메뉴 건너뛰기




Volumn 29, Issue 49, 2013, Pages 15336-15349

Dynamic measurements of membrane insertion potential of synthetic cell penetrating peptides

Author keywords

[No Author keywords available]

Indexed keywords

CELL PENETRATING PEPTIDES (CPPS); CELL-PENETRATING PEPTIDE; DRUG DELIVERY APPLICATIONS; HYDROPHOBIC AMINO ACIDS; HYDROPHOBIC PROPERTIES; INTRACELLULAR DRUG DELIVERY; MEMBRANE REORGANIZATION; PHOSPHOLIPID MONOLAYERS;

EID: 84890362716     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la403370p     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 84863768475 scopus 로고    scopus 로고
    • Effects of Tryptophan Content and Backbone Spacing on the Uptake Efficiency of Cell-Penetrating Peptides
    • Rydberg, H. A.; Matson, M.; Åmand, H. L.; Esbjörner, E. K.; Nordén, B. Effects of Tryptophan Content and Backbone Spacing on the Uptake Efficiency of Cell-Penetrating Peptides Biochemistry 2012, 51 (27) 5531-5539
    • (2012) Biochemistry , vol.51 , Issue.27 , pp. 5531-5539
    • Rydberg, H.A.1    Matson, M.2    Åmand, H.L.3    Esbjörner, E.K.4    Nordén, B.5
  • 2
    • 77951956539 scopus 로고    scopus 로고
    • Cellular endocytosis and gene delivery
    • Ziello, J. E.; Huang, Y.; Jovin, I. S. Cellular Endocytosis and Gene Delivery Mol. Med. 2010, 16 (5-6) 222
    • (2010) Mol. Med. , vol.16 , Issue.56 , pp. 222
    • Ziello, J.E.1    Huang, Y.2    Jovin, I.S.3
  • 3
    • 79955592687 scopus 로고    scopus 로고
    • Can Non-Viral technologies knockdown the barriers to siRNA delivery and achieve the next generation of cancer therapeutics?
    • Guo, J.; Bourre, L.; Soden, D. M.; O'Sullivan, G. C.; O'Driscoll, C. Can Non-Viral Technologies Knockdown the Barriers to siRNA Delivery and Achieve the Next Generation of Cancer Therapeutics? Biotechnol. Adv. 2011, 29 (4) 402-417
    • (2011) Biotechnol. Adv. , vol.29 , Issue.4 , pp. 402-417
    • Guo, J.1    Bourre, L.2    Soden, D.M.3    O'Sullivan, G.C.4    O'Driscoll, C.5
  • 5
    • 34548760754 scopus 로고    scopus 로고
    • Interactions of cell penetrating peptide tat with model membranes: A biophysical study
    • Dennison, S. R.; Baker, R. D.; Nicholl, I. D.; Phoenix, D. A. Interactions of Cell Penetrating Peptide Tat with Model Membranes: a Biophysical Study Biochem. Biophys. Res. Commun. 2007, 363 (1) 178-182
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , Issue.1 , pp. 178-182
    • Dennison, S.R.1    Baker, R.D.2    Nicholl, I.D.3    Phoenix, D.A.4
  • 7
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the Use of Cell-Penetrating Peptides for medical and biological Applications
    • Fonseca, S. B.; Pereira, M. P.; Kelley, S. O. Recent Advances in the Use of Cell-Penetrating Peptides for Medical and Biological Applications Adv. Drug Delivery Rev. 2009, 61 (11) 953-964
    • (2009) Adv. Drug Delivery Rev. , vol.61 , Issue.11 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 8
    • 84878715268 scopus 로고    scopus 로고
    • Noncovalently Associated Cell-Penetrating Peptides for Gene Delivery Applications
    • Alhakamy, N. A.; Nigatu, A. S.; Berkland, C. J.; Ramsey, J. D. Noncovalently Associated Cell-Penetrating Peptides for Gene Delivery Applications Ther. Delivery 2013, 4 (6) 741-757
    • (2013) Ther. Delivery , vol.4 , Issue.6 , pp. 741-757
    • Alhakamy, N.A.1    Nigatu, A.S.2    Berkland, C.J.3    Ramsey, J.D.4
  • 9
    • 79952197259 scopus 로고    scopus 로고
    • Classes and prediction of Cell-Penetrating Peptides
    • Springer; New York
    • Lindgren, M.; Langel, Ü. Classes and Prediction of Cell-Penetrating Peptides. In Cell-Penetrating Peptides; Springer; New York, 2011; pp 3-19.
