메뉴 건너뛰기




Volumn 13, Issue 7, 2012, Pages 620-631

Membrane interacting peptides: From killers to helpers

Author keywords

Beta sheet ; CD; Cyclic ; Electron microscopy; Helical ; IR; Linear peptides; Membrane crossing; Membrane leakage; Membrane reinforcement; Molecular dynamics; NMR; X rays

Indexed keywords

ALAMETHICIN; ANTIBIOTIC AGENT; CECROPIN B; CHOLESTEROL; CYCLOPEPTIDE; GROWTH FACTOR RECEPTOR; HEMOLYSIN; LANTIBIOTIC; MASTOPARAN; MELITTIN; MEMBRANE INTERACTING PEPTIDE; METENKEPHALIN; NISIN; PEPTIDE; PHOSPHATIDYLCHOLINE; PROTEIN BAX; SPHINGOLIPID; SPHINGOSINE; SURFACTIN; UNCLASSIFIED DRUG;

EID: 84874866161     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312804142138     Document Type: Review
Times cited : (22)

References (92)
  • 1
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M.; Vogel, H. J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta-Biomembr., 1999, 1462, 11-28.
    • (1999) Biochim. Biophys. Acta-Biomembr , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 2
    • 0023100945 scopus 로고
    • Biosynthesis and degradation of peptides derived from Xenopus-Laevis Prohormones
    • Giovannini, M. G.; Poulter, L.; Gibson, B. W.; Williams, D. H. Biosynthesis and degradation of peptides derived from Xenopus-Laevis Prohormones. Biochem. J., 1987, 243, 113-120.
    • (1987) Biochem. J , vol.243 , pp. 113-120
    • Giovannini, M.G.1    Poulter, L.2    Gibson, B.W.3    Williams, D.H.4
  • 3
    • 0020985676 scopus 로고
    • A novel peptide designated pyla and its precursor as predicted from cloned messenger-RNA of xenopus-laevis skin
    • Hoffmann, W.; Richter, K.; Kreil, G. A novel peptide designated pyla and its precursor as predicted from cloned messenger-RNA of xenopus-laevis skin. Embo J., 1983, 2, 711-714.
    • (1983) Embo J , vol.2 , pp. 711-714
    • Hoffmann, W.1    Richter, K.2    Kreil, G.3
  • 4
    • 50549170868 scopus 로고
    • Uber das Giftsekret der Gelbbauchunke, Bombina variegata L (Primary structure of two oligopeptides of the toxin of Bombina variegata L.)
    • Kiss, G.; Michl, H. Uber das Giftsekret der Gelbbauchunke, Bombina variegata L (Primary structure of two oligopeptides of the toxin of Bombina variegata L.). Toxicon, 1962, 1, 33-34.
    • (1962) Toxicon , vol.1 , pp. 33-34
    • Kiss, G.1    Michl, H.2
  • 5
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq, J. L.; Bulet, P.; Hetru, C.; Hoffmann, J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 1998, 47, 465-477.
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 6
    • 58149376976 scopus 로고    scopus 로고
    • The Epidermal Growth Factor Receptor Ligands at a Glance
    • Schneider, M. R.; Wolf, E. The Epidermal Growth Factor Receptor Ligands at a Glance. J. Cell. Physiol., 2009, 218, 460-466.
    • (2009) J. Cell. Physiol , vol.218 , pp. 460-466
    • Schneider, M.R.1    Wolf, E.2
  • 7
    • 54749145468 scopus 로고    scopus 로고
    • Peptide probes for protein transmembrane domains
    • Slivka, P. F.; Wong, J.; Caputo, G. A.; Yin, H. Peptide probes for protein transmembrane domains. ACS Chem. Biol., 2008, 3, 402-411.
