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Volumn 89, Issue 6, 2005, Pages 4056-4066

Membrane surface-associated helices promote lipid interactions and cellular uptake of human calcitonin-derived cell penetrating peptides

Author keywords

[No Author keywords available]

Indexed keywords

5 DOXYLSTEAREATE; CALCITONIN DERIVATIVE; DODECYLPHOSPHORYLCHOLINE; GREEN FLUORESCENT PROTEIN; HUMAN CALCITONIN DERIVED CELL PENETRATING PEPTIDE[9-32]; LIPID; LIPOSOME; MUTANT PROTEIN; PEPTIDE A23; PEPTIDE W30; PLASMID DNA; STEARIC ACID; UNCLASSIFIED DRUG;

EID: 28444464129     PISSN: 00063495     EISSN: 00063495     Source Type: Journal    
DOI: 10.1529/biophysj.105.068692     Document Type: Article
Times cited : (36)

References (69)
  • 1
    • 0037592877 scopus 로고    scopus 로고
    • Insight into the mechanism of the peptide-based gene delivery system MPG: Implications for delivery of siRNA into mammalian cells
    • Simeoni, F., M. C. Morris, F. Heitz, and G. Divita. 2003. Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. Nucleic Acids Res. 31:2717-2724.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2717-2724
    • Simeoni, F.1    Morris, M.C.2    Heitz, F.3    Divita, G.4
  • 2
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris, M. C., P. Vidal, L. Chaloin, F. Heitz, and G. Divita. 1997. A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res. 25:2730-2736.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 3
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris, M. C., J. Depollier, J. Mery, F. Heitz, and G. Divita. 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
  • 5
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi, D., G. Chassaing, and A. Prochiantz. 1998. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 8:84-87.
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 6
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder, E. L., and S. F. Dowdy. 2004. Cell penetrating peptides in drug delivery. Pharm. Res. 21:389-393.
    • (2004) Pharm. Res. , vol.21 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 7
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • Schwarze, S. R., K. A. Hruska, and S. F. Dowdy. 2000. Protein transduction: unrestricted delivery into all cells? Trends Cell Biol. 10:290-295.
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 8
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers-the first direct observation
    • Thoren, P. E., D. Persson, M. Karlsson, and B. Norden. 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
    • Thoren, P.E.1    Persson, D.2    Karlsson, M.3    Norden, B.4
  • 9
    • 0030273590 scopus 로고    scopus 로고
    • Getting hydrophilic compounds into cells: Lessons from homeopeptides
    • Prochiantz, A. 1996. Getting hydrophilic compounds into cells: lessons from homeopeptides. Curr. Opin. Neurobiol. 6:629-634.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 629-634
    • Prochiantz, A.1
  • 10
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains
    • Lundberg, M., S. Wikstrom, and M. Johansson. 2003. Cell surface adherence and endocytosis of protein transduction domains. Mol. Ther. 8:143-150.
    • (2003) Mol. Ther. , vol.8 , pp. 143-150
    • Lundberg, M.1    Wikstrom, S.2    Johansson, M.3
  • 11
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J. S., R. V. Stan, and S. F. Dowdy. 2004. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10:310-315.
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 14
    • 3843092828 scopus 로고    scopus 로고
    • Chances and pitfalls of cell penetrating peptides for cellular drug delivery
    • Trehin, R., and H. P. Merkle. 2004. Chances and pitfalls of cell penetrating peptides for cellular drug delivery. Eur. J. Pharm. Biopharm. 58:209-223.
    • (2004) Eur. J. Pharm. Biopharm. , vol.58 , pp. 209-223
    • Trehin, R.1    Merkle, H.P.2
  • 16
    • 0035078052 scopus 로고    scopus 로고
    • Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity
    • Drin, G., M. Mazel, P. Clair, D. Mathieu, M. Kaczorek, and J. Temsamani. 2001. Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity. Eur. J. Biochem. 268:1304-1314.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1304-1314
    • Drin, G.1    Mazel, M.2    Clair, P.3    Mathieu, D.4    Kaczorek, M.5    Temsamani, J.6
  • 19
    • 1642457360 scopus 로고    scopus 로고
    • Cellular internalization of human calcitonin derived peptides in MDCK monolayers: A comparative study with Tat(47-57) and penetratin(43-58)
    • Trehin, R., U. Krauss, R. Muff, M. Meinecke, A. G. Beck-Sickinger, and H. P. Merkle. 2004. Cellular internalization of human calcitonin derived peptides in MDCK monolayers: a comparative study with Tat(47-57) and penetratin(43-58). Pharm. Res. 21:33-42.
