Trichogin Topology and Activity in Model Membranes as Determined by Fluorescence Spectroscopy

N. Sewald, and H.-D. Jakubke, Peptides: Chemistry and Biology (Wiley-Vch, Weinheim, 2002).Google Scholar

Y. Shai, Mode of action of membrane active antimicrobial peptides, Biopolymers 66, 236–248 (2002).PubMedCrossRefGoogle Scholar

R. M. Epand, and H. J. Vogel, Diversity of antimicrobial peptides and their mechanisms of action, Biochim. Biophys. Acta 1462, 11–28 (1999).PubMedCrossRefGoogle Scholar

K. Matsuzaki, Molecular mechanisms of membrane perturbation by antimicrobial peptides, in Development of Novel Antimicrobial Agents: Emerging Strategies, edited by K. Lohner (Horizon Scientific Press, Wymondham, 2002), pp. 167–181.Google Scholar

L. Yang, T. A. Harroun, T. M. Weiss, L. Ding, and H. W. Huang, Barrel stave or toroidal model? A case study on melittin pores, Biophys. J. 81, 1475–1485 (2001).PubMedGoogle Scholar

F. Y. Chen., M. T. Lee, and H. W. Huang, Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin, Biophys. J. 82, 908–914 (2002).PubMedGoogle Scholar

C. Toniolo, M. Crisma, F. Formaggio, C. Peggion, R. F. Epand, and R. M. Epand, Lipopeptaibols, a novel family of membrane active, antimicrobial peptides, Cell. Mol. Life Sci. 58, 1179–1188 (2001).PubMedCrossRefGoogle Scholar

B. Pispisa, L. Stella, M. Venanzi, A. Palleschi, F. Marchiori, A. Polese, A., and C. Toniolo, A spectroscopic and molecular mechanics investigation on a series of Aib-based linear peptides and a peptide template, both containing tryptophan and a nitroxide derivatives as probes, Biopolymers 53, 169–181 (2000).PubMedCrossRefGoogle Scholar

B. Pispisa, L. Stella, M. Venanzi, A. Palleschi, C. Viappiani, A. Polese, F. Formaggio, and C. Toniolo, Quenching mechanisms in bichromophoric, 3₁₀-helical Aib-based peptides, modulated by chain-length dependent topologies, Macromolecules 33, 906–915 (2000).CrossRefGoogle Scholar

P. Scrimin, P. Tecilla, U. Tonellato, A. Veronese, M. Crisma, F. Formaggio, and C. Toniolo, Zinc(II) as an allosteric regulator of liposomal membrane permeability induced by synthetic template-assembled tripodal polypeptides., Chem. Eur. J. 8, 2753–2763 (2002).CrossRefGoogle Scholar

A. D. Milov, Y. D. Tsvetkov, F. Formaggio, M. Crisma, C. Toniolo, and J. Raap, Self-assembling and membrane modifying properties of a lipopeptaibol studied by CW-ESR and PELDOR spectroscopies, J. Pept. Sci. 9, 690–700 (2003).PubMedCrossRefGoogle Scholar

B. Pispisa, A. Palleschi, C. Mazzuca, L. Stella, A. Valeri, M. Venanzi, F. Formaggio, C. Toniolo, and Q. B. Broxterman, The versatility of combining FRET measurements and molecular mechanics results for determining the structural features of ordered peptides in solution, J. Fluoresc. 12, 213–217 (2002).CrossRefGoogle Scholar

C. Toniolo, A. Polese, F. Formaggio, M. Crisma, and J. Kamphuis, Circular dichroism spectrum of a peptide 3₁₀-helix, J. Am. Chem. Soc. 118, 2744–2745 (1996).CrossRefGoogle Scholar

B. Pispisa, C. Mazzuca, A. Palleschi, L. Stella, M. Venanzi, F. Formaggio, C. Toniolo, and Q. B. Broxterman, Structural features and conformational equilibria of 3₁₀-helical peptides in solution by spectroscopic and molecular mechanics studies, Biopolymers (Biospectroscopy) 67, 247–250 (2002).CrossRefGoogle Scholar