    • (2011) Cell-Penetrating Peptides , pp. 3-19
    • Lindgren, M.1    Langel, Ü.2
  • 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.; Rothbard, J. B. The Design, Synthesis, and Evaluation of Molecules That Enable or Enhance Cellular Uptake: Peptoid Molecular Transporters Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (24) 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.24 , 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
  • 11
    • 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.; Prochiantz, A. Cell Internalization of the Third Helix of the Antennapedia Homeodomain Is Receptor-Independent J. Biol. Chem. 1996, 271 (30) 18188-18193
    • (1996) J. Biol. Chem. , vol.271 , Issue.30 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 12
    • 77949890248 scopus 로고    scopus 로고
    • Cell Penetrating Peptides: Overview and Applications to the Delivery of Oligonucleotides
    • Hassane, F. S.; Saleh, A.; Abes, R.; Gait, M.; Lebleu, B. Cell Penetrating Peptides: Overview and Applications to the Delivery of Oligonucleotides Cell. Mol. Life Sci. 2010, 67 (5) 715-726
    • (2010) Cell. Mol. Life Sci. , vol.67 , Issue.5 , pp. 715-726
    • Hassane, F.S.1    Saleh, A.2    Abes, R.3    Gait, M.4    Lebleu, B.5
  • 13
    • 17144373997 scopus 로고    scopus 로고
    • Membrane Destabilizing Properties of Cell-Penetrating Peptides
    • Thorén, P. E.; Persson, D.; Lincoln, P.; Nordén, B. Membrane Destabilizing Properties of Cell-Penetrating Peptides Biophys, Chem. 2005, 114 (2) 169-179
    • (2005) Biophys, Chem. , vol.114 , Issue.2 , pp. 169-179
    • Thorén, P.E.1    Persson, D.2    Lincoln, P.3    Nordén, B.4
  • 14
    • 0036159271 scopus 로고    scopus 로고
    • Different Mechanisms for Cellular Internalization of the HIV-1 Tat-Derived Cell Penetrating Peptide and Recombinant Proteins Fused to Tat
    • Silhol, M.; Tyagi, M.; Giacca, M.; Lebleu, B.; Vivès, E. Different Mechanisms for Cellular Internalization of the HIV-1 Tat-Derived Cell Penetrating Peptide and Recombinant Proteins Fused to Tat Eur. J. Biochem. 2002, 269 (2) 494-501
    • (2002) Eur. J. Biochem. , vol.269 , Issue.2 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.4    Vivès, E.5
  • 15
    • 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.; Langel, Ü.; Gräslund, A. Interaction and Structure Induction of Cell-Penetrating Peptides in the Presence of Phospholipid Vesicles Biochim. Biophys. Acta (BBA)-Biomembr. 2001, 1512 (1) 77-89
    • (2001) Biochim. Biophys. Acta (BBA)-Biomembr. , vol.1512 , Issue.1 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson, L.3    Langel, Ü.4    Gräslund, A.5
  • 16
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-Rich Cell-Penetrating Peptides
    • Schmidt, N.; Mishra, A.; Lai, G. H.; Wong, G. C. Arginine-Rich Cell-Penetrating Peptides FEBS Lett. 2010, 584 (9) 1806-13
    • (2010) FEBS Lett. , vol.584 , Issue.9 , pp. 1806-1813
    • Schmidt, N.1    Mishra, A.2    Lai, G.H.3    Wong, G.C.4
  • 17
    • 68849106030 scopus 로고    scopus 로고
    • Interaction of Poly (l -arginine) with Negatively Charged DPPG Membranes: Calorimetric and Monolayer Studies
    • Schwieger, C.; Blume, A. Interaction of Poly (l -arginine) with Negatively Charged DPPG Membranes: Calorimetric and Monolayer Studies Biomacromolecules 2009, 10 (8) 2152-2161
    • (2009) Biomacromolecules , vol.10 , Issue.8 , pp. 2152-2161
    • Schwieger, C.1    Blume, A.2
  • 18
