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Volumn 43, Issue 49, 2004, Pages 15610-15616

Membrane translocation mechanism of the antimicrobial peptide buforin 2

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; ISOMERIZATION; LIPIDS; MICROBIOLOGY; SKIN; SUPRAMOLECULAR CHEMISTRY;

EID: 10644260444     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048206q     Document Type: Article
Times cited : (134)

References (41)
  • 1
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer, R. I., and Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence, Curr. Opin. Immunol. 11, 23-27.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 2
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E., and Scott, M. G. (2000) The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. U.S.A. 97, 8856-8861.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 3
    • 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
  • 4
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R., and Yount, N. Y. (2003) Mechanisms of antimicrobial peptide action and resistance, Pharmacol. Rev. 55, 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 5
    • 2042513493 scopus 로고
    • Magainins, a class of zntimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequene of a precursor
    • Zasloff, M. (1987) Magainins, a class of zntimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequene of a precursor, Proc. Natl. Acad. Sci. U.S.A. 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 6
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. (1998) Magainins as paradigm for the mode of action of pore forming polypeptides, Biochim. Biophys. Acta 1376, 391-400.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 7
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defence? Magainins and tachyplesins as archetypes
    • Matsuzaki, K. (1999) Why and how are peptide-lipid interactions utilized for self-defence? Magainins and tachyplesins as archetypes, Biochim. Biophys. Acta 1462, 1-10.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 8
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., Zasloff, M., and Opella, S. J. (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2, 2077-2084.
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 9
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., Murase, O., Tokuda, H., Funakoshi, S., Fujii, N., and Miyajima, K. (1994) Orientational and aggregational states of magainin 2 in phospholipid bilayers, Biochemistry 33, 3342-3349.
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 10
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antimicrobial peptides
    • Wieprecht, T., Dathe, M., Epand, R. M., Beyermann, M., Krause, E., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997) Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antimicrobial peptides. Biochemistry 36, 12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 12
    • 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
  • 14
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1995) Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore, Biochemistry 34, 6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 15
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptides from Bufo bufo gargarizans
    • Park, C. B., Kim, M. S., and Kim, S. C. (1996) A novel antimicrobial peptides from Bufo bufo gargarizans, Biochem. Biophys. Res. Commun. 218, 408-413.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 16
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor
    • Kobayashi, S., Takeshima, K., Park, C. B., Kim, S. C., and Matsuzaki, K. (2000) Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor, Biochemistry 39, 8648-8654.
    • (2000) Biochemistry , vol.39 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 17
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin ii: Buforin ii kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park, C. B., Kim, H. S., and Kim, S. C. (1998) Mechanism of action of the antimicrobial peptide buforin ii: buforin ii kills microorganisms by penetrating the cell membrane and inhibiting cellular functions, Biochem. Biophys. Res. Commun. 244, 253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 18
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima, K., Chikushi, A., Lee, K.-K., Yonehara, S., and Matsuzaki, K. (2003) Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes, J. Biol. Chem. 278, 1310-1315.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1310-1315
    • Takeshima, K.1    Chikushi, A.2    Lee, K.-K.3    Yonehara, S.4    Matsuzaki, K.5
  • 19
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. (1959) Phosphorus assay in column chromatography. J. Biol. Chem. 234, 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 20
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • Ladokhin, A. S., Wimley, W. C., and White, S. H. (1995) Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching, Biophys. J., 1964-1971.
    • (1995) Biophys. J. , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 21
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh, E., Raussens, V., and Ruysschaert, J.-M. (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1422, 105-185.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 22
    • 0026066649 scopus 로고