    • (2008) ACS Chem. Biol , vol.3 , pp. 402-411
    • Slivka, P.F.1    Wong, J.2    Caputo, G.A.3    Yin, H.4
  • 8
    • 49249106612 scopus 로고    scopus 로고
    • Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins
    • Brunger, A. T.; Jin, R.; Breidenbach, M. A. Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins. Cell. Mol. Life Sci., 2008, 65, 2296-2306.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 2296-2306
    • Brunger, A.T.1    Jin, R.2    Breidenbach, M.A.3
  • 9
    • 0347541112 scopus 로고    scopus 로고
    • Detailed structure and dynamics of bicelle phospholipids using selectively deuterated and perdeuterated labels. H-2 NMR and molecular mechanics study
    • Aussenac, F.; Laguerre, M.; Schmitter, J. M.; Dufourc, E. J. Detailed structure and dynamics of bicelle phospholipids using selectively deuterated and perdeuterated labels. H-2 NMR and molecular mechanics study. Langmuir, 2003, 19, 10468-10479.
    • (2003) Langmuir , vol.19 , pp. 10468-10479
    • Aussenac, F.1    Laguerre, M.2    Schmitter, J.M.3    Dufourc, E.J.4
  • 10
    • 34249811510 scopus 로고    scopus 로고
    • Plant sterols in rafts: A better way to regulate membrane thermal shocks
    • Beck, J. G.; Mathieu, D.; Loudet, C.; Buchoux, S.; Dufourc, E. J. Plant sterols in rafts: a better way to regulate membrane thermal shocks. Faseb J., 2007, 21, 1714-1723.
    • (2007) Faseb J , vol.21 , pp. 1714-1723
    • Beck, J.G.1    Mathieu, D.2    Loudet, C.3    Buchoux, S.4    Dufourc, E.J.5
  • 11
    • 56049097681 scopus 로고    scopus 로고
    • Surfactin-triggered small vesicle formation of negatively charged membranes: A novel membranelysis mechanism
    • Buchoux, S.; Lai-Kee-Him, J.; Garnier, M.; Tsan, P.; Besson, F.; Brisson, A.; Dufourc, E. J. Surfactin-triggered small vesicle formation of negatively charged membranes: A novel membranelysis mechanism. Biophys. J., 2008, 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    Brisson, A.6    Dufourc, E.J.7
  • 12
    • 70349780373 scopus 로고    scopus 로고
    • Cytochrome c interaction with neutral lipid membranes: Influence of lipid packing and protein charges
    • El Kirat, K.; Morandat, S. Cytochrome c interaction with neutral lipid membranes: influence of lipid packing and protein charges. Chem. Phys. Lipids, 2009, 162, 17-24.
    • (2009) Chem. Phys. Lipids , vol.162 , pp. 17-24
    • El Kirat, K.1    Morandat, S.2
  • 13
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a bax-derived peptide: Effect on the line tension of the membrane probed by AFM
    • Garcia-Saez, A. J.; Chiantia, S.; Salgado, J.; Schwille, P. Pore formation by a bax-derived peptide: Effect on the line tension of the membrane probed by AFM. Biophys. J., 2007, 93, 103-112.
    • (2007) Biophys. J , vol.93 , pp. 103-112
    • Garcia-Saez, A.J.1    Chiantia, S.2    Salgado, J.3    Schwille, P.4
  • 15
    • 77749306487 scopus 로고    scopus 로고
    • Peptide-Induced Domain Formation in Supported Lipid Bilayers: Direct Evidence by Combined Atomic Force and Polarized Total Internal Reflection Fluorescence Microscopy
    • Oreopoulos, J.; Epand, R. F.; Epand, R. M.; Yip, C. M. Peptide-Induced Domain Formation in Supported Lipid Bilayers: Direct Evidence by Combined Atomic Force and Polarized Total Internal Reflection Fluorescence Microscopy. Biophys. J., 2010, 98, 815-823.
    • (2010) Biophys. J , vol.98 , pp. 815-823
    • Oreopoulos, J.1    Epand, R.F.2    Epand, R.M.3    Yip, C.M.4
  • 16
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and Xray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • Lohner, K.; Prenner, E. J. Differential scanning calorimetry and Xray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim. Biophys. Acta-Biomembr., 1999, 1462, 141-156.
    • (1999) Biochim. Biophys. Acta-Biomembr , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 17
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • Seelig, J. Titration calorimetry of lipid-peptide interactions. Biochim. Biophys. Acta-Rev. Biomembr., 1997, 1331, 103-116.
