메뉴 건너뛰기




Volumn 54, Issue 2, 2015, Pages 194-207

Translocation mechanism(s) of cell-penetrating peptides: Biophysical studies using artificial membrane bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CELLS; CYTOLOGY; MACHINERY; MECHANISMS; PEPTIDES;

EID: 84922460774     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501392n     Document Type: Article
Times cited : (138)

References (112)
  • 1
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes J. Biol. Chem. 269, 10444
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 2
    • 0033520487 scopus 로고    scopus 로고
    • In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse
    • Schwarze, S. R., Ho, A., Vocero-Akbani, A., and Dowdy, S. F. (1999) In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse Science 285, 1569-1572
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 3
    • 0842346326 scopus 로고    scopus 로고
    • Conjugate for efficient delivery of short interfering RNA (siRNA) into mammalian cells
    • Muratovska, A. and Eccles, M. R. (2004) Conjugate for efficient delivery of short interfering RNA (siRNA) into mammalian cells FEBS Lett. 558, 63-68
    • (2004) FEBS Lett. , vol.558 , pp. 63-68
    • Muratovska, A.1    Eccles, M.R.2
  • 4
    • 0034006169 scopus 로고    scopus 로고
    • Tat peptide-derivatized magnetic nanoparticles allow in vivo tracking and recovery of progenitor cells
    • Lewin, M., Carlesso, N., Tung, C.-H., Tang, X.-W., Cory, D., Scadden, D. T., and Weissleder, R. (2000) Tat peptide-derivatized magnetic nanoparticles allow in vivo tracking and recovery of progenitor cells Nat. Biotechnol. 18, 410-414
    • (2000) Nat. Biotechnol. , vol.18 , pp. 410-414
    • Lewin, M.1    Carlesso, N.2    Tung, C.-H.3    Tang, X.-W.4    Cory, D.5    Scadden, D.T.6    Weissleder, R.7
  • 5
    • 84862674370 scopus 로고    scopus 로고
    • Cell entry of cell penetrating peptides: Tales of tails wagging dogs
    • Jones, A. T. and Sayers, E. J. (2012) Cell entry of cell penetrating peptides: Tales of tails wagging dogs J. Controlled Release 161, 582-591
    • (2012) J. Controlled Release , vol.161 , pp. 582-591
    • Jones, A.T.1    Sayers, E.J.2
  • 7
    • 22144453931 scopus 로고    scopus 로고
    • Quantification of the Cellular Uptake of Cell-Penetrating Peptides by MALDI-TOF Mass Spectrometry
    • Burlina, F., Sagan, S., Bolbach, G., and Chassaing, G. (2005) Quantification of the Cellular Uptake of Cell-Penetrating Peptides by MALDI-TOF Mass Spectrometry Angew. Chem., Int. Ed. 44, 4244-4247
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 4244-4247
    • Burlina, F.1    Sagan, S.2    Bolbach, G.3    Chassaing, G.4
  • 9
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vivès, E., Brodin, P., and Lebleu, B. (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 272, 16010-16017
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 10
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 12
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris, M. C., Depollier, J., Mery, J., Heitz, F., and Divita, G. (2001) A peptide carrier for the delivery of biologically active proteins into mammalian cells Nat. Biotechnol. 19, 1173-1176
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 14
    • 18944361896 scopus 로고    scopus 로고
    • Environmental factors that enhance the action of the cell penetrating peptide pep-1: A spectroscopic study using lipidic vesicles
    • Henriques, S. T. and Castanho, M. A. R. B. (2005) Environmental factors that enhance the action of the cell penetrating peptide pep-1: A spectroscopic study using lipidic vesicles Biochim. Biophys. Acta 1669, 75-86
    • (2005) Biochim. Biophys. Acta , vol.1669 , pp. 75-86
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 15
    • 77952990022 scopus 로고    scopus 로고
    • Fast membrane association is a crucial factor in the peptide pep-1 translocation mechanism: A kinetic study followed by surface plasmon resonance
    • Henriques, S. T., Castanho, M. A. R. B., Pattenden, L. K., and Aguilar, M.-I. (2010) Fast membrane association is a crucial factor in the peptide pep-1 translocation mechanism: A kinetic study followed by surface plasmon resonance Pept. Sci. 94, 314-322
    • (2010) Pept. Sci. , vol.94 , pp. 314-322
    • Henriques, S.T.1    Castanho, M.A.R.B.2    Pattenden, L.K.3    Aguilar, M.-I.4
  • 16
    • 40149084042 scopus 로고    scopus 로고
    • Small Changes in the Primary Structure of Transportan 10 Alter the Thermodynamics and Kinetics of its Interaction with Phospholipid Vesicles
    • Yandek, L. E., Pokorny, A., and Almeida, P. F. F. (2008) Small Changes in the Primary Structure of Transportan 10 Alter the Thermodynamics and Kinetics of its Interaction with Phospholipid Vesicles Biochemistry 47, 3051-3060
    • (2008) Biochemistry , vol.47 , pp. 3051-3060
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.F.3
  • 17
    • 34047238809 scopus 로고    scopus 로고
    • Mechanism of the Cell-Penetrating Peptide Transportan 10 Permeation of Lipid Bilayers
    • Yandek, L. E., Pokorny, A., Florén, A., Knoelke, K., Langel, Ü., and Almeida, P. F. F. (2007) Mechanism of the Cell-Penetrating Peptide Transportan 10 Permeation of Lipid Bilayers Biophys. J. 92, 2434-2444
