The interaction of cell-penetrating peptides with lipid model systems and subsequent lipid reorganization: Thermodynamic and structural characterization

Journal of Peptide Science

Volumn 15, Issue 3, 2009, Pages 200-209

  Alves, Isabel D ^a,b   Correia, Isabelle ^a,b   Jiao, Chen Yu ^a,b   Sachon, Emmanuelle ^a,b   Sagan, Sandrine ^a,b   Lavielle, Solange ^a,b   Tollin, Gordon ^c   Chassaing, Gérard ^a,b  

^a SORBONNE UNIVERSITÉ   (France)

^b CNRS   (France)

^c UNIVERSITY OF ARIZONA   (United States)

Author keywords

31P NMR; Antimicrobial peptide; Cell penetrating peptide; Differential scanning calorimetry; Lipid supramolecular organization; Peptide membrane interaction; Plasmon waveguide resonance spectroscopy

Indexed keywords

CELL PENETRATING PEPTIDE; LIPID; PEPTIDE;

BINDING AFFINITY; CONFERENCE PAPER; CONTROLLED STUDY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; THERMODYNAMICS; ARTICLE; CELL MEMBRANE; CHEMISTRY; DIFFERENTIAL SCANNING CALORIMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EUKARYOTA;

CALORIMETRY, DIFFERENTIAL SCANNING; CELL MEMBRANE; LIPIDS; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; THERMODYNAMICS;

EID: 63449087071     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1070     Document Type: Conference Paper

References (41)