    • 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.; Seelig, J. Binding of Oligoarginine to Membrane Lipids and Heparan Sulfate: Structural and Thermodynamic Characterization of a Cell-Penetrating Peptide Biochemistry 2005, 44 (7) 2692-2702
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2692-2702
    • Gonçalves, E.1    Kitas, E.2    Seelig, J.3
  • 19
    • 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.; Lebleu, B. A Truncated HIV-1 Tat Protein Basic Domain Rapidly Translocates through the Plasma Membrane and Accumulates in the Cell Nucleus J. Biol. Chem. 1997, 272 (25) 16010-16017
    • (1997) J. Biol. Chem. , vol.272 , Issue.25 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 20
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine Enters Cells More Efficiently Than Other Polycationic Homopolymers
    • Mitchell, D.; Steinman, L.; Kim, D.; Fathman, C.; Rothbard, J. Polyarginine Enters Cells More Efficiently Than Other Polycationic Homopolymers J. Pept. Res. 2000, 56 (5) 318-325
    • (2000) J. Pept. Res. , vol.56 , Issue.5 , pp. 318-325
    • Mitchell, D.1    Steinman, L.2    Kim, D.3    Fathman, C.4    Rothbard, J.5
  • 23
    • 0037103242 scopus 로고    scopus 로고
    • Arginine-Rich Molecular Transporters for Drug Delivery: Role of Backbone Spacing in Cellular Uptake
    • Rothbard, J. B.; Kreider, E.; VanDeusen, C. L.; Wright, L.; Wylie, B. L.; Wender, P. A. Arginine-Rich Molecular Transporters for Drug Delivery: Role of Backbone Spacing in Cellular Uptake J. Med. Chem. 2002, 45 (17) 3612-3618
    • (2002) J. Med. Chem. , vol.45 , Issue.17 , pp. 3612-3618
    • Rothbard, J.B.1    Kreider, E.2    Vandeusen, C.L.3    Wright, L.4    Wylie, B.L.5    Wender, P.A.6
  • 24
    • 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.; Saito, H. Physicochemical Mechanism for the Enhanced Ability of Lipid Membrane Penetration of Polyarginine Langmuir 2011, 27 (11) 7099-7107
    • (2011) Langmuir , vol.27 , Issue.11 , pp. 7099-7107
    • Takechi, Y.1    Yoshii, H.2    Tanaka, M.3    Kawakami, T.4    Aimoto, S.5    Saito, H.6
  • 25
    • 0141942114 scopus 로고    scopus 로고
    • Membrane Permeability Commonly Shared among Arginine-Rich Peptides
    • Futaki, S.; Goto, S.; Sugiura, Y. Membrane Permeability Commonly Shared among Arginine-Rich Peptides J. Mol. Recognit. 2003, 16 (5) 260-264
    • (2003) J. Mol. Recognit. , vol.16 , Issue.5 , pp. 260-264
    • Futaki, S.1    Goto, S.2    Sugiura, Y.3
  • 27
    • 39149103400 scopus 로고    scopus 로고
    • The design of guanidinium-rich transporters and their internalization mechanisms
    • Wender, P. A.; Galliher, W. C.; Goun, E. A.; Jones, L. R.; Pillow, T. H. The design of guanidinium-rich transporters and their internalization mechanisms Adv. Drug Delivery Rev. 2008, 60 (4) 452-472
    • (2008) Adv. Drug Delivery Rev. , vol.60 , Issue.4 , pp. 452-472
    • Wender, P.A.1    Galliher, W.C.2    Goun, E.A.3    Jones, L.R.4    Pillow, T.H.5
  • 28
    • 67349143369 scopus 로고    scopus 로고
    • The Affinity of Two Antimicrobial Peptides Derived from Bovine Milk Proteins for Model Lipid Membranes
    • Barzyk, W.; Campagna, S.; WieÌ̈cław, K.; Korchowiec, B.; Rogalska, E. The Affinity of Two Antimicrobial Peptides Derived from Bovine Milk Proteins for Model Lipid Membranes Colloids Surf., A 2009, 343 (1) 104-110
    • (2009) Colloids Surf., A , vol.343 , Issue.1 , pp. 104-110
    • Barzyk, W.1    Campagna, S.2    Wieì̈cław, K.3    Korchowiec, B.4    Rogalska, E.5
  • 29
    • 0033179620 scopus 로고    scopus 로고
    • Lipid Monolayers: Why Use Half a Membrane to Characterize Protein-Membrane Interactions?