    • (2007) Biophys. J. , vol.92 , pp. 2434-2444
    • Yandek, L.E.1    Pokorny, A.2    Florén, A.3    Knoelke, K.4    Langel Ü.5    Almeida, P.F.F.6
  • 18
    • 34447339142 scopus 로고    scopus 로고
    • Single-Molecule Imaging of the Association of the Cell-Penetrating Peptide Pep-1 to Model Membranes
    • Sharonov, A. and Hochstrasser, R. M. (2007) Single-Molecule Imaging of the Association of the Cell-Penetrating Peptide Pep-1 to Model Membranes Biochemistry 46, 7963-7972
    • (2007) Biochemistry , vol.46 , pp. 7963-7972
    • Sharonov, A.1    Hochstrasser, R.M.2
  • 19
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles
    • Säälik, P., Niinep, A., Pae, J., Hansen, M., Lubenets, D., Langel, Ü., and Pooga, M. (2011) Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles J. Controlled Release 153, 117-125
    • (2011) J. Controlled Release , vol.153 , pp. 117-125
    • Säälik, P.1    Niinep, A.2    Pae, J.3    Hansen, M.4    Lubenets, D.5    Langel Ü.6    Pooga, M.7
  • 21
    • 0037457905 scopus 로고    scopus 로고
    • Application of a Novel Analysis to Measure the Binding of the Membrane-Translocating Peptide Penetratin to Negatively Charged Liposomes
    • Persson, D., Thorén, P. E. G., Herner, M., Lincoln, P., and Nordén, B. (2003) Application of a Novel Analysis To Measure the Binding of the Membrane-Translocating Peptide Penetratin to Negatively Charged Liposomes Biochemistry 42, 421-429
    • (2003) Biochemistry , vol.42 , pp. 421-429
    • Persson, D.1    Thorén, P.E.G.2    Herner, M.3    Lincoln, P.4    Nordén, B.5
  • 23
    • 4644224822 scopus 로고    scopus 로고
    • Vesicle Membrane Interactions of Penetratin Analogues
    • Persson, D., Thorén, P. E. G., Lincoln, P., and Nordén, B. (2004) Vesicle Membrane Interactions of Penetratin Analogues Biochemistry 43, 11045-11055
    • (2004) Biochemistry , vol.43 , pp. 11045-11055
    • Persson, D.1    Thorén, P.E.G.2    Lincoln, P.3    Nordén, B.4
  • 24
    • 33745151952 scopus 로고    scopus 로고
    • Membrane Interactions of Cell-Penetrating Peptides Probed by Tryptophan Fluorescence and Dichroism Techniques: Correlations of Structure to Cellular Uptake
    • Caesar, C. E. B., Esbjörner, E. K., Lincoln, P., and Nordén, B. (2006) Membrane Interactions of Cell-Penetrating Peptides Probed by Tryptophan Fluorescence and Dichroism Techniques: Correlations of Structure to Cellular Uptake Biochemistry 45, 7682-7692
    • (2006) Biochemistry , vol.45 , pp. 7682-7692
    • Caesar, C.E.B.1    Esbjörner, E.K.2    Lincoln, P.3    Nordén, B.4
  • 25
    • 0035852797 scopus 로고    scopus 로고
    • Translocation of the pAntp Peptide and Its Amphipathic Analogue AP-2AL
    • Drin, G., Déméné, H., Temsamani, J., and Brasseur, R. (2001) Translocation of the pAntp Peptide and Its Amphipathic Analogue AP-2AL Biochemistry 40, 1824-1834
    • (2001) Biochemistry , vol.40 , pp. 1824-1834
    • Drin, G.1    Déméné, H.2    Temsamani, J.3    Brasseur, R.4
  • 27
    • 0032473539 scopus 로고    scopus 로고
    • Peptide-liposome association. A critical examination with mastoparan-X
    • Hellmann, N. and Schwarz, G. (1998) Peptide-liposome association. A critical examination with mastoparan-X Biochim. Biophys. Acta 1369, 267-277
    • (1998) Biochim. Biophys. Acta , vol.1369 , pp. 267-277
    • Hellmann, N.1    Schwarz, G.2
  • 28
    • 0344011975 scopus 로고    scopus 로고
    • Interaction of the Trojan peptide penetratin with anionic lipid membranes: A calorimetric study
    • Binder, H. and Lindblom, G. (2003) Interaction of the Trojan peptide penetratin with anionic lipid membranes: A calorimetric study Phys. Chem. Chem. Phys. 5, 5108-5117
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 5108-5117
    • Binder, H.1    Lindblom, G.2
  • 29
    • 0037339402 scopus 로고    scopus 로고
    • Plasmon-Waveguide Resonance and Impedance Spectroscopy Studies of the Interaction between Penetratin and Supported Lipid Bilayer Membranes
    • Salamon, Z., Lindblom, G., and Tollin, G. (2003) Plasmon-Waveguide Resonance and Impedance Spectroscopy Studies of the Interaction between Penetratin and Supported Lipid Bilayer Membranes Biophys. J. 84, 1796-1807
    • (2003) Biophys. J. , vol.84 , pp. 1796-1807
    • Salamon, Z.1    Lindblom, G.2    Tollin, G.3
  • 30
    • 35448992145 scopus 로고    scopus 로고
    • Isothermal titration calorimetry for studying interactions between peptides and lipid membranes
    • Wieprecht, T. and Seelig, J. (2002) Isothermal titration calorimetry for studying interactions between peptides and lipid membranes Curr. Top. Membr. 52, 31-56
    • (2002) Curr. Top. Membr. , vol.52 , pp. 31-56
    • Wieprecht, T.1    Seelig, J.2
  • 31
    • 77954374712 scopus 로고    scopus 로고
    • Cell-Penetrating HIV1 TAT Peptides Can Generate Pores in Model Membranes
    • Ciobanasu, C., Siebrasse, J. P., and Kubitscheck, U. (2010) Cell-Penetrating HIV1 TAT Peptides Can Generate Pores in Model Membranes Biophys. J. 99, 153-162
    • (2010) Biophys. J. , vol.99 , pp. 153-162
    • Ciobanasu, C.1    Siebrasse, J.P.2    Kubitscheck, U.3
  • 33
    • 33947686656 scopus 로고    scopus 로고
