메뉴 건너뛰기




Volumn 92, Issue 7, 2007, Pages 2434-2444

Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CELL PENETRATING PEPTIDE; FLUORESCEIN; MONOMER; PROTEIN TRANSPORTAN 10; UNCLASSIFIED DRUG;

EID: 34047238809     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.100198     Document Type: Article
Times cited : (154)

References (44)
  • 1
    • 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
  • 2
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green, M., and P. M. Lowenstein. 1988. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell. 55:1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Lowenstein, P.M.2
  • 3
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and C. O. Pabo. 1988. Cellular uptake of the tat protein from human immunodeficiency virus. Cell. 55:1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 6
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature. 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 8
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles
    • Magzoub, M., K. Kilk, L. E. G. Eriksson, U. Langel, and A. Gräslund. 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, U.4    Gräslund, A.5
  • 11
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D., H. Steiner, T. Rasmuson, and H. G. Boman. 1980. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106:7-16.
    • (1980) Eur. J. Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 12
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H., D. Hultmark, A. Engstrom, H. Bennich, and H. G. Boman. 1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature. 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 13
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. 1987. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA. 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 14
    • 0025787585 scopus 로고
    • Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin
    • Mor, A., V. H. Nguyen, A. Delfour, D. Migliore-Samour, and P. Nicolas. 1991. Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry. 30:8824-8830.
    • (1991) Biochemistry , vol.30 , pp. 8824-8830
    • Mor, A.1    Nguyen, V.H.2    Delfour, A.3    Migliore-Samour, D.4    Nicolas, P.5
  • 15
    • 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., E. K. Esbjörner, P. Lincoln, and B. Nordén. 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
  • 16
    • 12344275753 scopus 로고    scopus 로고
    • Direct observation of anion-mediated translocation of fluorescent oligoarginine carriers into and across bulk liquid and anionic bilayer membranes
    • Sakai, N., T. Takeuchi, S. Futaki, and S. Matile. 2005. Direct observation of anion-mediated translocation of fluorescent oligoarginine carriers into and across bulk liquid and anionic bilayer membranes. ChemBioChem. 6:114-122.
    • (2005) ChemBioChem , vol.6 , pp. 114-122
    • Sakai, N.1    Takeuchi, T.2    Futaki, S.3    Matile, S.4
  • 17
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of d-lysin interaction with phospholipid vesicles
    • Pokorny, A., T. H. Birkbeck, and P. F. F. Almeida. 2002. Mechanism and kinetics of d-lysin interaction with phospholipid vesicles. Biochemistry. 41:11044-11056.
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 18
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides
    • Pokorny, A., and P. F. F. Almeida. 2004. Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides. Biochemistry. 43:8846-8857.
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 19
    • 21844443548 scopus 로고    scopus 로고
    • Permeabilization of raft-containing lipid vesicles by δ-lysin: A mechanism for cell sensitivity to cytotoxic peptides
    • Pokorny, A., and P. F. F. Almeida. 2005. Permeabilization of raft-containing lipid vesicles by δ-lysin: a mechanism for cell sensitivity to cytotoxic peptides. Biochemistry. 44:9538-9544.
    • (2005) Biochemistry , vol.44 , pp. 9538-9544
    • Pokorny, A.1    Almeida, P.F.F.2
  • 20
    • 33750288787 scopus 로고    scopus 로고
    • Probing membrane insertion activity of antimicrobial polymers via coarse-grain molecular dynamics
    • Lopez, C. F., S. O. Nielsen, G. Srinivas, W. F. DeGrado, and M. L. Klein. 2006. Probing membrane insertion activity of antimicrobial polymers via coarse-grain molecular dynamics. J. Chem. Theory and Comput. 2:649-655.
    • (2006) J. Chem. Theory and Comput , vol.2 , pp. 649-655
    • Lopez, C.F.1    Nielsen, S.O.2    Srinivas, G.3    DeGrado, W.F.4    Klein, M.L.5
  • 23
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H., and W. C. Wimley. 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
  • 24
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorous assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 25