    • Brockman, H. Lipid Monolayers: Why Use Half a Membrane to Characterize Protein-Membrane Interactions? Curr. Opin. Struct. Biol. 1999, 9 (4) 438-443
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , Issue.4 , pp. 438-443
    • Brockman, H.1
  • 31
    • 12144267932 scopus 로고    scopus 로고
    • Langmuir Monolayers to Study Interactions at Model Membrane Surfaces
    • Brezesinski, G.; Möhwald, H. Langmuir Monolayers to Study Interactions at Model Membrane Surfaces Adv. Colloid Interface Sci. 2003, 100, 563-584
    • (2003) Adv. Colloid Interface Sci. , vol.100 , pp. 563-584
    • Brezesinski, G.1    Möhwald, H.2
  • 32
    • 70350049076 scopus 로고    scopus 로고
    • Biophysical Interactions with Model Lipid Membranes: Applications in Drug Discovery and Drug Delivery
    • Peetla, C.; Stine, A.; Labhasetwar, V. Biophysical Interactions with Model Lipid Membranes: Applications in Drug Discovery and Drug Delivery Mol. Pharmaceutics 2009, 6 (5) 1264-1276
    • (2009) Mol. Pharmaceutics , vol.6 , Issue.5 , pp. 1264-1276
    • Peetla, C.1    Stine, A.2    Labhasetwar, V.3
  • 33
    • 33751225343 scopus 로고    scopus 로고
    • Comparison of Paclitaxel Penetration in Normal and Cancerous Cervical Model Monolayer Membranes
    • Preetha, A.; Huilgol, N.; Banerjee, R. Comparison of Paclitaxel Penetration in Normal and Cancerous Cervical Model Monolayer Membranes Colloids Surf., B 2006, 53 (2) 179-186
    • (2006) Colloids Surf., B , vol.53 , Issue.2 , pp. 179-186
    • Preetha, A.1    Huilgol, N.2    Banerjee, R.3
  • 34
    • 0016717097 scopus 로고
    • Relation between Various Phospholipase Actions on Human Red Cell Membranes and the Interfacial Phospholipid Pressure in Monolayers
    • Demel, R.; Geurts van Kessel, W.; Zwaal, R.; Roelofsen, B.; Van Deenen, L. Relation between Various Phospholipase Actions on Human Red Cell Membranes and the Interfacial Phospholipid Pressure in Monolayers Biochim. Biophys. Acta (BBA)-Biomembr. 1975, 406 (1) 97-107
    • (1975) Biochim. Biophys. Acta (BBA)-Biomembr. , vol.406 , Issue.1 , pp. 97-107
    • Demel, R.1    Geurts Van Kessel, W.2    Zwaal, R.3    Roelofsen, B.4    Van Deenen, L.5
  • 35
    • 0018795945 scopus 로고
    • A Comparative Study of the Phase Transitions of Phospholipid Bilayers and Monolayers
    • Blume, A. A Comparative Study of the Phase Transitions of Phospholipid Bilayers and Monolayers Biochim. Biophys. Acta (BBA)-Biomembr. 1979, 557 (1) 32-44
    • (1979) Biochim. Biophys. Acta (BBA)-Biomembr. , vol.557 , Issue.1 , pp. 32-44
    • Blume, A.1
  • 38
    • 71749092534 scopus 로고    scopus 로고
    • Translocation and Endocytosis for Cell-Penetrating Peptide Internalization
    • Jiao, C.-Y.; Delaroche, D.; Burlina, F.; Alves, I. D.; Chassaing, G.; Sagan, S. Translocation and Endocytosis for Cell-Penetrating Peptide Internalization J. Biol. Chem. 2009, 284 (49) 33957-33965
    • (2009) J. Biol. Chem. , vol.284 , Issue.49 , pp. 33957-33965
    • Jiao, C.-Y.1    Delaroche, D.2    Burlina, F.3    Alves, I.D.4    Chassaing, G.5    Sagan, S.6
  • 39
