메뉴 건너뛰기




Volumn 1758, Issue 9, 2006, Pages 1529-1539

Detergent-like actions of linear amphipathic cationic antimicrobial peptides

Author keywords

Bilayer; Peptide pore formation; Phospholipid membrane; Polypeptide lipid interaction; Regulation; Selectivity

Indexed keywords

ALAMETHICIN; ANTIBIOTIC AGENT; BUFORIN 2; CATION; CECROPIN; DEFENSIN; DETERGENT; GRAMICIDIN S; MAGAININ 1; MAGAININ 2; NISIN; PARDAXIN; PEPTIDE; PEXIGANAN ACETATE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; UNCLASSIFIED DRUG;

EID: 33748947334     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.07.001     Document Type: Review
Times cited : (505)

References (158)
  • 2
    • 0033542413 scopus 로고    scopus 로고
    • Emergence of vancomycin tolerance in Streptococcus pneumoniae
    • Novak R., Henriques B., Charpentier E., Normark S., and Tuomanen E. Emergence of vancomycin tolerance in Streptococcus pneumoniae. Nature 399 (1999) 590-593
    • (1999) Nature , vol.399 , pp. 590-593
    • Novak, R.1    Henriques, B.2    Charpentier, E.3    Normark, S.4    Tuomanen, E.5
  • 3
    • 50549170868 scopus 로고
    • Über das Giftsekret der Gelbbauchunke Bombina variegata L
    • Kiss G., and Michl H. Über das Giftsekret der Gelbbauchunke Bombina variegata L. Toxicon (Oxford) 1 (1962) 33-39
    • (1962) Toxicon (Oxford) , vol.1 , pp. 33-39
    • Kiss, G.1    Michl, H.2
  • 4
    • 0030949597 scopus 로고    scopus 로고
    • Magainin 2 effects on the ultrastructure of five plant pathogens
    • Kristyanne E.S., Kim K.S., and Steward J.M. Magainin 2 effects on the ultrastructure of five plant pathogens. Mycologia 89 (1997) 353-360
    • (1997) Mycologia , vol.89 , pp. 353-360
    • Kristyanne, E.S.1    Kim, K.S.2    Steward, J.M.3
  • 5
    • 0032031617 scopus 로고    scopus 로고
    • Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens
    • Cavallarin L., Andreu D., and San Segundo B. Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens. Mol. Plant-Microb. Interact. 11 (1998) 218-227
    • (1998) Mol. Plant-Microb. Interact. , vol.11 , pp. 218-227
    • Cavallarin, L.1    Andreu, D.2    San Segundo, B.3
  • 6
    • 0037057687 scopus 로고    scopus 로고
    • Antimicrobial peptides in health and disease
    • Zasloff M. Antimicrobial peptides in health and disease. N. Engl. J. Med. 347 (2002) 1199-1200
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1199-1200
    • Zasloff, M.1
  • 7
    • 0035986972 scopus 로고    scopus 로고
    • Sensitivity of bacterial and fungal plant pathogens to the lytic peptides, MSI-99, magainin II, and cecropin B
    • Alan A.R., and Earle E.D. Sensitivity of bacterial and fungal plant pathogens to the lytic peptides, MSI-99, magainin II, and cecropin B. Mol. Plant-Microb. Interact. 15 (2002) 701-708
    • (2002) Mol. Plant-Microb. Interact. , vol.15 , pp. 701-708
    • Alan, A.R.1    Earle, E.D.2
  • 8
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254 (2003) 197-215
    • (2003) J. Intern. Med. , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 9
    • 0033863173 scopus 로고    scopus 로고
    • Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies
    • Blondelle S.E., and Lohner K. Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55 (2000) 74-87
    • (2000) Biopolymers , vol.55 , pp. 74-87
    • Blondelle, S.E.1    Lohner, K.2
  • 10
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming polypeptides: magainins, cecropins, melittin and alamethicin
    • Bechinger B. Structure and functions of channel-forming polypeptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156 (1997) 197-211
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 11
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • Hwang P.M., and Vogel H.J. Structure-function relationships of antimicrobial peptides. Biochem. Cell. Biol. 76 (1998) 235-246
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 12
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers J.P., and Hancock R.E. The relationship between peptide structure and antibacterial activity. Peptides 24 (2003) 1681-1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 15
    • 0025818448 scopus 로고
    • Antibacterial peptides: key components needed in immunity
    • Boman H.G. Antibacterial peptides: key components needed in immunity. Cell 65 (1991) 205-207
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 17
    • 0001637567 scopus 로고
    • Isolierung und Strukturaufklärung eines hämolytisch wirkenden Polypeptides aus dem Abwehrsekret europäischer Unken
    • Csordas A., and Michl H. Isolierung und Strukturaufklärung eines hämolytisch wirkenden Polypeptides aus dem Abwehrsekret europäischer Unken. Monatsh. Chem. 101 (1970) 182-189
    • (1970) Monatsh. Chem. , vol.101 , pp. 182-189
    • Csordas, A.1    Michl, H.2
  • 18
    • 0020985676 scopus 로고
    • A novel peptide designated PYLa and its precursor as predicted from cloned mRNA of Xenopus laevis skin
    • Hoffmann W., Richter K., and Kreil G. A novel peptide designated PYLa and its precursor as predicted from cloned mRNA of Xenopus laevis skin. EMBO J. 2 (1983) 711-714
    • (1983) EMBO J. , vol.2 , pp. 711-714
    • Hoffmann, W.1    Richter, K.2    Kreil, G.3
  • 19
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 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
  • 20
    • 0020366780 scopus 로고
    • Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • Hultmark D., Engstrom A., Bennich H., Kapur R., and Boman H.G. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur. J. Biochem. 127 (1982) 207-217
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 21
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462 (1999) 157-183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 22
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 23
    • 0027978980 scopus 로고
    • Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import
    • Hugosson M., Andreu D., Boman H.G., and Glaser E. Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import. Eur. J. Biochem. 223 (1994) 1027-1033
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1027-1033
