Abstract
Natural and synthetic membrane active peptides as well as fragments from membrane proteins interact with membranes. In several cases, such interactions cause the insertion of the peptides to the membrane and their assembly within the lipid bilayer. Here we present spectroscopic approaches utilizing NBD and rhodamine fluorescently labeled peptides to measure peptide–membrane interaction and peptide–peptide interaction within the membrane. The usage of the physical properties of NBD and rhodamine in solution and in membranes provides useful information on the interplay between peptides and lipids.
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References
Shai Y (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1462:55–70
Papo N, Shai Y (2003) Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 42:458–466
Oren Z, Hong J, Shai Y (1999) A comparative study on the structure and function of a cytolytic alpha-helical peptide and its antimicrobial beta-sheet diastereomer. Eur J Biochem 259:360–369
Merklinger E, Gofman Y, Kedrov A, Driessen AJ, Ben-Tal N, Shai Y, Rapaport D (2012) Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors. Biochem J 442:381–389
Freire E (1995) Differential scanning calorimetry. Methods Mol Biol 40:191–218
Epand RM, Rotem S, Mor A, Berno B, Epand RF (2008) Bacterial membranes as predictors of antimicrobial potency. J Am Chem Soc 130:14346–14352
Oren Z, Ramesh J, Avrahami D, Suryaprakash N, Shai Y, Jelinek R (2002) Structures and mode of membrane interaction of a short alpha helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy. Eur J Biochem 269:3869–3880
Grieco P, Carotenuto A, Auriemma L, Saviello MR, Campiglia P, Gomez-Monterrey IM, Marcellini L, Luca V, Barra D, Novellino E, Mangoni ML (2012) The effect of d-amino acid substitution on the selectivity of temporin L towards target cells: identification of a potent anti-Candida peptide. Biochim Biophys Acta 1828(2):652–660
Mansson R, Bysell H, Hansson P, Schmidtchen A, Malmsten M (2011) Effects of peptide secondary structure on the interaction with oppositely charged microgels. Biomacromolecules 12:419–424
Gable JE, Schlamadinger DE, Cogen AL, Gallo RL, Kim JE (2009) Fluorescence and UV resonance Raman study of peptide-vesicle interactions of human cathelicidin LL-37 and its F6W and F17W mutants. Biochemistry 48:11264–11272
Chattopadhyay A, London E (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26:39–45
Rapaport D, Shai Y (1992) Aggregation and organization of pardaxin in phospholipid membranes. A fluorescence energy transfer study. J Biol Chem 267:6502–6509
Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y (1992) Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31:12416–12423
Gazit E, Lee WJ, Brey PT, Shai Y (1994) Mode of action of the antibacterial cecropin B2: a spectrofluorometric study. Biochemistry 33:10681–10692
Oren Z, Lerman JC, Gudmundsson GH, Agerberth B, Shai Y (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem J 341(Pt 3):501–513
Hetru C, Letellier L, Oren Z, Hoffmann JA, Shai Y (2000) Androctonin, a hydrophilic disulphide-bridged non-haemolytic anti-microbial peptide: a plausible mode of action. Biochem J 345(Pt 3):653–664
Merrifield RB, Vizioli LD, Boman HG (1982) Synthesis of the antibacterial peptide cecropin A (1–33). Biochemistry 21:5020–5031
Avrahami D, Oren Z, Shai Y (2001) Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry 40:12591–12603
Reuven EM, Dadon Y, Viard M, Manukovsky N, Blumenthal R, Shai Y (2012) HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion. Biochemistry 51:2867–2878
Cohen T, Cohen SJ, Antonovsky N, Cohen IR, Shai Y (2010) HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferation. PLoS Pathog 6:e1001085
Cohen T, Pevsner-Fischer M, Cohen N, Cohen IR, Shai Y (2008) Characterization of the interacting domain of the HIV-1 fusion peptide with the transmembrane domain of the T-cell receptor. Biochemistry 47:4826–4833
Acknowledgments
This work was supported by the Israel Science Foundation, German-Israel Foundation (GIF), Israel Ministry of Health, Benoziyo Center for Neurological Diseases, and European Community Grant No. 278998. Yechiel Shai is the incumbent of the Harold S. and Harriet B. Brady Professorial Chair in Cancer Research.
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Saar-Dover, R., Ashkenazi, A., Shai, Y. (2013). Peptide Interaction with and Insertion into Membranes. In: Rapaport, D., Herrmann, J. (eds) Membrane Biogenesis. Methods in Molecular Biology, vol 1033. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-487-6_12
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DOI: https://doi.org/10.1007/978-1-62703-487-6_12
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