    • 23944483437 scopus 로고    scopus 로고
    • Cell-Penetrating Peptides: Tools for Intracellular Delivery of Therapeutics
    • Deshayes, S.; Morris, M.; Divita, G.; Heitz, F. Cell-Penetrating Peptides: Tools for Intracellular Delivery of Therapeutics Cell. Mol. Life Sci. 2005, 62 (16) 1839-1849
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.16 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.2    Divita, G.3    Heitz, F.4
  • 40
    • 84890367503 scopus 로고    scopus 로고
    • Structure and Dynamics of the Two Amphipathic Arginine-Rich Peptides RW9 and RL9 in a Lipid Environment Investigated by Solid-State NMR and MD Simulations
    • Witte, K.; Olausson, B. E.; Walrant, A.; Alves, I. D.; Vogel, A. Structure and Dynamics of the Two Amphipathic Arginine-Rich Peptides RW9 and RL9 in a Lipid Environment Investigated by Solid-State NMR and MD Simulations. Biochim. Biophys. Acta (BBA)-Biomembr. 2012.
    • (2012) Biochim. Biophys. Acta (BBA)-Biomembr.
    • Witte, K.1    Olausson, B.E.2    Walrant, A.3    Alves, I.D.4    Vogel, A.5
  • 41
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of Cationic Antimicrobial Peptides with Model Membranes
    • Zhang, L.; Rozek, A.; Hancock, R. E. Interaction of Cationic Antimicrobial Peptides with Model Membranes J. Biol. Chem. 2001, 276 (38) 35714-35722
    • (2001) J. Biol. Chem. , vol.276 , Issue.38 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3
  • 42
    • 33746191398 scopus 로고    scopus 로고
    • Anion Hopping of (and on) Functional Oligoarginines: From Chloroform to Cells
    • Sakai, N.; Futaki, S.; Matile, S. Anion Hopping of (and on) Functional Oligoarginines: From Chloroform to Cells Soft Matter 2006, 2 (8) 636-641
    • (2006) Soft Matter , vol.2 , Issue.8 , pp. 636-641
    • Sakai, N.1    Futaki, S.2    Matile, S.3
  • 43
    • 46349095610 scopus 로고    scopus 로고
    • Relationships between the Orientation and the Structural Properties of Peptides and Their Membrane Interactions
    • Lins, L.; Decaffmeyer, M.; Thomas, A.; Brasseur, R. Relationships between the Orientation and the Structural Properties of Peptides and Their Membrane Interactions Biochim. Biophys. Acta (BBA)-Biomembr. 2008, 1778 (7) 1537-1544
    • (2008) Biochim. Biophys. Acta (BBA)-Biomembr. , vol.1778 , Issue.7 , pp. 1537-1544
    • Lins, L.1    Decaffmeyer, M.2    Thomas, A.3    Brasseur, R.4
  • 45
    • 20444403719 scopus 로고    scopus 로고
    • Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides
    • Maiolo, J. R.; Ferrer, M.; Ottinger, E. A. Effects of cargo molecules on the cellular uptake of arginine-rich cell-penetrating peptides Biochimica et Biophysica Acta (BBA)-Biomembranes 2005, 1712 (2) 161-172
    • (2005) Biochimica et Biophysica Acta (BBA)-Biomembranes , vol.1712 , Issue.2 , pp. 161-172
    • Maiolo, J.R.1    Ferrer, M.2    Ottinger, E.A.3
  • 46
    • 0032552880 scopus 로고    scopus 로고
    • The Preference of Tryptophan for Membrane Interfaces
    • Yau, W.-M.; Wimley, W. C.; Gawrisch, K.; White, S. H. The Preference of Tryptophan for Membrane Interfaces Biochemistry 1998, 37 (42) 14713-14718