    • (1997) Biochim. Biophys. Acta-Rev. Biomembr , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 18
    • 0035080814 scopus 로고    scopus 로고
    • The lipid charge density at the bilayer surface modulates the effects of melittin on membranes
    • Pott, T.; Maillet, J. C.; Abad, C.; Campos, A.; Dufourcq, J.; Dufourc, E. J. The lipid charge density at the bilayer surface modulates the effects of melittin on membranes. Chem. Phys. Lipids, 2001, 109, 209-223.
    • (2001) Chem. Phys. Lipids , vol.109 , pp. 209-223
    • Pott, T.1    Maillet, J.C.2    Abad, C.3    Campos, A.4    Dufourcq, J.5    Dufourc, E.J.6
  • 19
    • 0028965734 scopus 로고
    • Acylchain length dependence in the stability of melittinphosphatidylcholine complexes -A light scattering and P-31-NMR study
    • Faucon, J. F.; Bonmatin, J. M.; Dufourcq, J.; Dufourc, E. J. Acylchain length dependence in the stability of melittinphosphatidylcholine complexes -A light scattering and P-31-NMR study. Biochim. Biophys. Acta-Biomembr., 1995, 1234, 235-243.
    • (1995) Biochim. Biophys. Acta-Biomembr , vol.1234 , pp. 235-243
    • Faucon, J.F.1    Bonmatin, J.M.2    Dufourcq, J.3    Dufourc, E.J.4
  • 20
    • 24044479637 scopus 로고    scopus 로고
    • Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi-and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy
    • Castano, S.; Desbat, B. Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi-and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy. Biochim. Biophys. Acta-Biomembr., 2005, 1715, 81-95.
    • (2005) Biochim. Biophys. Acta-Biomembr , vol.1715 , pp. 81-95
    • Castano, S.1    Desbat, B.2
  • 21
    • 33847146719 scopus 로고    scopus 로고
    • Pro-apoptotic bax-alpha 1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes
    • Sani, M. A.; Loudet, C.; Grobner, G.; Dufourc, E. J. Pro-apoptotic bax-alpha 1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes. J. Pept. Sci., 2007, 13, 100-106.
    • (2007) J. Pept. Sci , vol.13 , pp. 100-106
    • Sani, M.A.1    Loudet, C.2    Grobner, G.3    Dufourc, E.J.4
  • 23
    • 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. Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic LiKj(i=2j) peptides. Biochim. Biophys. Acta-Biomembr., 1999, 1416, 176-194.
    • (1999) Biochim. Biophys. Acta-Biomembr , vol.1416 , pp. 176-194
    • Castano, S.1    Desbat, B.2    Laguerre, M.3    Dufourcq, J.4
  • 24
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers -A polarized attenuated total reflection infrared study
    • Frey, S.; Tamm, L. K. Orientation of melittin in phospholipid bilayers -A polarized attenuated total reflection infrared study. Biophys. J., 1991, 60, 922-930.
    • (1991) Biophys. J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 26
    • 58749101895 scopus 로고    scopus 로고
    • Pore Formation Induced by an Antimicrobial Peptide: Electrostatic Effects
    • Jean-Francois, F.; Elezgaray, J.; Berson, P.; Vacher, P.; Dufourc, E. J. Pore Formation Induced by an Antimicrobial Peptide: Electrostatic Effects. Biophys. J., 2008, 95, 5748-5756.
    • (2008) Biophys. J , vol.95 , pp. 5748-5756
    • Jean-Francois, F.1    Elezgaray, J.2    Berson, P.3    Vacher, P.4    Dufourc, E.J.5
  • 27
    • 78651076403 scopus 로고    scopus 로고
    • The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments
    • Bechinger, B.; Resende, J. M.; Aisenbrey, C. The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments. Biophys. Chem., 2011, 153, 115-125.