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • Ladokhin, A. S., W. C. Wimley, and S. H. White. 1995. Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching. Biophys. J. 69:1964-1971.
    • (1995) Biophys. J , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 26
    • 0031008251 scopus 로고    scopus 로고
    • Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching
    • Ladokhin, A. S., W. C. Wimley, K. Hristova, and S. H. White. 1997. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching. Methods Enzymol. 278:474-486.
    • (1997) Methods Enzymol , vol.278 , pp. 474-486
    • Ladokhin, A.S.1    Wimley, W.C.2    Hristova, K.3    White, S.H.4
  • 28
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro, L., K. Gupta, J. N. Weiser, and P. H. Axelsen. 1997. The concentration-dependent membrane activity of cecropin A. Biochemistry. 36:11452-11460.
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 29
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G., and H. Lehar. 1977. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10:1-34.
    • (1977) Q. Rev. Biophys , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lehar, H.2
  • 31
    • 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., O. Murase, N. Fujii, and K. Miyajima. 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
  • 32
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. 2002. Mode of action of membrane active antimicrobial peptides. Biopolymers. 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 33
    • 1042267410 scopus 로고    scopus 로고
    • Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?
    • Papo, N., and Y. Shai. 2003. Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes? Peptides. 24:1693-1703.
    • (2003) Peptides , vol.24 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 34
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. 1999. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta. 1462:157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 35
    • 0033863799 scopus 로고    scopus 로고
    • Membrane-induced folding of cecropin A
    • Silvestro, L., and P. H. Axelsen. 2000. Membrane-induced folding of cecropin A. Biophys. J. 79:1465-1477.
    • (2000) Biophys. J , vol.79 , pp. 1465-1477
    • Silvestro, L.1    Axelsen, P.H.2
  • 36
    • 0032763732 scopus 로고    scopus 로고
    • Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy
    • Marassi, F. M., S. J. Opella, P. Juvvadi, and R. B. Merrifield. 1999. Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy. Biophys. J. 77:3152-3155.
    • (1999) Biophys. J , vol.77 , pp. 3152-3155
    • Marassi, F.M.1    Opella, S.J.2    Juvvadi, P.3    Merrifield, R.B.4
  • 37
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z., J. C. Lerman, G. H. Gudmundsson, B. Agerberth, and Y. Shai. 1999. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341:501-513.
    • (1999) Biochem. J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 38
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K. A., D.-K. Lee, and A. Ramamoorthy. 2003. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry. 42:6545-6558.
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 39
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
    • Ramamoorthy, A., S. Thennarasu, D.-K. Lee, A. Tan, and L. Maloy. 2006. Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys. J. 91:206-216.
    • (2006) Biophys. J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.-K.3    Tan, A.4    Maloy, L.5
  • 40
    • 0026742166 scopus 로고
    • Structure and interactions of magainin antibiotic peptides in lipid bilayers: A solidstate nuclear magnetic resonance investigation
    • Bechinger, B., M. Zasloff, and S. J. Opella. 1992. Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solidstate nuclear magnetic resonance investigation. Biophys. J. 62:12-14.
    • (1992) Biophys. J , vol.62 , pp. 12-14
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 41
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • Bechinger, B., J.-M. Ruysschaert, and E. Goormaghtigh. 1999. Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys. J. 76:552-563.
    • (1999) Biophys. J , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 42
    • 0347319182 scopus 로고    scopus 로고
    • Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: A site-directed spin-labeling study
    • Bhargava, K., and J. B. Feix. 2004. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study. Biophys. J. 86:329-336.
    • (2004) Biophys. J , vol.86 , pp. 329-336
    • Bhargava, K.1    Feix, J.B.2
  • 43
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • Ludtke, S. J., K. He, and H. W. Huang. 1994. Cooperative membrane insertion of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta. 1190:181-184.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 181-184
    • Ludtke, S.J.1    He, K.2    Huang, H.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.