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Volumn 8, Issue 10, 2013, Pages

Biophysical Investigation of the Membrane-Disrupting Mechanism of the Antimicrobial and Amyloid-Like Peptide Dermaseptin S9

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOLYTE; AMYLOID; ANION; CATION; DERMASEPTIN S9; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84885405196     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075528     Document Type: Article
Times cited : (43)

References (56)
  • 1
    • 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
  • 2
    • 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, (1999) 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: 55-70.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 3
    • 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, et al. (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35: 12612-12622.
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5
  • 4
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper HE, Kramer NE, Smith JL, Hillman JD, Zachariah C, et al. (2006) An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313: 1636-1637.
    • (2006) Science , vol.313 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5
  • 5
    • 0035479424 scopus 로고    scopus 로고
    • Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin AS, White SH, (2001) 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim Biophys Acta 1514: 253-260.
    • (2001) Biochim Biophys Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 6
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights
    • Ramamoorthy A, (2009) Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights. Solid State Nucl Magn Reson 35: 201-207.
    • (2009) Solid State Nucl Magn Reson , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 7
    • 84877737915 scopus 로고    scopus 로고
    • Lipid Composition-Dependent Membrane Fragmentation and Pore-Forming Mechanisms of Membrane Disruption by Pexiganan (MSI-78)
    • Lee DK, Brender JR, Sciacca MF, Krishnamoorthy J, Yu C, et al. (2013) Lipid Composition-Dependent Membrane Fragmentation and Pore-Forming Mechanisms of Membrane Disruption by Pexiganan (MSI-78). Biochemistry.
    • (2013) Biochemistry
    • Lee, D.K.1    Brender, J.R.2    Sciacca, M.F.3    Krishnamoorthy, J.4    Yu, C.5
  • 8
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P, Mor A, (1995) Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu Rev Microbiol 49: 277-304.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 9
    • 0038706380 scopus 로고    scopus 로고
    • Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain
    • Vanhoye D, Bruston F, Nicolas P, Amiche M, (2003) Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Eur J Biochem 270: 2068-2081.
    • (2003) Eur J Biochem , vol.270 , pp. 2068-2081
    • Vanhoye, D.1    Bruston, F.2    Nicolas, P.3    Amiche, M.4
  • 10
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu LP, Deber CM, (1998) Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47: 41-62.
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2
  • 11
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • Stark M, Liu LP, Deber CM, (2002) Cationic hydrophobic peptides with antimicrobial activity. Antimicrob Agents Chemother 46: 3585-3590.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3585-3590
    • Stark, M.1    Liu, L.P.2    Deber, C.M.3
  • 12
    • 4644245658 scopus 로고    scopus 로고
    • Helix induction in antimicrobial peptides by alginate in biofilms
    • Chan C, Burrows LL, Deber CM, (2004) Helix induction in antimicrobial peptides by alginate in biofilms. J Biol Chem 279: 38749-38754.
    • (2004) J Biol Chem , vol.279 , pp. 38749-38754
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 13
    • 30744459874 scopus 로고    scopus 로고
    • Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini
    • Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, et al. (2006) Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. Biochemistry 45: 468-480.
    • (2006) Biochemistry , vol.45 , pp. 468-480
    • Lequin, O.1    Ladram, A.2    Chabbert, L.3    Bruston, F.4    Convert, O.5
  • 14
    • 48249143665 scopus 로고    scopus 로고
    • Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9
    • Auvynet C, El Amri C, Lacombe C, Bruston F, Bourdais J, et al. (2008) Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9. FEBS J 275: 4134-4151.
    • (2008) FEBS J , vol.275 , pp. 4134-4151
    • Auvynet, C.1    El Amri, C.2    Lacombe, C.3    Bruston, F.4    Bourdais, J.5
  • 15
    • 0014779155 scopus 로고
    • 2 Dimensional Thin Layer Chromatographic Separation of Polar Lipids and Determination of Phospholipids by Phosphorus Analysis of Spots
    • Rouser G, Fleische.S, Yamamoto A, (1970) 2 Dimensional Thin Layer Chromatographic Separation of Polar Lipids and Determination of Phospholipids by Phosphorus Analysis of Spots. Lipids 5: 494-&.
