Influence of the secondary structure on the pore forming properties of synthetic alamethicin analogs: NMR and molecular modelling studies

Journal of Peptide Science

Volumn 4, Issue 5, 1998, Pages 344-354

  Brachais, Laurent ^a   Mayer, Catherine ^b   Davoust, Daniel ^b   Molle, Gérard ^a,c  

^a UNIVERSITÉ DE ROUEN   (France)

^b INSA   (France)

^c Normandie Université   (France)

Author keywords

Amphipathicity: helices; Bilayers; Ion channels; SDS micelles

Indexed keywords

ALAMETHICIN; DRUG DERIVATIVE; PORIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

ALAMETHICIN; AMINO ACID SEQUENCE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PORINS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0032132970     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199808)4:5<344::AID-PSC152>3.0.CO;2-A     Document Type: Article

References (42)

1. C.E. Meyer and F. Ruesser (1967). A polypeptide antibacterial agent Isolated from Trichoderma viride. Experientia 23, 85-86.
2. G. Boheim (1974). Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol. 19, 277-303.
3. M.S.P. Sansom (1993). Alamethicin and related peptaibols. Eur. Biophys. J. 22, 105-124.
4. J.E. Hall and I. Vodyanoy (1984). Alamethicin: a rich model for channel behavior. Biophys. J. 45, 233-247.
5. W. Hanke and G. Boheim (1980). The lowest conductance state of the alamethicin pore. Biochim. Biophys. Acta 596, 456-462.
6. L.G.M. Gordon and D.A. Haydon (1975). Potential-dependent conductances in lipid membranes containing alamethicin. Phil. Trans. R. Soc. London B 270, 433-447.
7. I. Vodyanoy, J.E. Hall and T.M. Balasubramanian (1983). Alamethicin-induced current-voltage curve asymmetry in lipid bilayers. Biophys. J. 42, 71-82.
8. G. Boheim, W. Hanke and G. Jung (1983). Alamethicin pore formation: voltage dependent flip-flop of a-helix dipoles. Biophys. Struct. Mech. 9, 181-191.
9. D.S. Cafiso (1994). Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Ann. Rev. Biomolec. Struct. 23, 141-165.
10. M.S.P. Sansom (1993). Alamethicin and related peptaibols-model ion channels. Q. Rev. Biophys. 26, 365-421.
11. R.O. Fox and F.M. Richards (1982). A voltage-gated ion channels model inferred from the crystal structure of alamethicin. Nature 300, 325-330.
12. G. Molle, H. Duclohier, J.-Y. Dugast and G. Spach (1989). Design and conformation of non-Aib synthetic peptides enjoying alamethicin-like ionophore activity. Biopolymers 28, 273-283.
13. G. Spach, H. Duclohier and G. Molle. Modulation of ionophore properties by chemical modifications of alamethicin synthetic analogues, in: Transport through Membranes: Carriers. Channels and pumps - The 21st Jerusalem Symposium in Quantum Chemistry and Biochemistry, A. Pullman, B. Pullman and P. Jortner, Eds., p. 67-76, D. Reidel Publishing, Amsterdam, 1988.
14. G. Molle, H. Duclohier, S. Julien and G. Spach (1991). Synthetic analogues of alamethicin: effect of C-terminal residue substitutions and chain lenght on the ion channel lifetimes. Biochim. Biophys. Acta 1064, 365-369.
15. G. Molle, H. Duclohier, J.-Y. Dugast and G. Spach. Influence of helix-helix contact on the stability of ion channels induced by a synthetic analogue of alamethicin, in: Peptides 1992. C. H. Schneider and A. N. Eberle (Eds.), p. 917-918, ESCOM Science Publishers B.V., 1993.
16. L. Brachais, D. Davoust and G. Molle (1995). Conformational study of a synthetic analogue of alamethicin: influence of the conformation on ion-channel lifetimes. Int. J. Peptide Protein Res. 45, 164-172.
17. L. 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.