    • Hugosson, M.1    Andreu, D.2    Boman, H.G.3    Glaser, E.4
  • 25
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro L., Gupta K., Weiser J.N., and Axelsen P.H. The concentration-dependent membrane activity of cecropin A. Biochemistry 36 (1997) 11452-11460
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 26
    • 0020025608 scopus 로고
    • Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue
    • DeGrado W.F., Musso G.F., Lieber M., Kaiser E.T., and Kezdy F.J. Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue. Biophys. J. 37 (1982) 329-338
    • (1982) Biophys. J. , vol.37 , pp. 329-338
    • DeGrado, W.F.1    Musso, G.F.2    Lieber, M.3    Kaiser, E.T.4    Kezdy, F.J.5
  • 28
    • 0031934251 scopus 로고    scopus 로고
    • Synthesis and study of normal, enantio, retro, and retroenantio isomers of cecropin A-melittin hybrids, their end group effects and selective enzyme inactivation
    • Vunnam S., Juvvadi P., Rotondi K.S., and Merrifield R.B. Synthesis and study of normal, enantio, retro, and retroenantio isomers of cecropin A-melittin hybrids, their end group effects and selective enzyme inactivation. J. Pept. Res. 51 (1998) 38-44
    • (1998) J. Pept. Res. , vol.51 , pp. 38-44
    • Vunnam, S.1    Juvvadi, P.2    Rotondi, K.S.3    Merrifield, R.B.4
  • 32
    • 0035471135 scopus 로고    scopus 로고
    • beta-Peptides: from structure to function
    • Cheng R.P., Gellman S.H., and DeGrado W.F. beta-Peptides: from structure to function. Chem. Rev. 101 (2001) 3219-3232
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    DeGrado, W.F.3
  • 33
    • 0032792710 scopus 로고    scopus 로고
    • Design, synthesis and characterization of antimicrobial pseudopeptides corresponding to membrane-active peptide
    • Oh J.E., Hong S.Y., and Lee K.H. Design, synthesis and characterization of antimicrobial pseudopeptides corresponding to membrane-active peptide. J. Pept. Res. 54 (1999) 129-136
    • (1999) J. Pept. Res. , vol.54 , pp. 129-136
    • Oh, J.E.1    Hong, S.Y.2    Lee, K.H.3
  • 34
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity
    • Lehrer R.I., Barton A., Daher K.A., Harwig S.S., Ganz T., and Selsted M.E. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J. Clin. Invest. 84 (1989) 553-561
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 35
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki K., Sugishita K., Harada M., Fujii N., and Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327 (1997) 119-130
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 36
    • 0344687481 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide PGLa on live Escherichia coli
    • da Silva Jr. A., and Teschke O. Effects of the antimicrobial peptide PGLa on live Escherichia coli. Biochim. Biophys. Acta 1643 (2003) 95-103
    • (2003) Biochim. Biophys. Acta , vol.1643 , pp. 95-103
    • da Silva Jr., A.1    Teschke, O.2
  • 37
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T., Dathe M., Epand R.M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., and Bienert M. Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 36 (1997) 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
  • 38
    • 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., Schumann M., Wieprecht T., Winkler A., Beyermann M., Krause E., Matsuzaki K., Murase O., and Bienert M. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35 (1996) 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
  • 39
    • 0033576264 scopus 로고    scopus 로고
    • 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids
    • Sharon M., Oren Z., Shai Y., and Anglister J. 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids. Biochemistry 38 (1999) 15305-15316
    • (1999) Biochemistry , vol.38 , pp. 15305-15316
    • Sharon, M.1    Oren, Z.2    Shai, Y.3    Anglister, J.4
  • 40
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe M., Nikolenko H., Meyer J., Beyermann M., and Bienert M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett. 501 (2001) 146-150
    • (2001) FEBS Lett. , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 41
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • Tachi T., Epand R.F., Epand R.M., and Matsuzaki K. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry 41 (2002) 10723-10731
    • (2002) Biochemistry , vol.41 , pp. 10723-10731
    • Tachi, T.1    Epand, R.F.2    Epand, R.M.3    Matsuzaki, K.4
  • 42
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics
    • Lohner K., and Blondelle S.E. Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics. Comb. Chem. High Throughout Screen. 8 (2005) 241-256
    • (2005) Comb. Chem. High Throughout Screen. , vol.8 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 43
    • 0023875642 scopus 로고
    • A two-dimensional NMR study of the antimicrobial peptide magainin 2
    • Marion D., Zasloff M., and Bax A. A two-dimensional NMR study of the antimicrobial peptide magainin 2. FEBS Lett. 227 (1988) 21-26
    • (1988) FEBS Lett. , vol.227 , pp. 21-26
    • Marion, D.1    Zasloff, M.2    Bax, A.3
  • 44
    • 0023735907 scopus 로고
    • Synthetic magainin analogues with improved antimicrobial activity
    • Chen H.C., Brown J.H., Morell J.L., and Huang C.M. Synthetic magainin analogues with improved antimicrobial activity. FEBS Lett. 236 (1988) 462-466
    • (1988) FEBS Lett. , vol.236 , pp. 462-466
    • Chen, H.C.1    Brown, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 45
    • 0032849898 scopus 로고    scopus 로고
    • The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers. The effects of charges and pH
    • Vogt T.C., and Bechinger B. The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers. The effects of charges and pH. J. Biol. Chem. 274 (1999) 29115-29121
    • (1999) J. Biol. Chem. , vol.274 , pp. 29115-29121
    • Vogt, T.C.1    Bechinger, B.2
  • 46
    • 0033543167 scopus 로고    scopus 로고
    • Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure
    • Wieprecht T., Beyermann M., and Seelig J. Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure. Biochemistry 38 (1999) 10377-10387