    • (2004) Pharm. Res. , vol.21 , pp. 33-42
    • Trehin, R.1    Krauss, U.2    Muff, R.3    Meinecke, M.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 20
    • 3242674408 scopus 로고    scopus 로고
    • Cellular uptake but low permeation of human calcitonin-derived cell penetrating peptides and Tat(47-57) through well-differentiated epithelial models
    • Trehin, R., U. Krauss, A. G. Beck-Sickinger, H. P. Merkle, and H. M. Nielsen. 2004. Cellular uptake but low permeation of human calcitonin-derived cell penetrating peptides and Tat(47-57) through well-differentiated epithelial models. Pharm. Res. 21:1248-1256.
    • (2004) Pharm. Res. , vol.21 , pp. 1248-1256
    • Trehin, R.1    Krauss, U.2    Beck-Sickinger, A.G.3    Merkle, H.P.4    Nielsen, H.M.5
  • 21
    • 4744368322 scopus 로고    scopus 로고
    • Metabolic cleavage of cell penetrating peptides in contact with epithelial models: Human calcitonin (hCT) derived peptides, Tat(47-57) and Penetratin(43-58)
    • Trehin, R., H. M. Nielsen, H. G. Jahnke, U. Krauss, A. G. Beck-Sickinger, and H. P. Merkle. 2004. Metabolic cleavage of cell penetrating peptides in contact with epithelial models: human calcitonin (hCT) derived peptides, Tat(47-57) and Penetratin(43-58). Biochem. J. 382:945-956.
    • (2004) Biochem. J. , vol.382 , pp. 945-956
    • Trehin, R.1    Nielsen, H.M.2    Jahnke, H.G.3    Krauss, U.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 22
    • 0032529540 scopus 로고    scopus 로고
    • Solution structure of human calcitonin in membrane-mimetic environment: The role of the amphipathic helix
    • Motta, A., G. Andreotti, P. Amodeo, G. Strazzullo, and M. A. Castiglione Morelli. 1998. Solution structure of human calcitonin in membrane-mimetic environment: the role of the amphipathic helix. Proteins. 32:314-323.
    • (1998) Proteins , vol.32 , pp. 314-323
    • Motta, A.1    Andreotti, G.2    Amodeo, P.3    Strazzullo, G.4    Castiglione Morelli, M.A.5
  • 23
    • 4744363014 scopus 로고    scopus 로고
    • Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR
    • Wagner, K., A. G. Beck-Sickinger, and D. Huster. 2004. Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR. Biochemistry. 43:12459-12468.
    • (2004) Biochemistry , vol.43 , pp. 12459-12468
    • Wagner, K.1    Beck-Sickinger, A.G.2    Huster, D.3
  • 24
    • 0141976738 scopus 로고    scopus 로고
    • Novel daunorubicin-carrier peptide conjugates derived from human calcitonin segments
    • Krauss, U., F. Kratz, and A. G. Beck-Sickinger. 2003. Novel daunorubicin-carrier peptide conjugates derived from human calcitonin segments. J. Mol. Recognit. 16:280-287.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 280-287
    • Krauss, U.1    Kratz, F.2    Beck-Sickinger, A.G.3
  • 25
    • 0028290593 scopus 로고
    • Partition coefficients in vitro: Artificial membranes as a standardized distribution model
    • Pauletti, G. M., and H. Wunderli-Allenspach. 1994. Partition coefficients in vitro: artificial membranes as a standardized distribution model. Eur. J. Pharm. Sci. 1:273-282.
    • (1994) Eur. J. Pharm. Sci. , vol.1 , pp. 273-282
    • Pauletti, G.M.1    Wunderli-Allenspach, H.2
  • 26
    • 0025674441 scopus 로고
    • A validated HPLC assay for salmon calcitonin analysis. Comparison of HPLC and biological assay
    • Buck, R. H., and F. Maxl. 1990. A validated HPLC assay for salmon calcitonin analysis. Comparison of HPLC and biological assay. J. Pharm. Biomed. Anal. 8:761-769.
    • (1990) J. Pharm. Biomed. Anal. , vol.8 , pp. 761-769
    • Buck, R.H.1    Maxl, F.2
  • 27
    • 33845378455 scopus 로고
    • Micelle to vesicle transition in aqueous-solutions of bile-salt and lecithin
    • Schurtenberger, P., N. Mazer, and W. Kanzig. 1985. Micelle to vesicle transition in aqueous-solutions of bile-salt and lecithin. J. Phys. Chem. 89:1042-1049.