    • (2011) Biophys. Chem , vol.153 , pp. 115-125
    • Bechinger, B.1    Resende, J.M.2    Aisenbrey, C.3
  • 28
    • 77951692765 scopus 로고    scopus 로고
    • Solid-State NMR Spectroscopy of Oriented Membrane Polypeptides at 100 K with Signal Enhancement by Dynamic Nuclear Polarization
    • Salnikov, E.; Rosay, M.; Pawsey, S.; Ouari, O.; Tordo, P.; Bechinger, B. Solid-State NMR Spectroscopy of Oriented Membrane Polypeptides at 100 K with Signal Enhancement by Dynamic Nuclear Polarization. J. Am. Chem. Soc., 2010, 132, 5940.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 5940
    • Salnikov, E.1    Rosay, M.2    Pawsey, S.3    Ouari, O.4    Tordo, P.5    Bechinger, B.6
  • 29
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of alpha-helices with lipid bilayers: A review of simulation studies
    • Biggin, P. C.; Sansom, M. S. P. Interactions of alpha-helices with lipid bilayers: a review of simulation studies. Biophys. Chem., 1999, 76, 161-183.
    • (1999) Biophys. Chem , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 30
  • 32
    • 58149181485 scopus 로고    scopus 로고
    • Lipids on the move: Simulations of membrane pores, domains, stalks and curves
    • Marrink, S. J.; de Vries, A. H.; Tieleman, D. P. Lipids on the move: Simulations of membrane pores, domains, stalks and curves. Biochim. Biophys. Acta-Biomembr., 2009, 1788, 149-168.
    • (2009) Biochim. Biophys. Acta-Biomembr , vol.1788 , pp. 149-168
    • Marrink, S.J.1    de Vries, A.H.2    Tieleman, D.P.3
  • 33
    • 0032942642 scopus 로고    scopus 로고
    • The amphipathic helix concept: Length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity
    • Castano, S.; Cornut, I.; Buttner, K.; Dasseux, J. L.; Dufourcq, J. The amphipathic helix concept: length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity. Biochim. Biophys. Acta-Biomembr., 1999, 1416, 161-175.
    • (1999) Biochim. Biophys. Acta-Biomembr , vol.1416 , pp. 161-175
    • Castano, S.1    Cornut, I.2    Buttner, K.3    Dasseux, J.L.4    Dufourcq, J.5
  • 34
    • 0028177259 scopus 로고
    • The amphipathic alpha-helix concept -Applications to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin
    • Cornut, I.; Buttner, K.; Dasseux, J. L.; Dufourcq, J. The amphipathic alpha-helix concept -Applications to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin. FEBS Lett., 1994, 349, 29-33.
    • (1994) FEBS Lett , vol.349 , pp. 29-33
    • Cornut, I.1    Buttner, K.2    Dasseux, J.L.3    Dufourcq, J.4
  • 35
    • 34249290759 scopus 로고    scopus 로고
    • Role of amphipathic alpha-helical structural elements in removing cellular cholesterol and protecting against cardiovascular disease
    • Oram, J. F.; Heinecke, J. W. Role of amphipathic alpha-helical structural elements in removing cellular cholesterol and protecting against cardiovascular disease. Future Lipidol., 2007, 2, 185-196.
    • (2007) Future Lipidol , vol.2 , pp. 185-196
    • Oram, J.F.1    Heinecke, J.W.2
  • 36
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito, H.; Lund-Katz, S.; Phillips, M. C. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res., 2004, 43, 350-380.
    • (2004) Prog. Lipid Res , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 37
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. Mode of action of membrane active antimicrobial peptides. Biopolymers, 2002, 66, 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 38
    • 0025963949 scopus 로고
    • The amphipahic alpha-helix concept -Consequences on the structure of staphilococcal delta-toxin in solution and bound to lipids
    • Thiaudiere, E.; Siffert, O.; Talbot, J. C.; Bolard, J.; Alouf, J. E.; Dufourcq, J. The amphipahic alpha-helix concept -Consequences on the structure of staphilococcal delta-toxin in solution and bound to lipids. Eur. J. Biochem., 1991, 195, 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
  • 39
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B.; Lohner, K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta-Biomembr., 2006, 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta-Biomembr , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 40
    • 0000348475 scopus 로고
    • The amphipathic helix in cytotoxic peptides
    • Epand, R. F., Ed.; CRC Press: Boca Raton
    • Cornut, I.; Thiaudière, E.; Dufourcq, J. The amphipathic helix in cytotoxic peptides In The Amphipathic Helix; Epand, R. F., Ed.; CRC Press: Boca Raton, 1993, 173-219.