    • (1999) Biochemistry , vol.38 , pp. 10377-10387
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 47
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: two-state model
    • Huang H.W. Action of antimicrobial peptides: two-state model. Biochemistry 39 (2000) 8347-8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 48
    • 0003401938 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, Norfolk, UK
    • Matsuzaki K. Molecular mechanisms of membrane perturbation by antimicrobial peptides. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, Norfolk, UK 167-181
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 167-181
    • Matsuzaki, K.1
  • 49
    • 2142768752 scopus 로고    scopus 로고
    • Molecular mechanism of cell selectivity by linear amphipathic-helical and diasteriomeric antimicrobial peptides
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, Norfolk, UK
    • Shai Z.O.Y. Molecular mechanism of cell selectivity by linear amphipathic-helical and diasteriomeric antimicrobial peptides. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, Norfolk, UK 183-204
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 183-204
    • Shai, Z.O.Y.1
  • 50
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols-model ion channels
    • Sansom M.S. Alamethicin and related peptaibols-model ion channels. Eur. Biophys. J. 22 (1993) 105-124
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.1
  • 51
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • Hallock K.J., Lee D.K., Omnaas J., Mosberg H.I., and Ramamoorthy A. Membrane composition determines pardaxin's mechanism of lipid bilayer disruption. Biophys. J. 83 (2002) 1004-1013
    • (2002) Biophys. J. , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 52
    • 7744229375 scopus 로고    scopus 로고
    • Structure and orientation of pardaxin determined by NMR experiments in model membranes
    • Porcelli F., Buck B., Lee D.K., Hallock K.J., Ramamoorthy A., and Veglia G. Structure and orientation of pardaxin determined by NMR experiments in model membranes. J. Biol. Chem. 279 (2004) 45815-45823
    • (2004) J. Biol. Chem. , vol.279 , pp. 45815-45823
    • Porcelli, F.1    Buck, B.2    Lee, D.K.3    Hallock, K.J.4    Ramamoorthy, A.5    Veglia, G.6
  • 53
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • Lohner K., and Prenner E.J. Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim. Biophys. Acta 1462 (1999) 141-156
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 54
    • 0002336563 scopus 로고    scopus 로고
    • The role of membrane lipid composition in cell targeting of antimicrobial peptides
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, Norfolk, UK
    • Lohner K. The role of membrane lipid composition in cell targeting of antimicrobial peptides. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, Norfolk, UK 149-165
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1
  • 55
    • 0024438756 scopus 로고
    • Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
    • Duclohier H., Molle G., and Spach G. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56 (1989) 1017-1021
    • (1989) Biophys. J. , vol.56 , pp. 1017-1021
    • Duclohier, H.1    Molle, G.2    Spach, G.3
  • 57
    • 0029616370 scopus 로고
    • Magainin-induced cytotoxicity in eukaryotic cells: kinetics, dose-response and channel characteristics
    • Haimovich B., and Tanaka J.C. Magainin-induced cytotoxicity in eukaryotic cells: kinetics, dose-response and channel characteristics. Biochim. Biophys. Acta 1240 (1995) 149-158
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 149-158
    • Haimovich, B.1    Tanaka, J.C.2
  • 58
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobal 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. An antimicrobal peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35 (1996) 11361-11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 60
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang L., Harroun T.A., Weiss T.M., Ding L., and Huang H.W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81 (2001) 1475-1485
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 61
    • 3042620560 scopus 로고    scopus 로고
    • Structure and function of membrane-lytic peptides
    • Bechinger B. Structure and function of membrane-lytic peptides. Crit. Rev. Plant Sci. 23 (2004) 271-292
    • (2004) Crit. Rev. Plant Sci. , vol.23 , pp. 271-292
    • Bechinger, B.1
  • 62
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny Y., Rapaport D., Mor A., Nicolas P., and Shai Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31 (1992) 12416-12423
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 64
    • 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. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2 (1993) 2077-2084
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 65
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z., and Shai Y. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47 (1998) 451-463
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 66
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects
    • Steiner H., Andreu D., and Merrifield R.B. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta 939 (1988) 260-266
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 67
  • 68
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen B., Fink J., Merrifield R.B., and Mauzerall D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 5072-5076
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 69
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides by multidimensional solid-state NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462 (1999) 157-183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 70
    • 20444400818 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy study
    • 31P solid-state NMR spectroscopy study. Biochim. Biophys. Acta 1712 (2005) 101-108
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 101-108
    • Bechinger, B.1
  • 71