    • (1985) J. Phys. Chem. , vol.89 , pp. 1042-1049
    • Schurtenberger, P.1    Mazer, N.2    Kanzig, W.3
  • 28
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer, L. D., M. J. Hope, and P. R. Cullis. 1986. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta. 858:161-168.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 29
    • 0002960529 scopus 로고
    • Characterization of liposomes
    • R. B. C. New, editor. Oxford University Press, New York
    • New, R. B. C. 1990. Characterization of liposomes. In Liposomes, A Practical Approach. R. B. C. New, editor. Oxford University Press, New York. 125-127.
    • (1990) Liposomes, A Practical Approach , pp. 125-127
    • New, R.B.C.1
  • 30
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe, M., M. Schumann, T. Wieprecht, A. Winkler, M. Beyermann, E. Krause, K. Matsuzaki, O. Murase, and M. Bienert. 1996. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry. 35:12612-12622.
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 31
    • 0019464732 scopus 로고
    • Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies
    • Brown, L. R., C. Bösch, and K. Wüthrich. 1981. Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies. Biochim. Biophys. Acta. 642:296-312.
    • (1981) Biochim. Biophys. Acta , vol.642 , pp. 296-312
    • Brown, L.R.1    Bösch, C.2    Wüthrich, K.3
  • 33
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., R. R. Ernst, and K. Wüthrich. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 35
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., C. Mumenthaler, and K. Wüthrich. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 37
    • 0028019692 scopus 로고
    • Location of the M13 major coat protein in sodium dodecylsulfate micelles as determined by NMR
    • Papavoine, C. H., R. N. Konings, C. W. Hilbers, and F. J. Van de Veen. 1994. Location of the M13 major coat protein in sodium dodecylsulfate micelles as determined by NMR. Biochemistry. 33:12990-12997.
    • (1994) Biochemistry , vol.33 , pp. 12990-12997
    • Papavoine, C.H.1    Konings, R.N.2    Hilbers, C.W.3    Van De Veen, F.J.4
  • 38
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported spectral analysis of biological macromolecules
    • Bartels, C., T. H. Xia, M. Billeter, P. Güntert, and K. Wüthrich. 1995. The program XEASY for computer-supported spectral analysis of biological macromolecules. J. Biomol. NMR. 6:1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 39
    • 4644355649 scopus 로고    scopus 로고
    • NMR of membrane-associated peptides and proteins
    • O. Zerbe, editor. Wiley-VCH, Weinheim
    • Bader, R., M. Lerch, and O. Zerbe. 2002. NMR of membrane-associated peptides and proteins. In BioNMR in Drug Research. O. Zerbe, editor. Wiley-VCH, Weinheim. 95-120.
    • (2002) BioNMR in Drug Research , pp. 95-120
    • Bader, R.1    Lerch, M.2    Zerbe, O.3
  • 40
    • 0035847111 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection
    • Bader, R., A. Bettio, A. G. Beck-Sickinger, and O. Zerbe. 2001. Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection. J. Mol. Biol. 305:307-329.
    • (2001) J. Mol. Biol. , vol.305 , pp. 307-329
    • Bader, R.1    Bettio, A.2    Beck-Sickinger, A.G.3    Zerbe, O.4
  • 41
    • 20444382011 scopus 로고    scopus 로고
    • Bilayer interaction and localization of cell penetrating peptides with model membranes: A comparative study of a human calcitonin (hCT)-derived peptide with pVEC and pAntp(43-58)
    • Herbig, M. E., U. Fromm, J. Leuenberger, U. Krauss, A. G. Beck-Sickinger, and H. P. Merkle. 2005. Bilayer interaction and localization of cell penetrating peptides with model membranes: a comparative study of a human calcitonin (hCT)-derived peptide with pVEC and pAntp(43-58). Biochim. Biophys. Acta. 1712:197-211.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 197-211
    • Herbig, M.E.1    Fromm, U.2    Leuenberger, J.3    Krauss, U.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 43
    • 0027318744 scopus 로고
    • A rapid and simple microfluorometric phagocytosis assay
    • Wan, C. P., C. S. Park, and B. H. S. Lau. 1993. A rapid and simple microfluorometric phagocytosis assay. J. Immunol. Methods. 162:1-7.