    • A Fluorescence Spectroscopy Study on the Interactions of the TAT-PTD Peptide with Model Lipid Membranes
    • Tiriveedhi, V. and Butko, P. (2007) A Fluorescence Spectroscopy Study on the Interactions of the TAT-PTD Peptide with Model Lipid Membranes Biochemistry 46, 3888-3895
    • (2007) Biochemistry , vol.46 , pp. 3888-3895
    • Tiriveedhi, V.1    Butko, P.2
  • 34
    • 0043166977 scopus 로고    scopus 로고
    • Protein Transduction Domains of HIV-1 and SIV TAT Interact with Charged Lipid Vesicles. Binding Mechanism and Thermodynamic Analysis
    • Ziegler, A., Li Blatter, X., Seelig, A., and Seelig, J. (2003) Protein Transduction Domains of HIV-1 and SIV TAT Interact with Charged Lipid Vesicles. Binding Mechanism and Thermodynamic Analysis Biochemistry 42, 9185-9194
    • (2003) Biochemistry , vol.42 , pp. 9185-9194
    • Ziegler, A.1    Li Blatter, X.2    Seelig, A.3    Seelig, J.4
  • 35
    • 14044270161 scopus 로고    scopus 로고
    • Binding of Oligoarginine to Membrane Lipids and Heparan Sulfate: Structural and Thermodynamic Characterization of a Cell-Penetrating Peptide
    • Gonçalves, E., Kitas, E., and Seelig, J. (2005) Binding of Oligoarginine to Membrane Lipids and Heparan Sulfate: Structural and Thermodynamic Characterization of a Cell-Penetrating Peptide Biochemistry 44, 2692-2702
    • (2005) Biochemistry , vol.44 , pp. 2692-2702
    • Gonçalves, E.1    Kitas, E.2    Seelig, J.3
  • 37
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G., and Prochiantz, A. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent J. Biol. Chem. 271, 18188-18193
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 38
    • 77952580991 scopus 로고    scopus 로고
    • Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
    • Eiríksdóttir, E., Konate, K., Langel, Ü., Divita, G., and Deshayes, S. (2010) Secondary structure of cell-penetrating peptides controls membrane interaction and insertion Biochim. Biophys. Acta 1798, 1119-1128
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1119-1128
    • Eiríksdóttir, E.1    Konate, K.2    Langel Ü.3    Divita, G.4    Deshayes, S.5
  • 39
    • 1042288299 scopus 로고    scopus 로고
    • Insight into the Mechanism of Internalization of the Cell-Penetrating Carrier Peptide Pep-1 through Conformational Analysis
    • Deshayes, S., Heitz, A., Morris, M. C., Charnet, P., Divita, G., and Heitz, F. (2004) Insight into the Mechanism of Internalization of the Cell-Penetrating Carrier Peptide Pep-1 through Conformational Analysis Biochemistry 43, 1449-1457
    • (2004) Biochemistry , vol.43 , pp. 1449-1457
    • Deshayes, S.1    Heitz, A.2    Morris, M.C.3    Charnet, P.4    Divita, G.5    Heitz, F.6
  • 40
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles
    • Magzoub, M., Kilk, K., Eriksson, L. E. G., Langel, Ü., and Gräslund, A. (2001) Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles Biochim. Biophys. Acta 1512, 77-89
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson, L.E.G.3    Langel Ü.4    Gräslund, A.5
  • 41
    • 78651234759 scopus 로고    scopus 로고
    • Distinct Behaviour of the Homeodomain Derived Cell Penetrating Peptide Penetratin in Interaction with Different Phospholipids
    • Maniti, O., Alves, I., Trugnan, G., and Ayala-Sanmartin, J. (2010) Distinct Behaviour of the Homeodomain Derived Cell Penetrating Peptide Penetratin in Interaction with Different Phospholipids PLoS One 5, e15819
    • (2010) PLoS One , vol.5 , pp. 15819
    • Maniti, O.1    Alves, I.2    Trugnan, G.3    Ayala-Sanmartin, J.4
  • 42
    • 46349095009 scopus 로고    scopus 로고
    • Membrane interaction and perturbation mechanisms induced by two cationic cell penetrating peptides with distinct charge distribution
    • Alves, I. D., Goasdoué, N., Correia, I., Aubry, S., Galanth, C., Sagan, S., Lavielle, S., and Chassaing, G. (2008) Membrane interaction and perturbation mechanisms induced by two cationic cell penetrating peptides with distinct charge distribution Biochim. Biophys. Acta 1780, 948-959
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 948-959
    • Alves, I.D.1    Goasdoué, N.2    Correia, I.3    Aubry, S.4    Galanth, C.5    Sagan, S.6    Lavielle, S.7    Chassaing, G.8
  • 43
    • 34249081426 scopus 로고    scopus 로고
    • Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1
    • Henriques, S. T., Quintas, A., Bagatolli, L. A., Homble, F., and Castanho, M. A. R. B. (2007) Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1 Mol. Membr. Biol. 24, 282-293
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 282-293
    • Henriques, S.T.1    Quintas, A.2    Bagatolli, L.A.3    Homble, F.4    Castanho, M.A.R.B.5
  • 44
    • 79957997146 scopus 로고    scopus 로고
    • Physicochemical Mechanism for the Enhanced Ability of Lipid Membrane Penetration of Polyarginine
    • Takechi, Y., Yoshii, H., Tanaka, M., Kawakami, T., Aimoto, S., and Saito, H. (2011) Physicochemical Mechanism for the Enhanced Ability of Lipid Membrane Penetration of Polyarginine Langmuir 27, 7099-7107
    • (2011) Langmuir , vol.27 , pp. 7099-7107
    • Takechi, Y.1    Yoshii, H.2    Tanaka, M.3    Kawakami, T.4    Aimoto, S.5    Saito, H.6
  • 45