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock K.J., Lee D.K., and Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84 (2003) 3052-3060
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 72
    • 0026084947 scopus 로고
    • Effects of small organic molecules on phospholipid phase transitions
    • Lohner K. Effects of small organic molecules on phospholipid phase transitions. Chem. Phys. Lipids 57 (1991) 341-362
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 341-362
    • Lohner, K.1
  • 73
    • 0020474447 scopus 로고
    • Stabilization of bilayer structure for unsaturated phosphatidylethanolamines by detergents
    • Madden T.D., and Cullis P.R. Stabilization of bilayer structure for unsaturated phosphatidylethanolamines by detergents. Biochim. Biophys. Acta 684 (1982) 149-153
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 149-153
    • Madden, T.D.1    Cullis, P.R.2
  • 74
    • 4243639317 scopus 로고
    • The effect of the detergent cetyltrimethaylammoniumchloride on the phase behavior of Dipalmitoylphosphatidylcholine. A high precision calorimetric studies
    • Müller K., LIPKA G., Lohner K., and Laggner P. The effect of the detergent cetyltrimethaylammoniumchloride on the phase behavior of Dipalmitoylphosphatidylcholine. A high precision calorimetric studies. Thermochim. Acta 94 (1985) 187-197
    • (1985) Thermochim. Acta , vol.94 , pp. 187-197
    • Müller, K.1    LIPKA, G.2    Lohner, K.3    Laggner, P.4
  • 75
    • 0027460820 scopus 로고
    • Solid-state NMR determination of intra- and intermolecular 31P-13C distances for shikimate 3-phosphate and [1-13C]glyphosate bound to enolpyruvylshikimate-3-phosphate synthase
    • Christensen A.M., and Schaefer J. Solid-state NMR determination of intra- and intermolecular 31P-13C distances for shikimate 3-phosphate and [1-13C]glyphosate bound to enolpyruvylshikimate-3-phosphate synthase. Biochemistry 32 (1993) 2868-2873
    • (1993) Biochemistry , vol.32 , pp. 2868-2873
    • Christensen, A.M.1    Schaefer, J.2
  • 76
    • 0017696015 scopus 로고
    • Triton X-100 as a channel-forming substance in artificial lipid bilayer membranes
    • Schlieper P., and De Robertis E. Triton X-100 as a channel-forming substance in artificial lipid bilayer membranes. Arch. Biochem. Biophys. 184 (1977) 204-208
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 204-208
    • Schlieper, P.1    De Robertis, E.2
  • 78
    • 0018844896 scopus 로고
    • The appearance of single-ion channels in unmodified lipid bilayer membranes at the phase transition temperature
    • Antonov V.F., Petrov V.V., Molnar A.A., Predvoditelev D.A., and Ivanov A.S. The appearance of single-ion channels in unmodified lipid bilayer membranes at the phase transition temperature. Nature 283 (1980) 585-586
    • (1980) Nature , vol.283 , pp. 585-586
    • Antonov, V.F.1    Petrov, V.V.2    Molnar, A.A.3    Predvoditelev, D.A.4    Ivanov, A.S.5
  • 79
    • 0020823426 scopus 로고
    • The induction by protons of ion channels through lipid bilayer membranes
    • Kaufmann K., and Silman I. The induction by protons of ion channels through lipid bilayer membranes. Biophys. Chem. 18 (1983) 89-99
    • (1983) Biophys. Chem. , vol.18 , pp. 89-99
    • Kaufmann, K.1    Silman, I.2
  • 80
    • 0023895717 scopus 로고
    • Electrical oscillation and fluctuation in phospholipid membranes. Phospholipids can form a channel without protein
    • Yoshikawa K., Fujimoto T., Shimooka T., Terada H., Kumazawa N., and Ishii T. Electrical oscillation and fluctuation in phospholipid membranes. Phospholipids can form a channel without protein. Biophys. Chem. 29 (1988) 293-299
    • (1988) Biophys. Chem. , vol.29 , pp. 293-299
    • Yoshikawa, K.1    Fujimoto, T.2    Shimooka, T.3    Terada, H.4    Kumazawa, N.5    Ishii, T.6
  • 81
    • 0024369039 scopus 로고
    • Pure lipid vesicles can induce channel-like conductances in planar bilayers
    • Woodbury D.J. Pure lipid vesicles can induce channel-like conductances in planar bilayers. J. Membr. Biol. 109 (1989) 145-150
    • (1989) J. Membr. Biol. , vol.109 , pp. 145-150
    • Woodbury, D.J.1
  • 82
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • Miteva M., Andersson M., Karshikoff A., and Otting G. Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin. FEBS Lett. 462 (1999) 155-158
    • (1999) FEBS Lett. , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 83
    • 0020479083 scopus 로고
    • The structure of melittin: I. Structure determination and partial refinement
    • Terwilliger T.C., and Eisenberg D. The structure of melittin: I. Structure determination and partial refinement. J. Biol. Chem. 257 (1982) 6010-6015
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 84
    • 0019872076 scopus 로고
    • Physicochemical studies on delta Haemolysin, a Staphylococcal cytolytic polypeptide
    • Fitton J.E. Physicochemical studies on delta Haemolysin, a Staphylococcal cytolytic polypeptide. FEBS Lett. 130 (1981) 257-260
    • (1981) FEBS Lett. , vol.130 , pp. 257-260
    • Fitton, J.E.1
  • 85
    • 0025963949 scopus 로고
    • The amphiphilic a-helix concept. Consequences on the structure of staphylococcal d-toxin in solution and bound to lipids
    • Thiaudiere E., Siffert O., Talbot J.-C., Bolard J., Alouf J.E., and Dufourcq J. The amphiphilic a-helix concept. Consequences on the structure of staphylococcal d-toxin in solution and bound to lipids. Eur. J. Biochem. 195 (1991) 203-213
    • (1991) Eur. J. Biochem. , vol.195 , pp. 203-213
    • Thiaudiere, E.1    Siffert, O.2    Talbot, J.-C.3    Bolard, J.4    Alouf, J.E.5    Dufourcq, J.6
  • 86
    • 0034705132 scopus 로고    scopus 로고
    • Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function
    • Oren Z., and Shai Y. Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function. Biochemistry 39 (2000) 6103-6114
    • (2000) Biochemistry , vol.39 , pp. 6103-6114
    • Oren, Z.1    Shai, Y.2
  • 87
    • 0037053317 scopus 로고    scopus 로고
    • Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives
    • Kustanovich I., Shalev D.E., Mikhlin M., Gaidukov L., and Mor A. Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives. J. Biol. Chem. 277 (2002) 16941-16951
    • (2002) J. Biol. Chem. , vol.277 , pp. 16941-16951
    • Kustanovich, I.1    Shalev, D.E.2    Mikhlin, M.3    Gaidukov, L.4    Mor, A.5
  • 88
    • 1142298536 scopus 로고    scopus 로고
    • Aggregation and water-membrane partition as major determinants of the activity of the antibiotic peptide trichogin GA IV
    • Stella L., Mazzuca C., Venanzi M., Palleschi A., Didone M., Formaggio F., Toniolo C., and Pispisa B. Aggregation and water-membrane partition as major determinants of the activity of the antibiotic peptide trichogin GA IV. Biophys. J. 86 (2004) 936-945
    • (2004) Biophys. J. , vol.86 , pp. 936-945
    • Stella, L.1    Mazzuca, C.2    Venanzi, M.3    Palleschi, A.4    Didone, M.5    Formaggio, F.6    Toniolo, C.7    Pispisa, B.8
  • 90
    • 0026519219 scopus 로고
    • Trichogin A IV, an 11-residue lipopeptaibol from Trichoderma longibrachiatum
    • Auvin-Guette C., Rebufatt S., Prigent Y., and Bodo B. Trichogin A IV, an 11-residue lipopeptaibol from Trichoderma longibrachiatum. J. Am. Chem. Soc. 114 (1992) 2170-2174
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2170-2174
    • Auvin-Guette, C.1    Rebufatt, S.2    Prigent, Y.3    Bodo, B.4
  • 92
    • 0036786839 scopus 로고    scopus 로고
    • Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells
    • Sal-Man N., Oren Z., and Shai Y. Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells. Biochemistry 41 (2002) 11921-11930
    • (2002) Biochemistry , vol.41 , pp. 11921-11930
    • Sal-Man, N.1    Oren, Z.2    Shai, Y.3
  • 93
    • 0026788013 scopus 로고
    • Mechanism of magainin 2a induced permeabilization of phospholipid vesicles
    • Grant Jr. E., Beeler T.J., Taylor K.M., Gable K., and Roseman M.A. Mechanism of magainin 2a induced permeabilization of phospholipid vesicles. Biochemistry 31 (1992) 9912-9918
    • (1992) Biochemistry , vol.31 , pp. 9912-9918
    • Grant Jr., E.1    Beeler, T.J.2    Taylor, K.M.3    Gable, K.4    Roseman, M.A.5
  • 94
    • 0034910318 scopus 로고    scopus 로고
    • Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: nucleation model of defect formation
    • Polozov I.V., Anantharamaiah G.M., Segrest J.P., and Epand R.M. Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: nucleation model of defect formation. Biophys. J. 81 (2001) 949-959
    • (2001) Biophys. J. , vol.81 , pp. 949-959
    • Polozov, I.V.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Epand, R.M.4
  • 95
    • 0027990232 scopus 로고
    • Ability of cecropin B to penetrate the enterobacterial outer membrane
    • Vaara M., and Vaara T. Ability of cecropin B to penetrate the enterobacterial outer membrane. Antimicrob. Agents Chemother. 38 (1994) 2498-2501
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2498-2501
    • Vaara, M.1    Vaara, T.2
  • 97
    • 0025247787 scopus 로고
    • Interaction of surfactants with model and biological membranes: II. Effect of N-alkyl-N,N,N-trimethylammonium ions on phosphatidylcholine bilayers as studied by spin probe ESR
    • Gallova J., Devinsky F., and Balgavy P. Interaction of surfactants with model and biological membranes: II. Effect of N-alkyl-N,N,N-trimethylammonium ions on phosphatidylcholine bilayers as studied by spin probe ESR. Chem. Phys. Lipids 53 (1990) 231-241
    • (1990) Chem. Phys. Lipids , vol.53 , pp. 231-241
    • Gallova, J.1    Devinsky, F.2    Balgavy, P.3
  • 98
    • 0021761592 scopus 로고
    • Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions
    • Simon S.A., and McIntosh T.J. Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions. Biochim. Biophys. Acta 773 (1984) 169-172
    • (1984) Biochim. Biophys. Acta , vol.773 , pp. 169-172
    • Simon, S.A.1    McIntosh, T.J.2
  • 99
    • 1442323941 scopus 로고    scopus 로고
    • Effects of non-ionic surfactants N-alkyl-N,N-dimethylamine-N-oxides on the structure of a phospholipid bilayer: small-angle X-ray diffraction study
    • Karlovska J., Lohner K., Degovics G., Lacko I., Devinsky F., and Balgavy P. Effects of non-ionic surfactants N-alkyl-N,N-dimethylamine-N-oxides on the structure of a phospholipid bilayer: small-angle X-ray diffraction study. Chem. Phys. Lipids 129 (2004) 31-41
    • (2004) Chem. Phys. Lipids , vol.129 , pp. 31-41
    • Karlovska, J.1    Lohner, K.2    Degovics, G.3    Lacko, I.4    Devinsky, F.5    Balgavy, P.6
  • 100
    • 0030581202 scopus 로고    scopus 로고
    • Cut-off effects in biological activities of surfactants
    • Balgavy P., and Devinsky F. Cut-off effects in biological activities of surfactants. Adv. Colloid Interface Sci. 66 (1996) 23-63
    • (1996) Adv. Colloid Interface Sci. , vol.66 , pp. 23-63
    • Balgavy, P.1    Devinsky, F.2
  • 102
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis P.R., and de Kruijff B. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    de Kruijff, B.2
  • 104
    • 0027139908 scopus 로고
    • Ultrasonic study of melittin effects on phospholipid model membranes
    • Colotto A., Kharakoz D.P., Lohner K., and Laggner P. Ultrasonic study of melittin effects on phospholipid model membranes. Biophys. J. 65 (1993) 2360-2367
    • (1993) Biophys. J. , vol.65 , pp. 2360-2367
    • Colotto, A.1    Kharakoz, D.P.2    Lohner, K.3    Laggner, P.4
  • 106
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin A.S., and White S.H. 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim. Biophys. Acta 1514 (2001) 253-260
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 107
    • 0021099105 scopus 로고
    • Cooperative effects in the interaction between melittin and phosphatidylcholine model membranes. Studies by temperature scanning densitometry
    • Posch M., Rakusch U., Mollay C., and Laggner P. Cooperative effects in the interaction between melittin and phosphatidylcholine model membranes. Studies by temperature scanning densitometry. J. Biol. Chem. 258 (1983) 1761-1766
    • (1983) J. Biol. Chem. , vol.258 , pp. 1761-1766
    • Posch, M.1    Rakusch, U.2    Mollay, C.3    Laggner, P.4
  • 108