    • A comparative study on interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers
    • Matsuzaki, K., Shioyama, T., Okamura, E., Umemura, J., Takenaka, T., Takaishi, Y., Fujita, T., and Miyajima, K. (1991) A comparative study on interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers. Biochim. Biophys. Acta 1070, 419-428.
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 419-428
    • Matsuzaki, K.1    Shioyama, T.2    Okamura, E.3    Umemura, J.4    Takenaka, T.5    Takaishi, Y.6    Fujita, T.7    Miyajima, K.8
  • 23
    • 0033799243 scopus 로고    scopus 로고
    • Polar angle as a determinant of amphipathic α-helix-lipid interactions: A model peptide study
    • Uematsu, N., and Matsuzaki, K. (2000) Polar angle as a determinant of amphipathic α-helix-lipid interactions: a model peptide study, Biophys. J. 79, 2075-2083.
    • (2000) Biophys. J. , vol.79 , pp. 2075-2083
    • Uematsu, N.1    Matsuzaki, K.2
  • 25
    • 0001490908 scopus 로고
    • Novel conformational distributions of methylproline peptides
    • Delaney, N. G., and Madison, V. (1982) Novel conformational distributions of methylproline peptides, J. Am. Chem. Soc. 104, 6635-6641.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6635-6641
    • Delaney, N.G.1    Madison, V.2
  • 26
    • 0025848453 scopus 로고
    • Synthesis, conformational properties, and antibody recognition of peptides containing β-turn mimetics based on α-alkylproline derivatives
    • Hinds, M. G., Welsh, J. H., Brennand, D. M., Fisher, J., Glennie, M. J., Richards, N. G. J., Turner, D. L., and Robinson, J. A. (1991) Synthesis, conformational properties, and antibody recognition of peptides containing β-turn mimetics based on α-alkylproline derivatives, J. Med. Chem. 34, 1777-1789.
    • (1991) J. Med. Chem. , vol.34 , pp. 1777-1789
    • Hinds, M.G.1    Welsh, J.H.2    Brennand, D.M.3    Fisher, J.4    Glennie, M.J.5    Richards, N.G.J.6    Turner, D.L.7    Robinson, J.A.8
  • 28
    • 0024291319 scopus 로고
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups, Biochemistry 27, 8239-8249.
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Huebner, W.2    Messner, G.3
  • 29
    • 0024294844 scopus 로고
    • Fourier transform infrared-attenuated total reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers
    • Ter-Minassian-Saraga, L., Okamura, E., Umemura, J., and Takenaka, T. (1988) Fourier transform infrared-attenuated total reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers, Biochim. Biophys. Acta 946, 417-423.
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 417-423
    • Ter-Minassian-Saraga, L.1    Okamura, E.2    Umemura, J.3    Takenaka, T.4
  • 30
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgradze, Y. N., Fedorov, O. V., and Trushina, N. P. (1975) Estimation of amino acid residue side chain absorption in the infrared spectra of protein solutions in heavy water, Biopolymers 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgradze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 31
    • 0142135619 scopus 로고    scopus 로고
    • Attenuated total reflection Fourier transform infrared spectroscopy: A method of choice for studying membrane proteins and lipids
    • Tatulian, S. A. (2003) Attenuated total reflection Fourier transform infrared spectroscopy: A method of choice for studying membrane proteins and lipids, Biochemistry 42, 11898-11907.
    • (2003) Biochemistry , vol.42 , pp. 11898-11907
    • Tatulian, S.A.1
  • 32
    • 0026731832 scopus 로고
    • Conformation of magainin 2 and related peptide in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
    • Jackson, M., Manisch, H. H., and Spencer, J. (1992) Conformation of magainin 2 and related peptide in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy, Biochemistry 31, 7289-7293.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Manisch, H.H.2    Spencer, J.3
  • 37
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F.-Y., Lee, M.-T., and Huang, H. W. (2002) Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin, Biophys. J. 82, 908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 38
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee, M.-T., Chen, F.-Y., and Huang, H. W. (2004) Energetics of pore formation induced by membrane active peptides, Biochemistry 43, 3590-3599.
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.-T.1    Chen, F.-Y.2    Huang, H.W.3
  • 39
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park, C. B., Yi, K.-S., Matsuzaki, K., Kim, M. S., and Kim, S. C. (2000) Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II, Proc. Natl. Acad. Sci., U.S.A. 97, 8245-8250.
    • (2000) Proc. Natl. Acad. Sci., U.S.A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.-S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 40
    • 0030602175 scopus 로고    scopus 로고
    • Solution structure of an antimicrobial peptide buforin II
    • Yi, G.-S., Park, C. B., Kim, S. C., and Cheong, C. (1996) Solution structure of an antimicrobial peptide buforin II, FEBS Lett. 398, 87-90.
    • (1996) FEBS Lett. , vol.398 , pp. 87-90
    • Yi, G.-S.1    Park, C.B.2    Kim, S.C.3    Cheong, C.4
  • 41
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • Ludtke, S. J., He, K., Wu, Y., and Huang, H. W. (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    Wu, Y.3    Huang, H.W.4


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