    • (1993) J. Immunol. Methods , vol.162 , pp. 1-7
    • Wan, C.P.1    Park, C.S.2    Lau, B.H.S.3
  • 44
    • 0020638326 scopus 로고
    • Differentiation between attached and ingested immune-complexes by a fluorescence quenching cytofluorometric assay
    • Sahlin, S., J. Hed, and I. Rundquist. 1983. Differentiation between attached and ingested immune-complexes by a fluorescence quenching cytofluorometric assay. J. Immunol. Methods. 60:115-124.
    • (1983) J. Immunol. Methods , vol.60 , pp. 115-124
    • Sahlin, S.1    Hed, J.2    Rundquist, I.3
  • 45
    • 0344946091 scopus 로고    scopus 로고
    • Uptake of chitosan and associated insulin in Caco-2 cell monolayers: A comparison between chitosan molecules and chitosan nanoparticles
    • Ma, Z. S., and L. Y. Lim. 2003. Uptake of chitosan and associated insulin in Caco-2 cell monolayers: a comparison between chitosan molecules and chitosan nanoparticles. Pharm. Res. 20:1812-1819.
    • (2003) Pharm. Res. , vol.20 , pp. 1812-1819
    • Ma, Z.S.1    Lim, L.Y.2
  • 46
    • 0030570264 scopus 로고    scopus 로고
    • Cationic liposomal delivery of plasmid to endothelial cells measured by quantitative flow cytometry
    • Tseng, W. C., N. B. Purvis, F. R. Haselton, and T. D. Giorgio. 1996. Cationic liposomal delivery of plasmid to endothelial cells measured by quantitative flow cytometry. Biotechnol. Bioeng. 50:548-554.
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 548-554
    • Tseng, W.C.1    Purvis, N.B.2    Haselton, F.R.3    Giorgio, T.D.4
  • 47
    • 0023236839 scopus 로고
    • The use of fluorescence quenching in flow cytofluorometry to measure the attachment and ingestion phases in phagocytosis in peripheral blood without prior cell separation
    • Hed, J., G. Hallden, S. G. Johansson, and P. Larsson. 1987. The use of fluorescence quenching in flow cytofluorometry to measure the attachment and ingestion phases in phagocytosis in peripheral blood without prior cell separation. J. Immunol. Methods. 101:119-125.
    • (1987) J. Immunol. Methods , vol.101 , pp. 119-125
    • Hed, J.1    Hallden, G.2    Johansson, S.G.3    Larsson, P.4
  • 48
    • 0033151933 scopus 로고    scopus 로고
    • A technique for the study of endocytosis in human oral epithelial cells
    • Innes, N. P., and G. R. Ogden. 1999. A technique for the study of endocytosis in human oral epithelial cells. Arch. Oral Biol. 44:519-523.
    • (1999) Arch. Oral Biol. , vol.44 , pp. 519-523
    • Innes, N.P.1    Ogden, G.R.2
  • 49
    • 0034653456 scopus 로고    scopus 로고
    • Comparison of the LDH and MTT assays for quantifying cell death: Validity for neuronal apoptosis?
    • Lobner, D. 2000. Comparison of the LDH and MTT assays for quantifying cell death: validity for neuronal apoptosis? J. Neurosci. Methods. 96:147-152.
    • (2000) J. Neurosci. Methods , vol.96 , pp. 147-152
    • Lobner, D.1
  • 50
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White, S. H., and W. C. Wimley. 1998. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta. 1376:339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 51
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K., S. Yoneyama, and K. Miyajima. 1997. Pore formation and translocation of melittin. Biophys. J. 73:831-838.
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 52
    • 0141942113 scopus 로고    scopus 로고
    • A brief introduction to cell-penetrating peptides
    • Lundberg, P., and U. Langel. 2003. A brief introduction to cell-penetrating peptides. J. Mol. Recognit. 16:227-233.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 227-233
    • Lundberg, P.1    Langel, U.2
  • 53
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D., S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing, and A. Prochiantz. 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
  • 54
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., D. Rapaport, A. Mor, P. Nicolas, and Y. Shai. 1992. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry. 31:12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 55
    • 0032930291 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of gram-negative bacteria
    • Matsuzaki, K., K. Sugishita, and K. Miyajima. 1999. Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of gram-negative bacteria. FEBS Lett. 449:221-224.
    • (1999) FEBS Lett. , vol.449 , pp. 221-224
    • Matsuzaki, K.1    Sugishita, K.2    Miyajima, K.3
  • 56
    • 0027953945 scopus 로고
    • Mode of action of the antibacterial cecropin B2: A spectrofluorometric study
    • Gazit, E., W. J. Lee, P. T. Brey, and Y. Shai. 1994. Mode of action of the antibacterial cecropin B2: a spectrofluorometric study. Biochemistry. 33:10681-10692.