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics
    • Almeida, P. F. and Pokorny, A. (2009) Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics Biochemistry 48, 8083-8093
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 46
    • 28544450399 scopus 로고    scopus 로고
    • Biophysical and Biological Studies of End-Group-Modified Derivatives of Pep-1
    • Weller, K., Lauber, S., Lerch, M., Renaud, A., Merkle, H. P., and Zerbe, O. (2005) Biophysical and Biological Studies of End-Group-Modified Derivatives of Pep-1 Biochemistry 44, 15799-15811
    • (2005) Biochemistry , vol.44 , pp. 15799-15811
    • Weller, K.1    Lauber, S.2    Lerch, M.3    Renaud, A.4    Merkle, H.P.5    Zerbe, O.6
  • 47
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • Magzoub, M., Eriksson, L. E., and Gräslund, A. (2002) Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration Biochim. Biophys. Acta 1563, 53-63
    • (2002) Biochim. Biophys. Acta , vol.1563 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.2    Gräslund, A.3
  • 48
    • 0037466075 scopus 로고    scopus 로고
    • Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles
    • Magzoub, M., Eriksson, L. E. G., and Gräslund, A. (2003) Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles Biophys. Chem. 103, 271-288
    • (2003) Biophys. Chem. , vol.103 , pp. 271-288
    • Magzoub, M.1    Eriksson, L.E.G.2    Gräslund, A.3
  • 49
    • 0035860429 scopus 로고    scopus 로고
    • Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles
    • Persson, D., Thorén, P. E., and Nordén, B. (2001) Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles FEBS Lett. 505, 307-312
    • (2001) FEBS Lett. , vol.505 , pp. 307-312
    • Persson, D.1    Thorén, P.E.2    Nordén, B.3
  • 50
    • 21844474526 scopus 로고    scopus 로고
    • The interaction of the cell-penetrating peptide penetratin with heparin, heparansulfates and phospholipid vesicles investigated by ESR spectroscopy
    • Ghibaudi, E., Boscolo, B., Inserra, G., Laurenti, E., Traversa, S., Barbero, L., and Ferrari, R. P. (2005) The interaction of the cell-penetrating peptide penetratin with heparin, heparansulfates and phospholipid vesicles investigated by ESR spectroscopy J. Pept. Sci. 11, 401-409
    • (2005) J. Pept. Sci. , vol.11 , pp. 401-409
    • Ghibaudi, E.1    Boscolo, B.2    Inserra, G.3    Laurenti, E.4    Traversa, S.5    Barbero, L.6    Ferrari, R.P.7
  • 51
    • 84898543428 scopus 로고    scopus 로고
    • The Efficacies of Cell-Penetrating Peptides in Accumulating in Large Unilamellar Vesicles Depend on their Ability to Form Inverted Micelles
    • Swiecicki, J.-M., Bartsch, A., Tailhades, J., Di Pisa, M., Heller, B., Chassaing, G., Mansuy, C., Burlina, F., and Lavielle, S. (2014) The Efficacies of Cell-Penetrating Peptides in Accumulating in Large Unilamellar Vesicles Depend on their Ability To Form Inverted Micelles ChemBioChem 15, 884-891
    • (2014) ChemBioChem , vol.15 , pp. 884-891
    • Swiecicki, J.-M.1    Bartsch, A.2    Tailhades, J.3    Di Pisa, M.4    Heller, B.5    Chassaing, G.6    Mansuy, C.7    Burlina, F.8    Lavielle, S.9
  • 52
    • 84862849271 scopus 로고    scopus 로고
    • Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis
    • Bode, S. A., Thévenin, M., Bechara, C., Sagan, S., Bregant, S., Lavielle, S., Chassaing, G., and Burlina, F. (2012) Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis Chem. Commun. 48, 7179-7181
    • (2012) Chem. Commun. , vol.48 , pp. 7179-7181
    • Bode, S.A.1    Thévenin, M.2    Bechara, C.3    Sagan, S.4    Bregant, S.5    Lavielle, S.6    Chassaing, G.7    Burlina, F.8
  • 53
    • 84890766631 scopus 로고    scopus 로고
    • Fifteen Years of Cell-Penetrating, Guanidinium-Rich Molecular Transporters: Basic Science, Research Tools, and Clinical Applications
    • Stanzl, E. G., Trantow, B. M., Vargas, J. R., and Wender, P. A. (2013) Fifteen Years of Cell-Penetrating, Guanidinium-Rich Molecular Transporters: Basic Science, Research Tools, and Clinical Applications Acc. Chem. Res. 46, 2944-2954
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2944-2954
    • Stanzl, E.G.1    Trantow, B.M.2    Vargas, J.R.3    Wender, P.A.4
  • 54
    • 63449087071 scopus 로고    scopus 로고
    • The interaction of cell-penetrating peptides with lipid model systems and subsequent lipid reorganization: Thermodynamic and structural characterization
    • Alves, I. D., Correia, I., Jiao, C. Y., Sachon, E., Sagan, S., Lavielle, S., Tollin, G., and Chassaing, G. (2009) The interaction of cell-penetrating peptides with lipid model systems and subsequent lipid reorganization: Thermodynamic and structural characterization J. Pept. Sci. 15, 200-209
    • (2009) J. Pept. Sci. , vol.15 , pp. 200-209
    • Alves, I.D.1    Correia, I.2    Jiao, C.Y.3    Sachon, E.4    Sagan, S.5    Lavielle, S.6    Tollin, G.7    Chassaing, G.8
  • 55
    • 80052451032 scopus 로고    scopus 로고
    • Relationships between Membrane Binding, Affinity and Cell Internalization Efficacy of a Cell-Penetrating Peptide: Penetratin as a Case Study
    • Alves, I. D., Bechara, C., Walrant, A., Zaltsman, Y., Jiao, C.-Y., and Sagan, S. (2011) Relationships between Membrane Binding, Affinity and Cell Internalization Efficacy of a Cell-Penetrating Peptide: Penetratin as a Case Study PLoS One 6, e24096