    • (1970) Lipids , vol.5 , pp. 494
    • Rouser, G.1    Fleische, S.2    Yamamoto, A.3
  • 18
    • 33846618622 scopus 로고    scopus 로고
    • Dimerization of Neu/Erb2 transmembrane domain is controlled by membrane curvature
    • Khemtémourian L, Buchoux S, Aussenac F, Dufourc EJ, (2007) Dimerization of Neu/Erb2 transmembrane domain is controlled by membrane curvature. Eur Biophys J 36: 107-112.
    • (2007) Eur Biophys J , vol.36 , pp. 107-112
    • Khemtémourian, L.1    Buchoux, S.2    Aussenac, F.3    Dufourc, E.J.4
  • 19
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N, Woody RW, (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209: 32-44.
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 20
    • 0032952095 scopus 로고    scopus 로고
    • Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic LiKj(i = 2j) peptides
    • Castano S, Desbat B, Laguerre M, Dufourcq J, (1999) Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic LiKj(i = 2j) peptides. Biochim Biophys Acta 1416: 176-194.
    • (1999) Biochim Biophys Acta , vol.1416 , pp. 176-194
    • Castano, S.1    Desbat, B.2    Laguerre, M.3    Dufourcq, J.4
  • 21
    • 0033957859 scopus 로고    scopus 로고
    • Ideally amphipathic beta-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL)(m)K peptides
    • Castano S, Desbat B, Dufourcq J, (2000) Ideally amphipathic beta-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL)(m)K peptides. Biochim Biophys Acta 1463: 65-80.
    • (2000) Biochim Biophys Acta , vol.1463 , pp. 65-80
    • Castano, S.1    Desbat, B.2    Dufourcq, J.3
  • 22
    • 0000745176 scopus 로고
    • Quadrupolar Echo Deuteron Magnetic-Resonance Spectroscopy in Ordered Hydrocarbon Chains
    • Davis JH, Jeffrey KR, Bloom M, Valic MI, Higgs TP, (1976) Quadrupolar Echo Deuteron Magnetic-Resonance Spectroscopy in Ordered Hydrocarbon Chains. Chem Phys Lett 42: 390-394.
    • (1976) Chem Phys Lett , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 23
    • 2442767079 scopus 로고
    • Obtaining High-Fidelity Spin-1/2 Powder Spectra in Anisotropic Media - Phase-Cycled Hahn Echo Spectroscopy
    • Rance M, Byrd RA, (1983) Obtaining High-Fidelity Spin-1/2 Powder Spectra in Anisotropic Media- Phase-Cycled Hahn Echo Spectroscopy. J Magnet Res 52: 221-240.
    • (1983) J Magnet Res , vol.52 , pp. 221-240
    • Rance, M.1    Byrd, R.A.2
  • 24
    • 0346213760 scopus 로고
    • Direct Determination of the Oriented Sample Nmr-Spectrum from the Powder Spectrum for Systems with Local Axial Symmetry
    • Bloom M, Davis JH, Mackay AL, (1981) Direct Determination of the Oriented Sample Nmr-Spectrum from the Powder Spectrum for Systems with Local Axial Symmetry. Chem Phys Lett 80: 198-202.
    • (1981) Chem Phys Lett , vol.80 , pp. 198-202
    • Bloom, M.1    Davis, J.H.2    Mackay, A.L.3
  • 25
    • 36849108707 scopus 로고
    • Deuteron Quadrupole Coupling Constants in 3 Solid Deuterated Paraffin Hydrocarbons-C2d6, C4d10, C6d14
    • Burnett LJ, Muller BH, (1971) Deuteron Quadrupole Coupling Constants in 3 Solid Deuterated Paraffin Hydrocarbons-C2d6, C4d10, C6d14. J Chem Phys 55: 5829-&.
    • (1971) J Chem Phys , vol.55 , pp. 5829
    • Burnett, L.J.1    Muller, B.H.2
  • 26
    • 56049097681 scopus 로고    scopus 로고
    • Surfactin-triggered small vesicle formation of negatively charged membranes: A novel membrane-lysis mechanism
    • Buchoux S, Lai-Kee-Him J, Garnier M, Tsan P, Besson F, et al. (2008) Surfactin-triggered small vesicle formation of negatively charged membranes: A novel membrane-lysis mechanism. Biophys J 95: 3840-3849.