    • 0344871874 scopus 로고
    • Low-dose effects of melittin on phospholipid structure. Differences between diester and diether phospholipids
    • Collotto A., Lohner K., and Laggner P. Low-dose effects of melittin on phospholipid structure. Differences between diester and diether phospholipids. Prog. Colloid Polym. Sci. 89 (1992) 334
    • (1992) Prog. Colloid Polym. Sci. , vol.89 , pp. 334
    • Collotto, A.1    Lohner, K.2    Laggner, P.3
  • 109
    • 0027511498 scopus 로고
    • Percolation and diffusion in three-component lipid bilayers: effect of cholesterol on an equimolar mixture of two phosphatidylcholines
    • Almeida P.F., Vaz W.L., and Thompson T.E. Percolation and diffusion in three-component lipid bilayers: effect of cholesterol on an equimolar mixture of two phosphatidylcholines. Biophys. J. 64 (1993) 399-412
    • (1993) Biophys. J. , vol.64 , pp. 399-412
    • Almeida, P.F.1    Vaz, W.L.2    Thompson, T.E.3
  • 110
    • 0022516431 scopus 로고
    • Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles
    • Dufourcq J., Faucon J.F., Fourche G., Dasseux J.L., le Maire M., and Gulik-Krzywicki T. Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles. Biochim. Biophys. Acta 859 (1986) 33-48
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 33-48
    • Dufourcq, J.1    Faucon, J.F.2    Fourche, G.3    Dasseux, J.L.4    le Maire, M.5    Gulik-Krzywicki, T.6
  • 111
    • 0028804445 scopus 로고
    • Modulation of melittin-induced lysis by surface charge density of membranes
    • Monette M., and Lafleur M. Modulation of melittin-induced lysis by surface charge density of membranes. Biophys. J. 68 (1995) 187-195
    • (1995) Biophys. J. , vol.68 , pp. 187-195
    • Monette, M.1    Lafleur, M.2
  • 112
    • 0022980372 scopus 로고
    • Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR
    • Dufourc E.J., Smith I.C., and Dufourcq J. Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR. Biochemistry 25 (1986) 6448-6455
    • (1986) Biochemistry , vol.25 , pp. 6448-6455
    • Dufourc, E.J.1    Smith, I.C.2    Dufourcq, J.3
  • 113
    • 0023648310 scopus 로고
    • A deuterium and phosphorus-31 nuclear magnetic resonance study of the interaction of melittin with dimyristoylphosphatidylcholine bilayers and the effects of contaminating phospholipase A2
    • Dempsey C.E., and Watts A. A deuterium and phosphorus-31 nuclear magnetic resonance study of the interaction of melittin with dimyristoylphosphatidylcholine bilayers and the effects of contaminating phospholipase A2. Biochemistry 26 (1987) 5803-5811
    • (1987) Biochemistry , vol.26 , pp. 5803-5811
    • Dempsey, C.E.1    Watts, A.2
  • 114
    • 0028965734 scopus 로고
    • Acyl chain length dependence in the stability of melittin-phosphatidylcholine complexes. A light scattering and 31P-NMR study
    • Faucon J.F., Bonmatin J.M., Dufourcq J., and Dufourc E.J. Acyl chain length dependence in the stability of melittin-phosphatidylcholine complexes. A light scattering and 31P-NMR study. Biochim. Biophys. Acta 1234 (1995) 235-243
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 235-243
    • Faucon, J.F.1    Bonmatin, J.M.2    Dufourcq, J.3    Dufourc, E.J.4
  • 115
    • 0038853451 scopus 로고
    • Dilatometric and calorimetric studies of the effect of Staphylococcus aureus delta-lysin on the phospholipid phase transition
    • Lohner K., Laggner P., and Freer J.H. Dilatometric and calorimetric studies of the effect of Staphylococcus aureus delta-lysin on the phospholipid phase transition. J. Solution Chem. 15 (1986) 189-198
    • (1986) J. Solution Chem. , vol.15 , pp. 189-198
    • Lohner, K.1    Laggner, P.2    Freer, J.H.3
  • 116
    • 0033554837 scopus 로고    scopus 로고
    • Effect of staphylococcal delta-lysin on the thermotropic phase behavior and vesicle morphology of dimyristoylphosphatidylcholine lipid bilayer model membranes. Differential scanning calorimetric, 31P nuclear magnetic resonance and Fourier transform infrared spectroscopic, and X-ray diffraction studies
    • Lohner K., Staudegger E., Prenner E.J., Lewis R.N., Kriechbaum M., Degovics G., and McElhaney R.N. Effect of staphylococcal delta-lysin on the thermotropic phase behavior and vesicle morphology of dimyristoylphosphatidylcholine lipid bilayer model membranes. Differential scanning calorimetric, 31P nuclear magnetic resonance and Fourier transform infrared spectroscopic, and X-ray diffraction studies. Biochemistry 38 (1999) 16514-16528
    • (1999) Biochemistry , vol.38 , pp. 16514-16528
    • Lohner, K.1    Staudegger, E.2    Prenner, E.J.3    Lewis, R.N.4    Kriechbaum, M.5    Degovics, G.6    McElhaney, R.N.7
  • 117
    • 0002551242 scopus 로고
    • Easman C.S.F., and Easman C.A. (Eds), Academic Press, London
    • Thelestam M. In: Easman C.S.F., and Easman C.A. (Eds). Staphylococci and Staphylococcal Diseases (1983), Academic Press, London 705-744
    • (1983) Staphylococci and Staphylococcal Diseases , pp. 705-744
    • Thelestam, M.1
  • 118
    • 0023688987 scopus 로고
    • Properties of ion channels formed by Staphylococcus aureus delta-toxin
    • Mellor I.R., Thomas D.H., and Sansom M.S. Properties of ion channels formed by Staphylococcus aureus delta-toxin. Biochim. Biophys. Acta 942 (1988) 280-294
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 280-294
    • Mellor, I.R.1    Thomas, D.H.2    Sansom, M.S.3
  • 119
    • 0024278460 scopus 로고
    • Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines
    • Batenburg A.M., van Esch J.H., and de Kruijff B. Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines. Biochemistry 27 (1988) 2324-2331
    • (1988) Biochemistry , vol.27 , pp. 2324-2331
    • Batenburg, A.M.1    van Esch, J.H.2    de Kruijff, B.3
  • 121
    • 0023626564 scopus 로고
    • Interaction of melittin with negatively charged phospholipids: consequences for lipid organization
    • Batenburg A.M., van Esch J.H., Leunissen-Bijvelt J., Verkleij A.J., and de Kruijff B. Interaction of melittin with negatively charged phospholipids: consequences for lipid organization. FEBS Lett. 223 (1987) 148-154