    • (2011) PLoS One , vol.6 , pp. 24096
    • Alves, I.D.1    Bechara, C.2    Walrant, A.3    Zaltsman, Y.4    Jiao, C.-Y.5    Sagan, S.6
  • 56
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) 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, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 58
  • 59
    • 77953727984 scopus 로고    scopus 로고
    • Tubular structures in heterogeneous membranes induced by the cell penetrating peptide penetratin
    • Lamaziere, A., Chassaing, G., Trugnan, G., and Ayala-Sanmartin, J. (2009) Tubular structures in heterogeneous membranes induced by the cell penetrating peptide penetratin Commun. Integr. Biol. 2, 223-224
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 223-224
    • Lamaziere, A.1    Chassaing, G.2    Trugnan, G.3    Ayala-Sanmartin, J.4
  • 61
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Prochiantz, A. (1998) Trojan peptides: The penetratin system for intracellular delivery Trends Cell Biol. 8, 84-87
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Prochiantz, A.1
  • 63
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • Henriques, S. T., Melo, M. N., and Castanho, M. A. R. B. (2006) Cell-penetrating peptides and antimicrobial peptides: How different are they? Biochem. J. 399, 1-7
    • (2006) Biochem. J. , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.R.B.3
  • 64
    • 0034713831 scopus 로고    scopus 로고
    • Action of Antimicrobial Peptides: Two-State Model
    • Huang, H. W. (2000) Action of Antimicrobial Peptides: Two-State Model Biochemistry 39, 8347-8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 65
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang, H. W. (2006) Molecular mechanism of antimicrobial peptides: The origin of cooperativity Biochim. Biophys. Acta 1758, 1292-1302
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 66
    • 34249036121 scopus 로고    scopus 로고
    • How to address CPP and AMP translocation? Methods to detect and quantify peptide internalization in vitro and in vivo
    • Troeira Henriques, S., Nuno Melo, M., and Castanho, M. A. R. B. (2007) How to address CPP and AMP translocation? Methods to detect and quantify peptide internalization in vitro and in vivo Mol. Membr. Biol. 24, 173-184
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 173-184
    • Troeira Henriques, S.1    Nuno Melo, M.2    Castanho, M.A.R.B.3
  • 67
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M. N., Ferre, R., and Castanho, M. A. R. B. (2009) Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations Nat. Rev. Microbiol. 7, 245-250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 68
    • 84903555096 scopus 로고    scopus 로고
    • Real-time Measurement of Membrane Conformational States Induced by Antimicrobial Peptides: Balance between Recovery and Lysis
    • Hall, K., Lee, T.-H., Mechler, A. I., Swann, M. J., and Aguilar, M.-I. (2014) Real-time Measurement of Membrane Conformational States Induced by Antimicrobial Peptides: Balance Between Recovery and Lysis Sci. Rep. 4, Article 5479
    • (2014) Sci. Rep. , vol.4 , pp. 5479
    • Hall, K.1    Lee, T.-H.2    Mechler, A.I.3    Swann, M.J.4    Aguilar, M.-I.5
  • 69
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-Rich Peptides Destabilize the Plasma Membrane, Consistent with a Pore Formation Translocation Mechanism of Cell-Penetrating Peptides
    • Herce, H. D., Garcia, A. E., Litt, J., Kane, R. S., Martin, P., Enrique, N., Rebolledo, A., and Milesi, V. (2009) Arginine-Rich Peptides Destabilize the Plasma Membrane, Consistent with a Pore Formation Translocation Mechanism of Cell-Penetrating Peptides Biophys. J. 97, 1917-1925
    • (2009) Biophys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6    Rebolledo, A.7    Milesi, V.8
  • 70
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • Herce, H. D. and Garcia, A. E. (2007) Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes Proc. Natl. Acad. Sci. U.S.A. 104, 20805-20810
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 71
    • 11844293998 scopus 로고    scopus 로고
    • The Cationic Cell-Penetrating Peptide CPP TAT Derived from the HIV-1 Protein TAT is Rapidly Transported into Living Fibroblasts: Optical, Biophysical, and Metabolic Evidence
    • Ziegler, A., Nervi, P., Dürrenberger, M., and Seelig, J. (2005) The Cationic Cell-Penetrating Peptide CPP TAT Derived from the HIV-1 Protein TAT Is Rapidly Transported into Living Fibroblasts: Optical, Biophysical, and Metabolic Evidence Biochemistry 44, 138-148
    • (2005) Biochemistry , vol.44 , pp. 138-148
    • Ziegler, A.1    Nervi, P.2    Dürrenberger, M.3    Seelig, J.4
  • 72
    • 0029775069 scopus 로고    scopus 로고
    • An Antimicrobial Peptide, Magainin 2, Induced Rapid Flip-Flop of Phospholipids Coupled with Pore Formation and Peptide Translocation
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1996) An Antimicrobial Peptide, Magainin 2, Induced Rapid Flip-Flop of Phospholipids Coupled with Pore Formation and Peptide Translocation Biochemistry 35, 11361-11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 74