    • (1993) The Amphipathic Helix , pp. 173-219
    • Cornut, I.1    Thiaudière, E.2    Dufourcq, J.3
  • 41
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin. J. Membr. Biol., 1997, 156, 197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 42
    • 0022455370 scopus 로고
    • Reversible disk-to-vesicle transition of melittin-DPPC complexes triggered by the phospholipid acyl chain melting
    • Dufourc, E. J.; Faucon, J. F.; Fourche, G.; Dufourcq, J.; Gulikkrzywicki, T.; Lemaire, M. Reversible disk-to-vesicle transition of melittin-DPPC complexes triggered by the phospholipid acyl chain melting. FEBS Lett., 1986, 201, 205-209.
    • (1986) FEBS Lett , vol.201 , pp. 205-209
    • Dufourc, E.J.1    Faucon, J.F.2    Fourche, G.3    Dufourcq, J.4    Gulikkrzywicki, T.5    Lemaire, M.6
  • 43
    • 0028919743 scopus 로고
    • Action of melittin on the DPPC-cholesterol liquid-ordered phase -A solid state H-2 NMR and P-31-NMR study
    • Pott, T.; Dufourc, E. J. Action of melittin on the DPPC-cholesterol liquid-ordered phase -A solid state H-2 NMR and P-31-NMR study. Biophys. J., 1995, 68, 965-977.
    • (1995) Biophys. J , vol.68 , pp. 965-977
    • Pott, T.1    Dufourc, E.J.2
  • 44
    • 20444400818 scopus 로고    scopus 로고
    • Detergent-like properties of magainin antibiotic peptides: A P-31 solid-state NMR spectroscopy study
    • Bechinger, B. Detergent-like properties of magainin antibiotic peptides: A P-31 solid-state NMR spectroscopy study. Biochim. Biophys. Acta-Biomembr., 2005, 1712, 101-108.
    • (2005) Biochim. Biophys. Acta-Biomembr , vol.1712 , pp. 101-108
    • Bechinger, B.1
  • 45
    • 0026615218 scopus 로고
    • Delta-toxin and analogs as peptides models for protein ion channels
    • Bladon, C. M.; Bladon, P.; Parkinson, J. A. Delta-toxin and analogs as peptides models for protein ion channels. Biochem. Soc. Trans., 1992, 20, 862-864.
    • (1992) Biochem. Soc. Trans , vol.20 , pp. 862-864
    • Bladon, C.M.1    Bladon, P.2    Parkinson, J.A.3
  • 46
    • 62749134453 scopus 로고    scopus 로고
    • Delta-hemolysin, an update on a membrane-interacting peptide
    • Verdon, J.; Girardin, N.; Lacombe, C.; Berjeaud, J. M.; Hechard, Y. delta-hemolysin, an update on a membrane-interacting peptide. Peptides, 2009, 30, 817-823.
    • (2009) Peptides , vol.30 , pp. 817-823
    • Verdon, J.1    Girardin, N.2    Lacombe, C.3    Berjeaud, J.M.4    Hechard, Y.5
  • 47
    • 53049090332 scopus 로고    scopus 로고
    • A dynamic view of peptides and proteins in membranes
    • Bechinger, B. A dynamic view of peptides and proteins in membranes. Cell. Mol. Life Sci., 2008, 65, 3028-3039.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 3028-3039
    • Bechinger, B.1
  • 48
    • 0026754487 scopus 로고
    • Model ion Channels -Gramicidin and alamethicin
    • Woolley, G. A.; Wallace, B. A. Model ion Channels -Gramicidin and alamethicin. J. Membr. Biol., 1992, 129, 109-136.
    • (1992) J. Membr. Biol , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 49
  • 50
    • 43649098591 scopus 로고    scopus 로고
    • Structure of the alamethicin pore reconstructed by x-ray diffraction analysis
    • Qian, S.; Wang, W. C.; Yang, L.; Huang, H. W. Structure of the alamethicin pore reconstructed by x-ray diffraction analysis. Biophys. J., 2008, 94, 3512-3522.