1. Derossi D, Chassaing G, Prochiantz A. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 1998; 8: 84-87.
2. Lindgren M, Hällbrink M, Prochiantz A, Langel U. Cell-penetrating peptides. Trends Pharmacol. Sci. 2000; 21: 99-103.
3. Snyder EL, Dowdy SF. Cell penetrating peptides in drug delivery. Pharm. Res. 2004; 21: 389-393.
4. Derossi D, Joliot AH, Chassaing G, Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 1994; 269: 10444-10450.
5. Derossi D, Calvet S, Trembleau A, Brunissen A, Chassaing G, Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 1996; 271: 18188-18193.
6. Derossi D, Chassaing G,Prochiantz A.Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 1998; 8: 84-87.
7. Chassaing G, Prochiantz A. Peptides usable as vectors for the intracellular addressing of bioactive molecules. PCT Int. Appl, WO 9712912: 31; 1997.
8. Drin G, Déméné H, Temsamani J, Brasseur R. Translocation of the pAntp peptide and its amphipathic analogue AP-2AL. Biochemistry 2001; 40: 1824-1834.
9. Prochiantz A. Getting hydrophilic compounds into cells: lessons from homeopeptides. Curr. Opin. Neurobiol. 1996; 6: 629-634.
10. Binder H, Lindblom G. Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys. J. 2003; 85: 982-995.
11. Conner SD, Schmid SL.Regulated portals of entry into the cell. Nature 2003; 422: 37-44.
12. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. J. Biol. Chem. 2003; 278: 31192-311201.
13. Fischer R, Köhler K, Fotin-Mleczek M, Brock R. A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 2004; 279: 12625-12635.
14. Lamaziere A, Burlina F, Wolf C, Chassaing G, Trugnan G, Ayala-Sanmartin J. Non-metabolic membrane tabulation and permeability induced by bioactive peptides. PLoS ONE 2007; 2: e201.
15. Alves ID, Goasdoué N, Correia I, AubryS, Galanth C, Sagan S, Lavielle S, Chassaing G. Membrane interaction and perturbation mechanisms induced by two cationic cell penetrating peptides with distinct charge distribution. Biochim. Biophys. Acta 2008; 1780: 948-959.
16. Salamon Z, Macleod HA, Tollin G. Coupled plasmon-waveguide resonators: a new spectroscopic tool for probing proteolipid film structure and properties. Biophys. J. 1997; 73: 2791-2797.
17. Tollin G, Salamon Z, Hruby VJ. Techniques: plasmon-waveguide resonance (PWR) spectroscopy as a tool to study ligand-GPCR interactions. Trends Pharmacol. Sci. 2003; 24: 655-659.
18. Mueller P, Rudin DO, Tien HT, Wescott WC. Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature 1962; 194: 979-980.
19. Salamon Z, Tollin G. Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy canprovide useful insights intomembraneprotein function. Biophys. J. 2004; 86: 2508-2516.
20. Devanathan S, Salamon Z, Tollin G, Fitch J, Meyer TE, Cusanovich MA. Binding of oxidized and reduced cytochrome c2 to photosynthetic reaction centers: plasmon-waveguide resonance spectroscopy. Biochemistry 2004; 43: 16405-16415.
21. 2+ and protein on the thermotropic behavior of the negatively charged phospholipids, phosphatidylglycerol. Biochim. Biophys. Acta 1974; 339: 432-437.
22. Girault L, Boudou A, Dufourc EJ. 113Cd-, 31P-NMR and fluorescence polarization studies of cadmium (II) interactions with phospholipids in modelmembranes. Biochim. Biophys. Acta 1998; 1414: 140-154.
23. Aussedat B, Sagan S, Chassaing G, Bolbach G, Burlina F. Quantification of the efficiency of cargo delivery by peptidic and pseudopeptidic Trojan carriers using MALDI-TOF mass spectrometry. Biochim. Biophys. Acta 2006; 1758: 375-383.
24. Delaroche D, Aussedat B, Aubry S, Chassaing G, Burlina F, Clodic G, Bolbach G, Lavielle S, Sagan S. Tracking a new cell-penetrating (W/R) nonapeptide, through an enzyme-stable mass spectrometry reporter tag. Anal. Chem. 2007; 79: 1932-1938.
25. Andrushchenko VV, Vogel HJ, Prenner EJ. Interactions of tryptophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry. Biochim. Biophys. Acta 2007; 1768: 2447-2458.
26. Henzler-Wildman KA, Martinez GV, Brown MF, Ramamoorthy A. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry 2004; 43(26): 8459-8469.
27. Prenner EJ, Lewis RN, Kondejewski LH, Hodges RS, McElhaney RN. Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes. Biochim. Biophys. Acta 1999; 1417: 211-223.
28. Matsuzaki K, Sugishita K, Ishibe N, Ueha M, Nakata S, Miyajima K, Epand RM. Relationship of membrane curvature to the formation of pores bymagainin 2. Biochemistry 1998; 37: 11856-11863.
29. Adão R, Seixas R, Gomes P, Pessoa JC, Bastos M. Membrane structure and interactions of a short Lycotoxin I analogue. J. Pept. Sci. 2008; 14: 528-534.
30. Salamon Z, Lindblom G, Tollin G. Plasmon-waveguide resonance and impedance spectroscopy studies of the interaction between penetratin and supported lipid bilayermembranes. Biophys. J. 2003; 84: 1796-1807.
31. Magzoub M, Kilk K, Eriksson LE, Langel U, Gräslund A. Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles. Biochim. Biophys. Acta 2001; 1512: 77-89.
32. Christiaens B, Symoens S, Verheyden S, Engelborghs Y, Joliot A, Prochiantz A, Vandekerckhove J, RosseneuM, Vanloo B. Tryptophan fluorescence study of the interaction of penetratin peptides with model membranes. Eur. J. Biochem. 2002; 269: 2918-2926.
33. Lamazière A, Wolf C, Lambert O, Chassaing G, Trugnan G, Ayala-Sanmartin J. The homeodomain derived peptide Penetratin induces curvature of fluid membrane domains. PLoS ONE 2008; 3: e1938.
34. Pott T, Paternostre M, Dufourc EJ. A comparative study of the action of melittin on sphingomyelin and phosphatidylcholine bilayers. Eur. Biophys. J. 1998; 27: 237-245.
35. Hallock KJ, Lee D-K, Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 2003; 84: 3052-3060.
36. Prenner EJ, Ruthven RNAH, McElhaney RE. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta 1999; 1462: 201-221.
37. Afonin S, Frey A, Bayerl S, Fischer D, Wadhwani P, Weinkauf S, Ulrich AS. The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes. ChemPhysChem 2006; 13: 2134-2142.
38. Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002; 66: 236-248.
39. Futaki S, Suzuki T, Ohashi W, Yagami T, Tanaka S, Ueda K, Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 2001; 276: 5836-5840.
40. Mitchell DJ, Kim DT, Steinman L, Fathman CG, Rothbard JB. Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 2000; 56: 318-325.
41. Persson D, Thorén PE, Nordén B. Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles. FEBS Lett. 2001; 505: 307-312.