    • 33847188537 scopus 로고    scopus 로고
    • Curvature Effect on the Structure of Phospholipid Bilayers
    • Kučerka, N., Pencer, J., Sachs, J. N., Nagle, J. F., and Katsaras, J. (2007) Curvature Effect on the Structure of Phospholipid Bilayers Langmuir 23, 1292-1299
    • (2007) Langmuir , vol.23 , pp. 1292-1299
    • Kučerka, N.1    Pencer, J.2    Sachs, J.N.3    Nagle, J.F.4    Katsaras, J.5
  • 75
    • 33845539697 scopus 로고    scopus 로고
    • Curvature and spatial organization in biological membranes
    • Parthasarathy, R. and Groves, J. T. (2006) Curvature and spatial organization in biological membranes Soft Matter 3, 24-33
    • (2006) Soft Matter , vol.3 , pp. 24-33
    • Parthasarathy, R.1    Groves, J.T.2
  • 76
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart, T., Hess, S. T., and Webb, W. W. (2003) Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension Nature 425, 821-824
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 77
    • 54149097120 scopus 로고    scopus 로고
    • Derivation of a new free energy for biological membranes
    • Deseri, L., Piccioni, M. D., and Zurlo, G. (2008) Derivation of a new free energy for biological membranes Continuum Mech. Thermodyn. 20, 255-273
    • (2008) Continuum Mech. Thermodyn. , vol.20 , pp. 255-273
    • Deseri, L.1    Piccioni, M.D.2    Zurlo, G.3
  • 78
    • 84882772243 scopus 로고    scopus 로고
    • Spontaneous tubulation of membranes and vesicles reveals membrane tension generated by spontaneous curvature
    • Lipowsky, R. (2013) Spontaneous tubulation of membranes and vesicles reveals membrane tension generated by spontaneous curvature Faraday Discuss. 161, 305-331
    • (2013) Faraday Discuss. , vol.161 , pp. 305-331
    • Lipowsky, R.1
  • 80
    • 84886721533 scopus 로고    scopus 로고
    • Antimicrobial peptides and induced membrane curvature: Geometry, coordination chemistry, and molecular engineering
    • Schmidt, N. W. and Wong, G. C. L. (2013) Antimicrobial peptides and induced membrane curvature: Geometry, coordination chemistry, and molecular engineering Curr. Opin. Solid State Mater. Sci. 17, 151-163
    • (2013) Curr. Opin. Solid State Mater. Sci. , vol.17 , pp. 151-163
    • Schmidt, N.W.1    Wong, G.C.L.2
  • 81
    • 44949104715 scopus 로고    scopus 로고
    • HIV TAT Forms Pores in Membranes by Inducing Saddle-Splay Curvature: Potential Role of Bidentate Hydrogen Bonding
    • Mishra, A., Gordon, V. D., Yang, L., Coridan, R., and Wong, G. C. L. (2008) HIV TAT Forms Pores in Membranes by Inducing Saddle-Splay Curvature: Potential Role of Bidentate Hydrogen Bonding Angew. Chem., Int. Ed. 47, 2986-2989
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 2986-2989
    • Mishra, A.1    Gordon, V.D.2    Yang, L.3    Coridan, R.4    Wong, G.C.L.5
  • 82
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-rich cell-penetrating peptides
    • Schmidt, N., Mishra, A., Lai, G. H., and Wong, G. C. L. (2010) Arginine-rich cell-penetrating peptides FEBS Lett. 584, 1806-1813
    • (2010) FEBS Lett. , vol.584 , pp. 1806-1813
    • Schmidt, N.1    Mishra, A.2    Lai, G.H.3    Wong, G.C.L.4
  • 83
    • 84860312568 scopus 로고    scopus 로고
    • Metabolic energy-independent mechanism of internalization for the cell penetrating peptide penetratin
    • Maniti, O., Blanchard, E., Trugnan, G., Lamazière, A., and Ayala-Sanmartin, J. (2012) Metabolic energy-independent mechanism of internalization for the cell penetrating peptide penetratin Int. J. Biochem. Cell Biol. 44, 869-875
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 869-875
    • Maniti, O.1    Blanchard, E.2    Trugnan, G.3    Lamazière, A.4    Ayala-Sanmartin, J.5
  • 85
    • 84903727207 scopus 로고    scopus 로고
    • The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes
    • Koller, D. and Lohner, K. (2014) The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes Biochim. Biophys. Acta 1838, 2250-2259
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2250-2259
    • Koller, D.1    Lohner, K.2
  • 86
    • 84856077925 scopus 로고    scopus 로고
    • Influence of stearyl and trifluoromethylquinoline modifications of the cell penetrating peptide TP10 on its interaction with a lipid membrane
    • Anko, M., Majhenc, J., Kogej, K., Sillard, R., Langel, U., Anderluh, G., and Zorko, M. (2012) Influence of stearyl and trifluoromethylquinoline modifications of the cell penetrating peptide TP10 on its interaction with a lipid membrane Biochim. Biophys. Acta 1818, 915-924
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 915-924
    • Anko, M.1    Majhenc, J.2    Kogej, K.3    Sillard, R.4    Langel, U.5    Anderluh, G.6    Zorko, M.7
  • 88
    • 80052468548 scopus 로고    scopus 로고
    • Transfer of Arginine into Lipid Bilayers is Nonadditive
    • MacCallum, J. L., Bennett, W. F. D., and Tieleman, D. P. (2011) Transfer of Arginine into Lipid Bilayers Is Nonadditive Biophys. J. 101, 110-117
    • (2011) Biophys. J. , vol.101 , pp. 110-117
    • Maccallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 89
    • 79954723199 scopus 로고    scopus 로고
    • On the role of anionic lipids in charged protein interactions with membranes