W. C. Wimley, and S. H. White, Experimentally determined hydrophobicity scale for proteins at membrane interfaces, Nat. Struct. Biol 3, 842–848 (1996).PubMedCrossRefGoogle Scholar

S. H. White, and W. C. Wimley, Hydrophobic interactions of peptides with membrane interfaces, Biochim. Biophys. Acta 1376, 339–352 (1998).PubMedGoogle Scholar

L. Stella, C. Mazzuca, M. Venanzi, A. Palleschi, M. Didonè, F. Formaggio, C. Toniolo, and B. Pispisa, Aggregation and water-membrane partition as major determinants of the activity of the antibiotic peptide trichogin GA IV, Biophys. J. 86, 936–945 (2004).PubMedGoogle Scholar

V. Rizzo, S. Stankowski, and G. Schwarz, Alamethicin incorporation in lipid bilayers: a thermodynamic study, Biochemistry 26, 2751–2759 (1987).PubMedCrossRefGoogle Scholar

M. Castanho, and M. Prieto, Filipin fluorescence quenching by spin-labeled probes: studies in acqueous solution and in a membrane model system, Biophys. J. 69, 155–168 (1995).PubMedGoogle Scholar

A. S. Ladokhin, and S. H. White, Alphas and taus of tryptophan fluorescence in membranes, Biophys. J. 81, 1825–1827 (2001).PubMedGoogle Scholar

H. W. Huang, Action of antimicrobial peptides: two-state model, Biochemistry 39, 8347–8352 (2000).PubMedCrossRefGoogle Scholar

S. H. White, and W. C. Wimley, Membrane protein folding and stability: physical principles, Annu Rev. Biophys. Biomol. Struct. 28, 319–365 (1999).PubMedCrossRefGoogle Scholar

T. J. McIntosh, A. Vidal, and S. A. Simon, The energetics of peptide-lipid interactions: modulation by interfacial dipoles and Cholesterol, in Peptide-Lipid Interactions, edited by T. J. McIntosh, and S. A. Simon (Academic Press, San Diego 2002), pp. 309–338.CrossRefGoogle Scholar

C. J. Russell, T. E. Thogeirsson, and Y.-K. Shin, The membrane affinities of the aliphatic amino acid side chains in an alpha-helical context are independent of membrane immersion depth, Biochemistry 38, 337–346 (1999).PubMedCrossRefGoogle Scholar

C. Tanford, The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed. (Wiley, New York, 1980).Google Scholar

B. Pispisa, M. Venanzi, L. Stella, A. Palleschi, A., and G. Zanotti, Photophysical and structural features of covalently bound peptide-protoporphyrin-peptide compounds carrying naphtalene chromophores, J. Phys. Chem. B 38, 8172–8179 (1999).CrossRefGoogle Scholar

L. Stella, M. Venanzi, M. Carafa, E. Maccaroni, M. E. Straccamore, G. Zanotti, A. Palleschi, and B. Pispisa, Structural features of model glycopeptides in solution and in membrane phase: a spectroscopic and molecular mechanics investigation, Biopolymers 64, 44–56 (2002)PubMedCrossRefGoogle Scholar

M. Schümann, M. Dathe, M., Wieprecht, T., Beyermann, M., and M. Bienert, The tendency of magainin to associate upon binding to phospholipid bilayers, Biochemistry 36, 4345–4351 (1997).PubMedCrossRefGoogle Scholar

J. Strahilevitz, A. Mor, P. Nicolas, and Y. Shai, Spectrum of antimicrobial activity and assembly of dermaseptin-b and its precursor form in phospholipid membranes, Biochemistry 33, 10951–10960 (1994).PubMedCrossRefGoogle Scholar

B. Pispisa, C. Mazzuca, A. Palleschi, L. Stella, M. Venanzi, M. Wakselman, J.-P. Mazaleyrat, M. Rainaldi, F. Formaggio, and C. Toniolo, A combined spectroscopic and theoretical study of a series of conformationally restricted hexapeptides carrying a rigid binaphthyl-nitroxide donor-acceptor pair, Chem. Eur. J. 9, 2–11 (2003).CrossRefGoogle Scholar

G. R. Jones, and A. R. Cossins, Physical methods of study, in Liposomes: a Practical Approach, edited by R. R. C. New (Oxford University Press, Oxford., 1990) pp. 183–220.Google Scholar