18. H. Duclohier, G. Molle, J.-Y. Dugast and G. Spach (1992) Prolines are not essential residues in the barrel-stave model for ion channel induced by alamethicin analogues. Biophys. J. 63, 868-873.
19. 1H NMR. Evidence for conformational heterogeneity in a voltage-gated peptide. Biochemistry 33, 4036-4045.
20. R.B. Merrifield (1963). Solid phase peptide synthesis: I The synthesis of a tetrapeptide. J. Am. Chem. Soc. 89, 2149-2154.
21. G. Molle G, J.-Y. Dugast, H. Duclohier, P. Daumas, F. Heitz and G. Spach (1988). Ionophore properties of a synthetic alpha-helical transmembrane fragment of the mitochondrial HF ATP synthetase of Saccharomyces cerevisiae. Biophys. J. 53, 193-203.
22. G. Molle and J.-Y. Dugast (1990). Synthèse sur support solide de peptide comportant un residu aminoalcool C-terminal. Tetrahedron Lett. 31, 6355-6356.
23. T.D. Lee in: Methods of protein microcharacterisation. J.E. Shively, Ed., p. 403-441, The Human Press Clifton. N.J., 1986.
24. C.T. Chang, C.-S.C. Wu and J.T. Yang (1978). Circular dichroic analysis of protein conformation: inclusion of the β-turns. Anal. Biochem. 91, 13-31.
25. J.T. Yang. C.-S.C. Wu. and H.M. Martinez (1986). Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
26. 1H NMR spectra by selective excitation of experimental subspectra. J. Am. Chem. Soc. 107, 7197-7198.
27. A.T. Brünger. The X-PLOR software manual version 3.1. Yale University, New Haven, CT, 1992.
28. B.R. Brooks, R.E. Bruccoleri, B.D. Olafson, D.J. States, S. Swaminathan and M. Karplus (1983). CHARMM: a program for macromolecular energy, minimization and dynamics calculations. J. Comp. Chem. 4, 187-217.
29. P. Kraulis (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
30. K. Wüthrich (1986). NMR of Proteins and Nucleic Acids, John Wiley and Sons, New York, 162-175.
31. A.A. Yee, R. Babiuk and J.D.J. O'Neil (1995). The conformation of an alamethicin in methanol by multinuclear NMR spectroscopy and distance geometry/ simulated annealing. Biopolymers 36, 781-792.
32. H. Vogel (1987). Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes. Biochemistry 26, 4562-4572.
33. G. Boheim, W. Hanke and G. Jung (1983). Alamethicin pore formation: voltage-dependent flip-flop of a-helix dipole. Biophys. Struct. Mech 2, 181-191.
34. M.K. Mathew and P. Balaram (1983). A helix dipole model for alamethicin and related transmembrane channels. FEBS Lett. 157, 1-5.
35. V. Rizzo, S. Stankowski and G. Schwarz (1987). Alamethicin incorporation in lipid bilayers: a thermodynamic analysis. Biochemistry 26, 2751-2759.
36. G. Baumann and P. Mueller (1974). A molecular model of membrane excitability. J. Supramol. Struct. 2, 538-557.
37. M. Barranger-Mathys and D.S. Cafiso (1996). Membrane structure of voltage-gated channel forming peptides by site-directed spin labeling. Biochemistry 35, 498-505.
38. J. Jacob and D.S. Cafiso (1997). Mechanism of voltage-gating in alamethicin: NMR studies of structural variance. Biophys. J. 72, A398.
39. 2H nuclear magnetic resonance spectroscopy. Biophys. J. 72, A398.
40. G. Molle, J.-Y. Dugast, H. Duclohier and G. Spach (1988). Conductance properties of des-Aib-Leu-des-Pheol-Phe-alamethicin in planar lipid bilayers. Biochim. Biophys. Acta 938, 310-314.
41. A. Matsubara, K. Asami, A. Akagi and N. Nishino (1996). Ion-channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by barrel stave model. Chem. Comm. 17, 2069-2070.
42. K. Asami, A. Matsubara, A. Akagi and N. Nishino (1996). Ion-channels of alamethicins assembled with a cyclic pseudopeptide. Prog. Biophys. Mol. Biol. 65, suppl. 1, 107, P-C3-07.