Lipidmembranen mittels Rontgenreflektivitat. PhD Dissertation, Goerg-August-Universität Göttingen, 2005.
67. Salditt T., Li C., Spaar A., and Mennicke U. X-ray reflectivity of solid-supported multilamellar membranes. Eur. Phys. J., E 7 (2002) 105
68. Constantin D., Mennicke U., Li C., and Salditt T. Solid-supported lipid bilayers: structure factor and fluctuations. Eur. Phys. J., E 12 (2003) 283-290
69. Blaurock A.E. Evidence of bilayer structure and of membrane. Biochem. Biophys. Acta 650 (1982) 167
70. Katsaras J. X-ray diffraction studies of oriented lipid bilayers. Biochem. Cell Biol. 73 (1995) 209
71. U. Mennicke, Struktur und Fluktuationen festkörpergestützter Phospholipidmembranen. Dissertation Universität Göttingen, (2003).
72. Mecke A., Lee D.K., Ramamoorthy A., Orr B.G., and Banaszak Holl M.M. Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of msi-78 in lipid bilayers. Biophys. J. 89 (2005) 4043-4050
73. Lei N., Safinya C.R., and Bruinsma R. Discrete harmonic model for stacked membranes: theory and experiment. J. Phys. II France 5 (1995) 1155
74. Y. Lyatskaya, Y. Liu, S. Tristram-Nagle, J. Katsaras, and J.F. Nagle, Method for obtaining structure and interactions from oriented lipid bilayers. Phys. Rev. E., 63 011907.
75. T. Salditt, M. Vogel, W. Fenzl, Thermal fluctuations and positional correlations in oriented lipid membranes. Phys. Rev. Lett. 90 (2003) 178101.
76. Brotons G., Constantin D., Madsen A., and Salditt T. Physica B 357 (2005) 61-65
77. C. Münster, Antibiotische Peptide in Phospholipiden: Strukturuntersuchungen mit Beugungsmethoden. PhD Dissertation, Sektion Physik, Ludwig-Maximilians-Universität München.
78. Münster C., Salditt T., Vogel M., and Peisl J. Nonspecular neutron scattering from highly aligned membranes. Europhys. Lett. 46 (1999) 486
79. Münster M., Spaar A., Bechinger B., and Salditt T. Magainin 2 in phospholipid bilayers: peptide orientation and lipid chain ordering studied by X-ray diffraction. Biochim. Biophys. Acta 1562 (2002) 37
80. May S. Theories on structural perturbations of lipid bilayers. Curr. Opin. Colloid Interface Sci. 5 (2000) 244
81. Z. Khattari, G. Brotons, M. Akkawi, A. Arbely, I.T. Arkin, and T.T. Salditt. Biophys. J 90 (6) (2006) 2038--2050.
82. C. Münster, J. Lu, S. Schinzel, B. Bechinger, and T. Salditt, Grazing incidence X-ray diffraction of highly aligned phospholipid membranes containing antimicrobial peptides magainin2. Biophy. Lett./Europ. Biophys. J. 28 683.
83. Heller H., Schaeffer M., and Schulten K. Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid-crystal phases. J. Phys. Chem. 97 (1993) 8343
84. Rheinstädter M.C., Ollinger C., Fragneto G., Demmel F., and Salditt T. Phys. Rev. Lett. 93 (2004) 107-108
85. Müller J., Münster C., and Salditt T. Thermal denaturing of bacteriorhodopsin by X-ray scattering from oriented purple membranes. Biophys. J. 78 (2000) 3208
86. Chen F.-Y., Lee M.-T., and Huang H.W. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82 (2002) 908
87. Heller W.T., Harroun T.A., Yang L., Ludtke S.J., He K., and Huang H.W. Membrane pores induced by magainin. Biochemistry 35 (1996) 13723
88. Heller W.T., Waring A.J., Lehrer R.I., Harroun T.A., Weiss T.M., Yang L., and Huang H.W. Membrane thinning effect of the β-sheet antimicrobial protegrin. Biochemistry 39 (2000) 139
89. Harroun T.A., Heller W.T., Weiss T.M., Yang L., and Huang H.W. Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin. Biophys. J. 76 (1999) 937-945
90. Weiss T.M., van der Wel P.C.A., Killian J.A., Koeppe R.E., and Huang H.W. Hydrophobic mismatch between helices and lipid bilayers. Biophys. J. 84 (2003) 379
91. Spaar A., Münster C., and Salditt T. Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering. Biophys. J. 87 (2004) 396-407
92. P. La Rocca, P.C. Biggin, D.P. Tielemann, M.S.P. Sansom, Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta, 1462:185.
93. Yang L., Harroun T.A., Heller W.T., Weiss T.M., and Huang H.W. Neutron off-plane scattering of aligned membranes: I. method of measurement. Biophys. J. 75 (1998) 641
94. Yang L., Weiss T.M., Lehrer R.I., and Huang H.W. Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys. J. 79 (2000) 2002-2009
95. A. Spaar, The structure of lipid membranes and the conformation of peptides in membranes studied by surface X-ray scattering. Dissertation thesis, Universität des Saarlan-des (2003).
96. Koltover I., Rädler J.O., Salditt T., and Safinya C.R. Phase behavior and interactions of the membrane-protein bacteriorhodopsin. Phys. Rev. Lett. 82 (1999) 3184
97. Chen S.H., Liao C.Y., Huang H.W., Weiss T.M., Bellisent-Funel M.C., and Sette F. Collective dynamics in fully hydrated phospholipid bilayers studied by inelastic X-ray scattering. Phys. Rev. Lett. 86 (2001) 740
98. Tarek M., Tobias D.J., Chen S.H., and Klein M.L. Short wavelength collective dynamics in phospholipid bilayers: a molecular dynamics study. Phys. Rev. Lett. 87 (2001) 101-238
99. H. Leontiadou, A.E. Mark, S.J. Marrink, Antimicrobial peptides in action, J. Am. Chem. Soc. (in press).