A. R. Curran, and D. M. Engelman, Sequence motifs, polar interactions and conformational changes in helical membrane proteins, Curr Op. Struct. Biol. 13, 412–417 (2003).CrossRefGoogle Scholar

K. Matsuzaki, O. Murase, N. Fujii, and K. Miyajima, Translocation of a channel forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore, Biochemistry 34, 6521–6526 (1995).PubMedCrossRefGoogle Scholar

W. C. Wimley, and S. H. White, Determining the membrane topology of peptides by fluorescence quenching. Biochemistry 39, 161–170 (2000).PubMedCrossRefGoogle Scholar

E. London, and A. S. Ladokhin, Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching, in Peptide-Lipid Interactions, edited by T.J. McIntosh, and S.A Simon (Academic Press, San Diego 2002) pp. 89–115.CrossRefGoogle Scholar

A. S. Ladokhin, Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide, Meth. Enzymol. 278, 462–473 (1997).PubMedGoogle Scholar

A. S. Ladokhin, Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: theoretical considerations, Biophys. J. 76, 946–955 (1999).PubMedGoogle Scholar

J.C. McIntyre, and R.G. Sleight, Fluorescence assay for phospholipid membrane asimmetry, Biochemistry 30, 11819–11827 (1991).PubMedCrossRefGoogle Scholar

L. J. Lis, M. McAlister, N. L. Fuller, R. P. Rand, and V. A. Parsegian, Measurement of the lateral compressibility of several phospholipid bilayers, Biophys. J. 37, 667–672 (1982).PubMedGoogle Scholar

S. Mazeres, V. Schram, J. F. Tocanne, and A. Lopez, 7-Nitrobenz-2-oxa-1,3-diazole-4-yl-labeled phospholipids in lipid membranes: differences in fluorescence behavior, Biophys. J. 71, 327–335 (1996).PubMedGoogle Scholar

D. E. Wolf, A. P. Winiski, A. E. Ting, K. M. Bocian, and R. E. Pagano, Determination of the transbilayer distribution of fluorescent lipid analogues by nonradiative fluorescence resonance energy transfer, Biochemistry 31, 2865–2873 (1992).PubMedCrossRefGoogle Scholar

M. Lee, F. Chen, and H. W. Huang, Energetics of pore formation induced by membrane active peptides, Biochemistry 43, 3590–3599 (2004).PubMedCrossRefGoogle Scholar

A. Coutinho, and M. Prieto, Cooperative partition model of nystatin interaction with phospholipid vesicles, Biophys. J. 84, 3061–3078 (2003).PubMedGoogle Scholar

M. Zuckermann, and T. Heimburg, Insertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces, Biophys. J. 81, 2458–2472 (2001).PubMedGoogle Scholar

R. F. Epand, R. M. Epand, V. Monaco, S. Stoia, F. Formaggio, M. Crisma, and C. Toniolo, The antimicrobial peptide trichogin and its interaction with phospholipid membranes, Eur. J. Biochem. 266, 1021–1028 (1999).PubMedCrossRefGoogle Scholar

R. D. Kaiser, and E. London, Determination of the depth of BODIPY probes in model membranes by parallax analysis of fluorescence quenching, Biochim. Biophys. Acta 1375, 13–22 (1998).PubMedCrossRefGoogle Scholar

C. Mazzuca, L. Stella, M. Venanzi, F. Formaggio, C. Toniolo, and B. Pispisa, Mechanism of membrane activity of the antibiotic trichogin GA IV: a two-state transition controlled by peptide concentration, Biophys. J. 88, 3411–3421 (2005).PubMedCrossRefGoogle Scholar

V. Monaco, F. Formaggio, M. Crisma, C. Toniolo, P. Hanson, and G. L. Millhauser, Orientation and immersion depth of a helical lipopeptaibol in membranes using TOAC as an ESR probe, Biopolymers 50, 239–253 (1999).PubMedCrossRefGoogle Scholar

M. R. R. de Planque, and J. A. Killian, Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring, Mol. Membr. Biol. 20, 271–284 (2003).PubMedCrossRefGoogle Scholar