    • Vorobyov, I. and Allen, T. W. (2011) On the role of anionic lipids in charged protein interactions with membranes Biochim. Biophys. Acta 1808, 1673-1683
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1673-1683
    • Vorobyov, I.1    Allen, T.W.2
  • 90
    • 32244432335 scopus 로고    scopus 로고
    • Comparison of Penetratin and Other Homeodomain-Derived Cell-Penetrating Peptides: Interaction in a Membrane-Mimicking Environment and Cellular Uptake Efficiency
    • Balayssac, S., Burlina, F., Convert, O., Bolbach, G., Chassaing, G., and Lequin, O. (2006) Comparison of Penetratin and Other Homeodomain-Derived Cell-Penetrating Peptides: Interaction in a Membrane-Mimicking Environment and Cellular Uptake Efficiency Biochemistry 45, 1408-1420
    • (2006) Biochemistry , vol.45 , pp. 1408-1420
    • Balayssac, S.1    Burlina, F.2    Convert, O.3    Bolbach, G.4    Chassaing, G.5    Lequin, O.6
  • 91
    • 0032987478 scopus 로고    scopus 로고
    • Membrane Protein Folding and Stability: Physical Principles
    • White, S. H. and Wimley, W. C. (1999) Membrane Protein Folding and Stability: Physical Principles Annu. Rev. Biophys. Biomol. Struct. 28, 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 92
    • 80052730940 scopus 로고    scopus 로고
    • What Determines the Activity of Antimicrobial and Cytolytic Peptides in Model Membranes
    • Clark, K. S., Svetlovics, J., McKeown, A. N., Huskins, L., and Almeida, P. F. (2011) What Determines the Activity of Antimicrobial and Cytolytic Peptides in Model Membranes Biochemistry 50, 7919-7932
    • (2011) Biochemistry , vol.50 , pp. 7919-7932
    • Clark, K.S.1    Svetlovics, J.2    McKeown, A.N.3    Huskins, L.4    Almeida, P.F.5
  • 94
    • 84887665716 scopus 로고    scopus 로고
    • Translocation of Cationic Amphipathic Peptides across the Membranes of Pure Phospholipid Giant Vesicles
    • Wheaten, S. A., Ablan, F. D. O., Spaller, B. L., Trieu, J. M., and Almeida, P. F. (2013) Translocation of Cationic Amphipathic Peptides across the Membranes of Pure Phospholipid Giant Vesicles J. Am. Chem. Soc. 135, 16517-16525
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16517-16525
    • Wheaten, S.A.1    Ablan, F.D.O.2    Spaller, B.L.3    Trieu, J.M.4    Almeida, P.F.5
  • 95
    • 79958796013 scopus 로고    scopus 로고
    • Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening
    • Marks, J. R., Placone, J., Hristova, K., and Wimley, W. C. (2011) Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening J. Am. Chem. Soc. 133, 8995-9004
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8995-9004
    • Marks, J.R.1    Placone, J.2    Hristova, K.3    Wimley, W.C.4
  • 96
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers: The first direct observation
    • Thorén, P. E. G., Persson, D., Karlsson, M., and Nordén, B. (2000) The Antennapedia peptide penetratin translocates across lipid bilayers: The first direct observation FEBS Lett. 482, 265-268
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thorén, P.E.G.1    Persson, D.2    Karlsson, M.3    Nordén, B.4
  • 97
    • 84863844388 scopus 로고    scopus 로고
    • A Highly Charged Voltage-Sensor Helix Spontaneously Translocates across Membranes
    • He, J., Hristova, K., and Wimley, W. C. (2012) A Highly Charged Voltage-Sensor Helix Spontaneously Translocates across Membranes Angew. Chem., Int. Ed. 51, 7150-7153
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 7150-7153
    • He, J.1    Hristova, K.2    Wimley, W.C.3
  • 99
    • 80053557483 scopus 로고    scopus 로고
    • Direct Quantitation of Peptide-Mediated Protein Transport across a Droplet-Interface Bilayer
    • Huang, J., Lein, M., Gunderson, C., and Holden, M. A. (2011) Direct Quantitation of Peptide-Mediated Protein Transport across a Droplet-Interface Bilayer J. Am. Chem. Soc. 133, 15818-15821
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15818-15821
    • Huang, J.1    Lein, M.2    Gunderson, C.3    Holden, M.A.4
  • 100
    • 0041843710 scopus 로고    scopus 로고
    • Charge-Dependent Translocation of the Trojan Peptide Penetratin across Lipid Membranes
    • Binder, H. and Lindblom, G. (2003) Charge-Dependent Translocation of the Trojan Peptide Penetratin across Lipid Membranes Biophys. J. 85, 982-995
    • (2003) Biophys. J. , vol.85 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 101
    • 84877711951 scopus 로고    scopus 로고
    • Direct translocation of cell-penetrating peptides in liposomes: A combined mass spectrometry quantification and fluorescence detection study
    • Walrant, A., Matheron, L., Cribier, S., Chaignepain, S., Jobin, M.-L., Sagan, S., and Alves, I. D. (2013) Direct translocation of cell-penetrating peptides in liposomes: A combined mass spectrometry quantification and fluorescence detection study Anal. Biochem. 438, 1-10
    • (2013) Anal. Biochem. , vol.438 , pp. 1-10
    • Walrant, A.1    Matheron, L.2    Cribier, S.3    Chaignepain, S.4    Jobin, M.-L.5    Sagan, S.6    Alves, I.D.7
  • 102
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans
    • Ziegler, A. (2008) Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans Adv. Drug Delivery Rev. 60, 580-597