    • (1987) FEBS Lett. , vol.223 , pp. 148-154
    • Batenburg, A.M.1    van Esch, J.H.2    Leunissen-Bijvelt, J.3    Verkleij, A.J.4    de Kruijff, B.5
  • 122
    • 0023192005 scopus 로고
    • Lipid specific penetration of melittin into phospholipid model membranes
    • Batenburg A.M., Hibbeln J.C., and de Kruijff B. Lipid specific penetration of melittin into phospholipid model membranes. Biochim. Biophys. Acta 903 (1987) 155-165
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 155-165
    • Batenburg, A.M.1    Hibbeln, J.C.2    de Kruijff, B.3
  • 123
    • 0000284138 scopus 로고
    • Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR
    • Dempsey C., Bitbol M., and Watts A. Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR. Biochemistry 28 (1989) 6590-6596
    • (1989) Biochemistry , vol.28 , pp. 6590-6596
    • Dempsey, C.1    Bitbol, M.2    Watts, A.3
  • 125
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli F., Buck-Koehntop B.A., Thennarasu S., Ramamoorthy A., and Veglia G. Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry 45 (2006) 5793-5799
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 126
  • 127
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke S., He K., and Huang H. Membrane thinning caused by magainin 2. Biochemistry 34 (1995) 16764-16769
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 128
    • 0033965650 scopus 로고    scopus 로고
    • Grazing incidence X-ray scattering of highly aligned phospholipid membranes containing antimicrobial peptides magainin 2
    • Münster C., Lu Y., Schinzel S., Bechinger B., and Salditt T. Grazing incidence X-ray scattering of highly aligned phospholipid membranes containing antimicrobial peptides magainin 2. Eur. Biophys. J. 28 (1999) 683-688
    • (1999) Eur. Biophys. J. , vol.28 , pp. 683-688
    • Münster, C.1    Lu, Y.2    Schinzel, S.3    Bechinger, B.4    Salditt, T.5
  • 129
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen F.Y., Lee M.T., and Huang H.W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84 (2003) 3751-3758
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 130
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers
    • Mecke A., Lee D.K., Ramamoorthy A., Orr B.G., and Banaszak Holl M.M. Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers. Biophys. J. 89 (2005) 4043-4050
    • (2005) Biophys. J. , vol.89 , pp. 4043-4050
    • Mecke, A.1    Lee, D.K.2    Ramamoorthy, A.3    Orr, B.G.4    Banaszak Holl, M.M.5
  • 131
    • 0026742166 scopus 로고
    • Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation
    • Bechinger B., Zasloff M., and Opella S.J. Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. Biophys. J. 62 (1992) 12-14
    • (1992) Biophys. J. , vol.62 , pp. 12-14
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 132
    • 33646594751 scopus 로고    scopus 로고
    • A high-resolution solid-state NMR approach for the structural studies of bicelles
    • Dvinskikh S., Durr U., Yamamoto K., and Ramamoorthy A. A high-resolution solid-state NMR approach for the structural studies of bicelles. J. Am. Chem. Soc. 128 (2006) 6326-6327
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6326-6327
    • Dvinskikh, S.1    Durr, U.2    Yamamoto, K.3    Ramamoorthy, A.4
  • 133
    • 33644925279 scopus 로고    scopus 로고
    • The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes
    • Mason A.J., Matinez A., Glaubitz C., Danos O., Kichler A., and Bechinger B. The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes. FASEB J. 20 (2006) 320-322
    • (2006) FASEB J. , vol.20 , pp. 320-322
    • Mason, A.J.1    Matinez, A.2    Glaubitz, C.3    Danos, O.4    Kichler, A.5    Bechinger, B.6
  • 134
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide pleurocidin
    • Mason A.J., Husnal-Chotimah I.N., Bertani P., and Bechinger B. A spectroscopic study of the membrane interaction of the antimicrobial peptide pleurocidin. Mol. Membr. Biol. 23 (2006) 185-194
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 185-194
    • Mason, A.J.1    Husnal-Chotimah, I.N.2    Bertani, P.3    Bechinger, B.4
  • 135
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • Lohner K., Latal A., Lehrer R.I., and Ganz T. Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems. Biochemistry 36 (1997) 1525-1531
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 136
    • 0034687122 scopus 로고    scopus 로고
    • Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study
    • Bonev B.B., Chan W.C., Bycroft B.W., Roberts G.C., and Watts A. Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study. Biochemistry 39 (2000) 11425-11433
    • (2000) Biochemistry , vol.39 , pp. 11425-11433
    • Bonev, B.B.1    Chan, W.C.2    Bycroft, B.W.3    Roberts, G.C.4    Watts, A.5
  • 137
    • 0030863833 scopus 로고    scopus 로고
    • Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids
    • Latal A., Degovics G., Epand R.F., Epand R.M., and Lohner K. Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. Eur. J. Biochem. 248 (1997) 938-946
    • (1997) Eur. J. Biochem. , vol.248 , pp. 938-946
    • Latal, A.1    Degovics, G.2    Epand, R.F.3    Epand, R.M.4    Lohner, K.5
  • 138
    • 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. Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor. Biochemistry 39 (2000) 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
  • 139
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus), isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S., Niwa M., Takao T., and Shimonishi Y. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus), isolation and chemical structure. J. Biol. Chem. 263 (1988) 16709-16713
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 141
    • 0033009036 scopus 로고    scopus 로고
    • Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes
    • Prenner E.J., Lewis R.N., Kondejewski L.H., Hodges R.S., and McElhaney R.N. Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes. Biochim. Biophys. Acta 1417 (1999) 211-223
    • (1999) Biochim. Biophys. Acta , vol.1417 , pp. 211-223