    • (2008) Biophys J , vol.95 , pp. 3840-3849
    • Buchoux, S.1    Lai-Kee-Him, J.2    Garnier, M.3    Tsan, P.4    Besson, F.5
  • 27
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers
    • Demel RA, Geurts van Kessel WS, Zwaal RF, Roelofsen B, van Deenen LL, (1975) Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim Biophys Acta 406: 97-107.
    • (1975) Biochim Biophys Acta , vol.406 , pp. 97-107
    • Demel, R.A.1    Geurts van Kessel, W.S.2    Zwaal, R.F.3    Roelofsen, B.4    van Deenen, L.L.5
  • 28
    • 67349258550 scopus 로고    scopus 로고
    • Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers
    • Calvez P, Bussieres S, Eric D, Salesse C, (2009) Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers. Biochimie 91: 718-733.
    • (2009) Biochimie , vol.91 , pp. 718-733
    • Calvez, P.1    Bussieres, S.2    Eric, D.3    Salesse, C.4
  • 29
    • 3042546066 scopus 로고    scopus 로고
    • Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin
    • Ambroggio EE, Separovic F, Bowie J, Fidelio GD, (2004) Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin. Biochim Biophys Acta 1664: 31-37.
    • (2004) Biochim Biophys Acta , vol.1664 , pp. 31-37
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.3    Fidelio, G.D.4
  • 30
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H, (1999) Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309: 274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine, H.1
  • 31
    • 61649121892 scopus 로고    scopus 로고
    • Amyloid aggregation on lipid bilayers and its impact on membrane permeability
    • Friedman R, Pellarin R, Caflisch A, (2009) Amyloid aggregation on lipid bilayers and its impact on membrane permeability. J Mol Biol 387: 407-415.
    • (2009) J Mol Biol , vol.387 , pp. 407-415
    • Friedman, R.1    Pellarin, R.2    Caflisch, A.3
  • 32
    • 72749086820 scopus 로고    scopus 로고
    • Impaired Processing of Human Pro-Islet Amyloid Polypeptide Is Not a Causative Factor for Fibril Formation or Membrane Damage in Vitro
    • Khemtémourian L, Casarramona GL, Suylen DPL, Hackeng TM, Meeldijk JD, et al. (2009) Impaired Processing of Human Pro-Islet Amyloid Polypeptide Is Not a Causative Factor for Fibril Formation or Membrane Damage in Vitro. Biochemistry 48: 10918-10925.
    • (2009) Biochemistry , vol.48 , pp. 10918-10925
    • Khemtémourian, L.1    Casarramona, G.L.2    Suylen, D.P.L.3    Hackeng, T.M.4    Meeldijk, J.D.5
  • 33
    • 68749107071 scopus 로고    scopus 로고
    • Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
    • Joanne P, Galanth C, Goasdoue N, Nicolas P, Sagan S, et al. (2009) Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry. Biochim Biophys Acta 1788: 1772-1781.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1772-1781
    • Joanne, P.1    Galanth, C.2    Goasdoue, N.3    Nicolas, P.4    Sagan, S.5
  • 34
    • 78649801857 scopus 로고    scopus 로고
    • Different membrane behaviour and cellular uptake of three basic arginine-rich peptides
    • Walrant A, Correia I, Jiao CY, Lequin O, Bent EH, et al. (2011) Different membrane behaviour and cellular uptake of three basic arginine-rich peptides. Biochim Biophys Acta 1808: 382-393.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 382-393
    • Walrant, A.1    Correia, I.2    Jiao, C.Y.3    Lequin, O.4    Bent, E.H.5
  • 35
    • 84863986217 scopus 로고    scopus 로고
    • ERalpha17p, a peptide reproducing the hinge region of the estrogen receptor alpha associates to biological membranes: A biophysical approach
    • Byrne C, Khemtémourian L, Pelekanou V, Kampa M, Leclercq G, et al. (2012) ERalpha17p, a peptide reproducing the hinge region of the estrogen receptor alpha associates to biological membranes: A biophysical approach. Steroids 77: 979-987.