    • (2008) Adv. Drug Delivery Rev. , vol.60 , pp. 580-597
    • Ziegler, A.1
  • 103
    • 34447626465 scopus 로고    scopus 로고
    • A Simple Fluorescence-Spectroscopic Membrane Translocation Assay
    • Keller, S., Böthe, M., Bienert, M., Dathe, M., and Blume, A. (2007) A Simple Fluorescence-Spectroscopic Membrane Translocation Assay ChemBioChem 8, 546-552
    • (2007) ChemBioChem , vol.8 , pp. 546-552
    • Keller, S.1    Böthe, M.2    Bienert, M.3    Dathe, M.4    Blume, A.5
  • 104
    • 0029802678 scopus 로고    scopus 로고
    • Conformational and Associative Behaviours of the Third Helix of Antennapedia Homeodomain in Membrane-Mimetic Environments
    • Berlose, J.-P., Convert, O., Derossi, D., Brunissen, A., and Chassaing, G. (1996) Conformational and Associative Behaviours of the Third Helix of Antennapedia Homeodomain in Membrane-Mimetic Environments Eur. J. Biochem. 242, 372-386
    • (1996) Eur. J. Biochem. , vol.242 , pp. 372-386
    • Berlose, J.-P.1    Convert, O.2    Derossi, D.3    Brunissen, A.4    Chassaing, G.5
  • 105
    • 0027287709 scopus 로고
    • Import of a mitochondrial presequence into protein-free phospholipid vesicles
    • Maduke, M. and Roise, D. (1993) Import of a mitochondrial presequence into protein-free phospholipid vesicles Science 260, 364-367
    • (1993) Science , vol.260 , pp. 364-367
    • Maduke, M.1    Roise, D.2
  • 106
    • 0345275894 scopus 로고    scopus 로고
    • Penetratin and Related Cell-Penetrating Cationic Peptides Can Translocate Across Lipid Bilayers in the Presence of a Transbilayer Potential
    • Terrone, D., Sang, S. L. W., Roudaia, L., and Silvius, J. R. (2003) Penetratin and Related Cell-Penetrating Cationic Peptides Can Translocate Across Lipid Bilayers in the Presence of a Transbilayer Potential Biochemistry 42, 13787-13799
    • (2003) Biochemistry , vol.42 , pp. 13787-13799
    • Terrone, D.1    Sang, S.L.W.2    Roudaia, L.3    Silvius, J.R.4
  • 107
    • 3343017389 scopus 로고    scopus 로고
    • Consequences of Nonlytic Membrane Perturbation to the Translocation of the Cell Penetrating Peptide Pep-1 in Lipidic Vesicles
    • Henriques, S. T. and Castanho, M. A. R. B. (2004) Consequences of Nonlytic Membrane Perturbation to the Translocation of the Cell Penetrating Peptide Pep-1 in Lipidic Vesicles Biochemistry 43, 9716-9724
    • (2004) Biochemistry , vol.43 , pp. 9716-9724
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 108
    • 23644454418 scopus 로고    scopus 로고
    • Re-evaluating the role of strongly charged sequences in amphipathic cell-penetrating peptides: A fluorescence study using Pep-1
    • Henriques, S. T., Costa, J., and Castanho, M. A. R. B. (2005) Re-evaluating the role of strongly charged sequences in amphipathic cell-penetrating peptides: A fluorescence study using Pep-1 FEBS Lett. 579, 4498-4502
    • (2005) FEBS Lett. , vol.579 , pp. 4498-4502
    • Henriques, S.T.1    Costa, J.2    Castanho, M.A.R.B.3
  • 109
    • 23044485527 scopus 로고    scopus 로고
    • Translocation of β-Galactosidase Mediated by the Cell-Penetrating Peptide Pep-1 into Lipid Vesicles and Human HeLa Cells is Driven by Membrane Electrostatic Potential
    • Henriques, S. T., Costa, J., and Castanho, M. A. R. B. (2005) Translocation of β-Galactosidase Mediated by the Cell-Penetrating Peptide Pep-1 into Lipid Vesicles and Human HeLa Cells Is Driven by Membrane Electrostatic Potential Biochemistry 44, 10189-10198
    • (2005) Biochemistry , vol.44 , pp. 10189-10198
    • Henriques, S.T.1    Costa, J.2    Castanho, M.A.R.B.3
  • 110
    • 33746853554 scopus 로고    scopus 로고
    • Real-Time Transmembrane Translocation of Penetratin Driven by Light-Generated Proton Pumping
    • Björklund, J., Biverståhl, H., Gräslund, A., Mäler, L., and Brzezinski, P. (2006) Real-Time Transmembrane Translocation of Penetratin Driven by Light-Generated Proton Pumping Biophys. J. 91, L29-L31
    • (2006) Biophys. J. , vol.91 , pp. 29-L31
    • Björklund, J.1    Biverståhl, H.2    Gräslund, A.3    Mäler, L.4    Brzezinski, P.5
  • 111
    • 84555175975 scopus 로고    scopus 로고
    • Liposome Model Systems to Study the Endosomal Escape of Cell-Penetrating Peptides: Transport across Phospholipid Membranes Induced by a Proton Gradient
    • Madani, F., Perálvarez-Marín, A., and Gräslund, A. (2011) Liposome Model Systems to Study the Endosomal Escape of Cell-Penetrating Peptides: Transport across Phospholipid Membranes Induced by a Proton Gradient J. Drug Delivery 897592
    • (2011) J. Drug Delivery , pp. 897592
    • Madani, F.1    Perálvarez-Marín, A.2    Gräslund, A.3
  • 112
    • 27744493266 scopus 로고    scopus 로고
    • Modeling the Endosomal Escape of Cell-Penetrating Peptides: Transmembrane pH Gradient Driven Translocation across Phospholipid Bilayers
    • Magzoub, M., Pramanik, A., and Gräslund, A. (2005) Modeling the Endosomal Escape of Cell-Penetrating Peptides: Transmembrane pH Gradient Driven Translocation across Phospholipid Bilayers Biochemistry 44, 14890-14897
    • (2005) Biochemistry , vol.44 , pp. 14890-14897
    • Magzoub, M.1    Pramanik, A.2    Gräslund, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.