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 47
    • 0027499143 scopus 로고
    • Non-Random Distribution of Amino Acids in the Transmembrane Segments of Human Type i Single Span Membrane Proteins
    • Landolt-Marticorena, C.; Williams, K. A.; Deber, C. M.; Reithmeier, R. A. Non-Random Distribution of Amino Acids in the Transmembrane Segments of Human Type I Single Span Membrane Proteins J. Mol. Biol. 1993, 229 (3) 602-608
    • (1993) J. Mol. Biol. , vol.229 , Issue.3 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 48
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-Rich Peptides: An Abundant Source of Membrane-Permeable Peptides Having Potential As Carriers for Intracellular Protein Delivery
    • 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 (8) 5836-5840
    • (2001) J. Biol. Chem. , vol.276 , Issue.8 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 49
    • 84873428784 scopus 로고    scopus 로고
    • Tryptophan within Basic Peptide Sequences Triggers Glycosaminoglycan- Dependent Endocytosis
    • Bechara, C.; Pallerla, M.; Zaltsman, Y.; Burlina, F.; Alves, I. D.; Lequin, O.; Sagan, S. Tryptophan within Basic Peptide Sequences Triggers Glycosaminoglycan-Dependent Endocytosis FASEB J. 2013, 27 (2) 738-749
    • (2013) FASEB J. , vol.27 , Issue.2 , pp. 738-749
    • Bechara, C.1    Pallerla, M.2    Zaltsman, Y.3    Burlina, F.4    Alves, I.D.5    Lequin, O.6    Sagan, S.7
  • 50
    • 75649122919 scopus 로고    scopus 로고
    • A Langmuir Monolayer Study of the Interaction of E1 (145- 162) Hepatitis G Virus Peptide with Phospholipid Membranes
    • Sánchez-Martín, M. J. s.; Haro, I.; Alsina, M. A.; Busquets, M. A.; Pujol, M. A Langmuir Monolayer Study of the Interaction of E1 (145- 162) Hepatitis G Virus Peptide with Phospholipid Membranes J. Phys. Chem. B 2009, 114 (1) 448-456
    • (2009) J. Phys. Chem. B , vol.114 , Issue.1 , pp. 448-456
    • Sánchez-Martín, M.J.S.1    Haro, I.2    Alsina, M.A.3    Busquets, M.A.4    Pujol, M.5
  • 51
    • 49649089563 scopus 로고    scopus 로고
    • Surface Behavior and Peptide- Lipid Interactions of the Cyclic Neuropeptide Melanin Concentrating Hormone
    • Varas, M.; Sánchez-Borzone, M.; Sánchez, J. M.; Barioglio, S. R. d.; Perillo, M. a. A. Surface Behavior and Peptide- Lipid Interactions of the Cyclic Neuropeptide Melanin Concentrating Hormone J. Phys. Chem. B 2008, 112 (24) 7330-7337
    • (2008) J. Phys. Chem. B , vol.112 , Issue.24 , pp. 7330-7337
    • Varas, M.1    Sánchez-Borzone, M.2    Sánchez, J.M.3    Barioglio, S.R.D.4    Perillo, A.M.A.5
  • 52
    • 33846393880 scopus 로고    scopus 로고
    • Penetration of Surfactin into Phospholipid Monolayers: Nanoscale Interfacial Organization
    • Eeman, M.; Berquand, A.; Dufrene, Y.; Paquot, M.; Dufour, S.; Deleu, M. Penetration of Surfactin into Phospholipid Monolayers: Nanoscale Interfacial Organization Langmuir 2006, 22 (26) 11337-11345
    • (2006) Langmuir , vol.22 , Issue.26 , pp. 11337-11345