    • Prenner, E.J.1    Lewis, R.N.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5
  • 142
    • 2442492150 scopus 로고    scopus 로고
    • The cyclic antimicrobial peptide RTD-1 induces stabilized lipid-peptide domains more efficiently than its open-chain analogue
    • Abuja P.M., Zenz A., Trabi M., Craik D.J., and Lohner K. The cyclic antimicrobial peptide RTD-1 induces stabilized lipid-peptide domains more efficiently than its open-chain analogue. FEBS Lett. 566 (2004) 301-306
    • (2004) FEBS Lett. , vol.566 , pp. 301-306
    • Abuja, P.M.1    Zenz, A.2    Trabi, M.3    Craik, D.J.4    Lohner, K.5
  • 143
    • 0030047564 scopus 로고    scopus 로고
    • Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study
    • Demel R.A., Peelen T., Siezen R.J., de Kruijff B., and Kuipers O.P. Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study. Eur. J. Biochem. 235 (1996) 267-274
    • (1996) Eur. J. Biochem. , vol.235 , pp. 267-274
    • Demel, R.A.1    Peelen, T.2    Siezen, R.J.3    de Kruijff, B.4    Kuipers, O.P.5
  • 144
    • 0029881913 scopus 로고    scopus 로고
    • Cardiotoxin II segregates phosphatidylglycerol from mixtures with phosphatidylcholine: (31)P and (2)H NMR spectroscopic evidence
    • Carbone M.A., and Macdonald P.M. Cardiotoxin II segregates phosphatidylglycerol from mixtures with phosphatidylcholine: (31)P and (2)H NMR spectroscopic evidence. Biochemistry 35 (1996) 3368-3378
    • (1996) Biochemistry , vol.35 , pp. 3368-3378
    • Carbone, M.A.1    Macdonald, P.M.2
  • 145
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta 1376 (1998) 353-368
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 146
    • 0025278001 scopus 로고
    • Ion-channel properties of mastoparan, a 14-residue peptide from wasp venom, and of MP3, a 12-residue analogue
    • Mellor I.R., and Sansom M.S. Ion-channel properties of mastoparan, a 14-residue peptide from wasp venom, and of MP3, a 12-residue analogue. Proc. R. Soc. London, B Biol. Sci. 239 (1990) 383-400
    • (1990) Proc. R. Soc. London, B Biol. Sci. , vol.239 , pp. 383-400
    • Mellor, I.R.1    Sansom, M.S.2
  • 148
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear J.D., Wasserman Z.R., and DeGrado W.F. Synthetic amphiphilic peptide models for protein ion channels. Science 240 (1988) 1177-1181
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 149
    • 0025756511 scopus 로고
    • Formation of ion channels in planar lipid bilayer membranes by synthetic basic peptides
    • Anzai K., Hamasuna M., Kadono H., Lee S., Aoyagi H., and Kirino Y. Formation of ion channels in planar lipid bilayer membranes by synthetic basic peptides. Biochim. Biophys. Acta 1064 (1991) 256-266
    • (1991) Biochim. Biophys. Acta , vol.1064 , pp. 256-266
    • Anzai, K.1    Hamasuna, M.2    Kadono, H.3    Lee, S.4    Aoyagi, H.5    Kirino, Y.6
  • 150
    • 0032930050 scopus 로고    scopus 로고
    • Structure-function relationship of model Aib-containing peptides as ion transfer intermembrane templates
    • Higashimoto Y., Kodama H., Jelokhani-Niaraki M., Kato F., and Kondo M. Structure-function relationship of model Aib-containing peptides as ion transfer intermembrane templates. J. Biochem. (Tokyo) 125 (1999) 705-712
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 705-712
    • Higashimoto, Y.1    Kodama, H.2    Jelokhani-Niaraki, M.3    Kato, F.4    Kondo, M.5
  • 151
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle S.E., and Houghten R.A. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 31 (1992) 12688-12694
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 152
    • 0036257707 scopus 로고    scopus 로고
    • Development of short antimicrobial peptides derived from host defense peptides or by combinatorial libraries
    • Lee K.H. Development of short antimicrobial peptides derived from host defense peptides or by combinatorial libraries. Curr. Pharm. Des. 8 (2002) 795-813
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 795-813
    • Lee, K.H.1
  • 153
    • 0038192455 scopus 로고    scopus 로고
    • The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes
    • Beven L., Castano S., Dufourcq J., Wieslander A., and Wroblewski H. The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur. J. Biochem. 270 (2003) 2207-2217
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2207-2217
    • Beven, L.1    Castano, S.2    Dufourcq, J.3    Wieslander, A.4    Wroblewski, H.5
  • 154
    • 0037716304 scopus 로고    scopus 로고
    • Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin
    • Schroder-Borm H., Willumeit R., Brandenburg K., and Andra J. Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin. Biochim. Biophys. Acta 1612 (2003) 164-171
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 164-171
    • Schroder-Borm, H.1    Willumeit, R.2    Brandenburg, K.3    Andra, J.4
  • 155
    • 0023644485 scopus 로고
    • Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly)
    • Nakajima Y., Qu X.M., and Natori S. Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly). J. Biol. Chem. 262 (1987) 1665-1669
    • (1987) J. Biol. Chem. , vol.262 , pp. 1665-1669
    • Nakajima, Y.1    Qu, X.M.2    Natori, S.3
  • 157
    • 21844443548 scopus 로고    scopus 로고
    • Permeabilization of raft-containing lipid vesicles by delta-lysin: a mechanism for cell sensitivity to cytotoxic peptides
    • Pokorny A., and Almeida P.F. Permeabilization of raft-containing lipid vesicles by delta-lysin: a mechanism for cell sensitivity to cytotoxic peptides. Biochemistry 44 (2005) 9538-9544
    • (2005) Biochemistry , vol.44 , pp. 9538-9544
    • Pokorny, A.1    Almeida, P.F.2
  • 158
    • 29244449637 scopus 로고    scopus 로고
    • A simple theory of peptide interactions on a membrane surface: excluded volume and entropic order
    • Almeida P.F., and Wiegel F.W. A simple theory of peptide interactions on a membrane surface: excluded volume and entropic order. J. Theor. Biol. 238 (2006) 269-278
    • (2006) J. Theor. Biol. , vol.238 , pp. 269-278
    • Almeida, P.F.1    Wiegel, F.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.