    • (2012) Steroids , vol.77 , pp. 979-987
    • Byrne, C.1    Khemtémourian, L.2    Pelekanou, V.3    Kampa, M.4    Leclercq, G.5
  • 36
    • 0034929069 scopus 로고    scopus 로고
    • Electrostatic peptide-lipid interactions of amyloid-beta peptide and pentalysine with membrane surfaces monitored by P-31 MAS NMR
    • Bonev B, Watts A, Bokvist M, Grobner G, (2001) Electrostatic peptide-lipid interactions of amyloid-beta peptide and pentalysine with membrane surfaces monitored by P-31 MAS NMR. Phys Chem Chem Phys 3: 2904-2910.
    • (2001) Phys Chem Chem Phys , vol.3 , pp. 2904-2910
    • Bonev, B.1    Watts, A.2    Bokvist, M.3    Grobner, G.4
  • 37
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • Seelig J, (1978) 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes. Biochim Biophys Acta 515: 105-140.
    • (1978) Biochim Biophys Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 38
    • 53249147452 scopus 로고    scopus 로고
    • Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study
    • Abbassi F, Galanth C, Amiche M, Saito K, Piesse C, et al. (2008) Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study. Biochemistry 47: 10513-10525.
    • (2008) Biochemistry , vol.47 , pp. 10513-10525
    • Abbassi, F.1    Galanth, C.2    Amiche, M.3    Saito, K.4    Piesse, C.5
  • 39
    • 77954656341 scopus 로고    scopus 로고
    • The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition
    • Khemtémourian L, Engel MF, Liskamp RM, Höppener JWM, Killian JA, (2010) The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition. Biochim Biophys Acta 1798: 1805-1811.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1805-1811
    • Khemtémourian, L.1    Engel, M.F.2    Liskamp, R.M.3    Höppener, J.W.M.4    Killian, J.A.5
  • 40
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • Knight JD, Miranker AD, (2004) Phospholipid catalysis of diabetic amyloid assembly. J Mol Biol 341: 1175-1187.
    • (2004) J Mol Biol , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 41
    • 14344250143 scopus 로고    scopus 로고
    • Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers
    • Zhao H, Jutila A, Nurminen T, Wickstrom SA, Keski-Oja J, et al. (2005) Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 44: 2857-2863.
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5
  • 42
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action
    • Zhao H, Sood R, Jutila A, Bose S, Fimland G, et al. (2006) Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action. Biochim Biophys Acta 1758: 1461-1474.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5
  • 43
    • 33847668734 scopus 로고    scopus 로고
    • Fluorescent temporin B derivative and its binding to liposomes
    • Sood R, Domanov Y, Kinnunen PK, (2007) Fluorescent temporin B derivative and its binding to liposomes. J Fluoresc 17: 223-234.
    • (2007) J Fluoresc , vol.17 , pp. 223-234
    • Sood, R.1    Domanov, Y.2    Kinnunen, P.K.3
  • 44
    • 79953133327 scopus 로고    scopus 로고
    • Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species
    • Jan A, Adolfsson O, Allaman I, Buccarello AL, Magistretti PJ, et al. (2011) Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species. J Biol Chem 286: 8585-8596.
    • (2011) J Biol Chem , vol.286 , pp. 8585-8596
    • Jan, A.1    Adolfsson, O.2    Allaman, I.3    Buccarello, A.L.4    Magistretti, P.J.5
  • 46
    • 84858632761 scopus 로고    scopus 로고
    • Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
    • Brender JR, Salamekh S, Ramamoorthy A, (2012) Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective. Acc Chem Res 45: 454-462.
    • (2012) Acc Chem Res , vol.45 , pp. 454-462
    • Brender, J.R.1    Salamekh, S.2    Ramamoorthy, A.3
  • 47
    • 0037379826 scopus 로고    scopus 로고
    • Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A
    • Ivanova VP, Makarov IM, Schaffer TE, Heimburg T, (2003) Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A. Biophys J. 84: 2427-2439.