    • Eeman, M.1    Berquand, A.2    Dufrene, Y.3    Paquot, M.4    Dufour, S.5    Deleu, M.6
  • 53
    • 65249097290 scopus 로고    scopus 로고
    • A Kinetic Model for β-Amyloid Adsorption at the Air/Solution Interface and Its Implication to the β-Amyloid Aggregation Process
    • Jiang, D.; Dinh, K. L.; Ruthenburg, T. C.; Zhang, Y.; Su, L.; Land, D. P.; Zhou, F. A Kinetic Model for β-Amyloid Adsorption at the Air/Solution Interface and Its Implication to the β-Amyloid Aggregation Process J. Phys. Chem. B 2009, 113 (10) 3160-3168
    • (2009) J. Phys. Chem. B , vol.113 , Issue.10 , pp. 3160-3168
    • Jiang, D.1    Dinh, K.L.2    Ruthenburg, T.C.3    Zhang, Y.4    Su, L.5    Land, D.P.6    Zhou, F.7
  • 54
    • 0032682964 scopus 로고    scopus 로고
    • Viral synthetic peptide interactions with membranes: A monolayer study
    • Sospedra, P.; Haro, I.; Alsina, M.; Reig, F.; Mestres, C. Viral synthetic peptide interactions with membranes: A monolayer study Langmuir 1999, 15 (16) 5303-5308
    • (1999) Langmuir , vol.15 , Issue.16 , pp. 5303-5308
    • Sospedra, P.1    Haro, I.2    Alsina, M.3    Reig, F.4    Mestres, C.5
  • 55
    • 3042546066 scopus 로고    scopus 로고
    • Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin
    • Ambroggio, E. E.; Separovic, F.; Bowie, J.; Fidelio, G. D. Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin Biochim. Biophys. Acta (BBA)-Biomembr. 2004, 1664 (1) 31-37
    • (2004) Biochim. Biophys. Acta (BBA)-Biomembr. , vol.1664 , Issue.1 , pp. 31-37
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.3    Fidelio, G.D.4
  • 56
    • 79959935354 scopus 로고    scopus 로고
    • Analysis of kinetic Langmuir model. Part I: Integrated kinetic Langmuir equation (IKL): A new complete analytical solution of the Langmuir rate equation
    • Marczewski, A. W. Analysis of kinetic Langmuir model. Part I: integrated kinetic Langmuir equation (IKL): a new complete analytical solution of the Langmuir rate equation Langmuir 2010, 26 (19) 15229-15238
    • (2010) Langmuir , vol.26 , Issue.19 , pp. 15229-15238
    • Marczewski, A.W.1
  • 57
    • 0031394868 scopus 로고    scopus 로고
    • Conformation and interactions of bioactive peptides from insect venoms: The bombolitins
    • Peggion, E.; Mammi, S.; Schievano, E. Conformation and interactions of bioactive peptides from insect venoms: The bombolitins Peptide Science 1997, 43 (6) 419-431
    • (1997) Peptide Science , vol.43 , Issue.6 , pp. 419-431
    • Peggion, E.1    Mammi, S.2    Schievano, E.3
  • 58
    • 0029208394 scopus 로고
    • Two-dimensional assembly formation of hydrophobic helical peptides at the air/water interface: Fluorescence microscopic study
    • Fujita, K.; Kimura, S.; Imanishi, Y.; Rump, E.; Ringsdorf, H. Two-dimensional assembly formation of hydrophobic helical peptides at the air/water interface: fluorescence microscopic study Langmuir 1995, 11 (1) 253-258
    • (1995) Langmuir , vol.11 , Issue.1 , pp. 253-258
    • Fujita, K.1    Kimura, S.2    Imanishi, Y.3    Rump, E.4    Ringsdorf, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.