    • (1994) Biochemistry , vol.33 , pp. 10681-10692
    • Gazit, E.1    Lee, W.J.2    Brey, P.T.3    Shai, Y.4
  • 57
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, maganin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1996. An antimicrobial peptide, maganin 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
  • 58
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig, J. 2004. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta. 1666:40-50.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 59
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 60
    • 0141942113 scopus 로고    scopus 로고
    • A brief introduction to cell-penetrating peptides
    • Lundberg, P., and U. Langel. 2003. A brief introduction to cell-penetrating peptides. J. Mol. Recognit. 16:227-233.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 227-233
    • Lundberg, P.1    Langel, U.2
  • 61
    • 0000181355 scopus 로고
    • A thermodynamic model of the lamellar to inverse hexangonal phase transition of lipid-membrane water systems
    • Kirk, G. L., S. M. Gruner, and D. L. Stein. 1984. A thermodynamic model of the lamellar to inverse hexangonal phase transition of lipid-membrane water systems. Biochemistry. 23:1093-1102.
    • (1984) Biochemistry , vol.23 , pp. 1093-1102
    • Kirk, G.L.1    Gruner, S.M.2    Stein, D.L.3
  • 62
    • 0029802678 scopus 로고    scopus 로고
    • Conformational and associative behaviours of the third helix of Antennapedia homeodomain in membrane-mimetic environments
    • Berlose, J. P., O. Convert, D. Derossi, A. Brunissen, and G. Chassaing. 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
  • 63
    • 0038375258 scopus 로고    scopus 로고
    • Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR
    • Lindberg, M., H. Biverstahl, A. Gräslund, and L. Mäler. 2003. Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR. Eur. J. Biochem. 270:3055-3063.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3055-3063
    • Lindberg, M.1    Biverstahl, H.2    Gräslund, A.3    Mäler, L.4
  • 64
    • 0342902198 scopus 로고    scopus 로고
    • The position of the cell penetrating peptide penetratin in SDS micelles determined by NMR
    • Lindberg, M., and A. Gräslund. 2001. The position of the cell penetrating peptide penetratin in SDS micelles determined by NMR. FEBS Lett. 497:39-44.
    • (2001) FEBS Lett. , vol.497 , pp. 39-44
    • Lindberg, M.1    Gräslund, A.2
  • 65
    • 0035853015 scopus 로고    scopus 로고
    • Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR
    • Lindberg, M., J. Jarvet, U. Langel, and A. Gräslund. 2001. Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry. 40:3141-3149.
    • (2001) Biochemistry , vol.40 , pp. 3141-3149
    • Lindberg, M.1    Jarvet, J.2    Langel, U.3    Gräslund, A.4
  • 66
    • 2942627932 scopus 로고    scopus 로고
    • NMR solution structure and position of transportan in neutral phospholipid bicelles
    • Barany-Wallje, E., A. Andersson, A. Gräslund, and L. Maler. 2004. NMR solution structure and position of transportan in neutral phospholipid bicelles. FEBS Lett. 567:265-269.
    • (2004) FEBS Lett. , vol.567 , pp. 265-269
    • Barany-Wallje, E.1    Andersson, A.2    Gräslund, A.3    Maler, L.4
  • 67
    • 0017390364 scopus 로고
    • Secondary structural prediction of proteins from their amino-acid sequence
    • Chou, P. Y., and G. D. Fasman. 1977. Secondary structural prediction of proteins from their amino-acid sequence. Trends Biochem. Sci. 2:128-131.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 128-131
    • Chou, P.Y.1    Fasman, G.D.2
  • 68
    • 0035200499 scopus 로고    scopus 로고
    • Channel formation by salmon and human calcitonin in black lipid membranes
    • Stipani, V., E. Gallucci, S. Micelli, V. Picciarelli, and R. Benz. 2001. Channel formation by salmon and human calcitonin in black lipid membranes. Biophys. J. 81:3332-3338.
    • (2001) Biophys. J. , vol.81 , pp. 3332-3338
    • Stipani, V.1    Gallucci, E.2    Micelli, S.3    Picciarelli, V.4    Benz, R.5
  • 69
    • 20944447518 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Small from inception to application
    • Magzoub, M., and A. Gräslund. 2004. Cell-penetrating peptides: small from inception to application. Q. Rev. Biophys. 37:147-195.
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 147-195
    • Magzoub, M.1    Gräslund, A.2


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