    • (2003) Biophys J , vol.84 , pp. 2427-2439
    • Ivanova, V.P.1    Makarov, I.M.2    Schaffer, T.E.3    Heimburg, T.4
  • 48
    • 0030071247 scopus 로고    scopus 로고
    • A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering
    • Heimburg T, Biltonen RL, (1996) A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering. Biophys J 70: 84-96.
    • (1996) Biophys J , vol.70 , pp. 84-96
    • Heimburg, T.1    Biltonen, R.L.2
  • 49
    • 67349205034 scopus 로고    scopus 로고
    • Membrane order perturbation in the presence of antimicrobial peptides by 2H solid-state NMR spectroscopy
    • Salnikov ES, Mason AJ, Bechinger B, (2009) Membrane order perturbation in the presence of antimicrobial peptides by 2H solid-state NMR spectroscopy. Biochimie 91: 734-743.
    • (2009) Biochimie , vol.91 , pp. 734-743
    • Salnikov, E.S.1    Mason, A.J.2    Bechinger, B.3
  • 50
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin
    • Mason AJ, Chotimah IN, Bertani P, Bechinger B, (2006) A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin. Mol Membr Biol 23: 185-194.
    • (2006) Mol Membr Biol , vol.23 , pp. 185-194
    • Mason, A.J.1    Chotimah, I.N.2    Bertani, P.3    Bechinger, B.4
  • 51
    • 37349109207 scopus 로고    scopus 로고
    • Membrane interaction of chrysophsin-1, a histidine-rich antimicrobial peptide from red sea bream
    • Mason AJ, Bertani P, Moulay G, Marquette A, Perrone B, et al. (2007) Membrane interaction of chrysophsin-1, a histidine-rich antimicrobial peptide from red sea bream. Biochemistry 46: 15175-15187.
    • (2007) Biochemistry , vol.46 , pp. 15175-15187
    • Mason, A.J.1    Bertani, P.2    Moulay, G.3    Marquette, A.4    Perrone, B.5
  • 52
    • 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, Thennarasu S, Lee DK, Tan A, Maloy L, (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
  • 53
    • 33646231496 scopus 로고    scopus 로고
    • Cell selectivity correlates with membrane-specific interactions: a case study on the antimicrobial peptide G15 derived from granulysin
    • Ramamoorthy A, Thennarasu S, Tan A, Lee DK, Clayberger C, et al. (2006) Cell selectivity correlates with membrane-specific interactions: a case study on the antimicrobial peptide G15 derived from granulysin. Biochim Biophys Acta 1758: 154-163.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 154-163
    • Ramamoorthy, A.1    Thennarasu, S.2    Tan, A.3    Lee, D.K.4    Clayberger, C.5
  • 54
    • 0025135466 scopus 로고
    • Delta-haemolysin from Staphylococcus aureus and model membranes. A solid-state 2H-NMR and 31P-NMR study
    • Dufourc EJ, Dufourcq J, Birkbeck TH, Freer JH, (1990) Delta-haemolysin from Staphylococcus aureus and model membranes. A solid-state 2H-NMR and 31P-NMR study. Eur J Biochem 187: 581-587.
    • (1990) Eur J Biochem , vol.187 , pp. 581-587
    • Dufourc, E.J.1    Dufourcq, J.2    Birkbeck, T.H.3    Freer, J.H.4
  • 55
    • 0022980372 scopus 로고
    • Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR
    • Dufourc EJ, Smith IC, Dufourcq J, (1986) Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR. Biochemistry 25: 6448-6455.
    • (1986) Biochemistry , vol.25 , pp. 6448-6455
    • Dufourc, E.J.1    Smith, I.C.2    Dufourcq, J.3
  • 56
    • 79960092012 scopus 로고    scopus 로고
    • Interactions of the Antimicrobial Peptide Maculatin 1.1 and Analogues with Phospholipid Bilayers
    • Fernandez DI, Sani MA, Separovic F, (2011) Interactions of the Antimicrobial Peptide Maculatin 1.1 and Analogues with Phospholipid Bilayers. Austr J Chem 64: 798-805.
    • (2011) Austr J Chem , vol.64 , pp. 798-805
    • Fernandez, D.I.1    Sani, M.A.2    Separovic, F.3


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