    • (2008) Biophys. J , vol.94 , pp. 3512-3522
    • Qian, S.1    Wang, W.C.2    Yang, L.3    Huang, H.W.4
  • 51
    • 0032738473 scopus 로고    scopus 로고
    • Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: Determination and biological specificity
    • Blondelle, S. E.; Lohner, K.; Aguilar, M. I. Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity. Biochim. Biophys. Acta-Biomembr., 1999, 1462, 89-108.
    • (1999) Biochim. Biophys. Acta-Biomembr , vol.1462 , pp. 89-108
    • Blondelle, S.E.1    Lohner, K.2    Aguilar, M.I.3
  • 52
    • 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.; 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 Throughput. Screen, 2005, 8, 241-256.
    • (2005) Comb. Chem. High Throughput. Screen , vol.8 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 54
    • 0031830332 scopus 로고    scopus 로고
    • Recent advances in the high resolution structures of bacterial channels: Gramicidin A
    • Wallace, B. A. Recent advances in the high resolution structures of bacterial channels: Gramicidin A. J. Struct. Biol., 1998, 121, 123-141.
    • (1998) J. Struct. Biol , vol.121 , pp. 123-141
    • Wallace, B.A.1
  • 55
    • 33846618622 scopus 로고    scopus 로고
    • Dimerization of Neu/Erb2 transmembrane domain is controlled by membrane curvature
    • Khemtemourian, L.; Buchoux, S.; Aussenac, F.; Dufourc, E. J. Dimerization of Neu/Erb2 transmembrane domain is controlled by membrane curvature. Euro. Biophys. J., 2007, 36, 107-112.
    • (2007) Euro. Biophys. J , vol.36 , pp. 107-112
    • Khemtemourian, L.1    Buchoux, S.2    Aussenac, F.3    Dufourc, E.J.4
  • 56
    • 0035967525 scopus 로고    scopus 로고
    • Evidence for an alpha-helix -> pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment. A H-1 NMR and circular dichroism study
    • Goetz, M.; Carlotti, C.; Bontems, F.; Dufourc, E. J. Evidence for an alpha-helix -> pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment. A H-1 NMR and circular dichroism study. Biochemistry, 2001, 40, 6534-6540.
    • (2001) Biochemistry , vol.40 , pp. 6534-6540
    • Goetz, M.1    Carlotti, C.2    Bontems, F.3    Dufourc, E.J.4
  • 57
    • 0031903860 scopus 로고    scopus 로고
    • Steady-state compartmentalization of lipid membranes by active proteins
    • Sabra, M. C.; Mouritsen, O. G. Steady-state compartmentalization of lipid membranes by active proteins. Biophys. J., 1998, 74, 745-752.
    • (1998) Biophys. J , vol.74 , pp. 745-752
    • Sabra, M.C.1    Mouritsen, O.G.2
  • 58
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta-Rev. Biomembr., 1998, 1376, 401-416.
    • (1998) Biochim. Biophys. Acta-Rev. Biomembr , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 59
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • Killian, J. A.; Nyholm, T. K. M. Peptides in lipid bilayers: the power of simple models. Curr. Opin. Struct. Biol., 2006, 16, 473-479.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.M.2
  • 61
    • 0001768252 scopus 로고
    • Dependence of lipid-membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness
    • Sperotto, M. M.; Mouritsen, O. G. Dependence of lipid-membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness. Eur. Biophys. J. Biophys. Lett., 1988, 16, 1-10.
    • (1988) Eur. Biophys. J. Biophys. Lett , vol.16 , pp. 1-10
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 62
    • 0033783447 scopus 로고    scopus 로고
    • Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: A CD,N-15 and P-31 solid-state NMR spectroscopy investigation
    • Harzer, U.; Bechinger, B. Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: A CD,N-15 and P-31 solid-state NMR spectroscopy investigation. Biochemistry, 2000, 39, 13106-13114.
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 63
    • 58849139281 scopus 로고    scopus 로고
    • Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented N-15 and P-31 Solid-State NMR Spectroscopy
    • Salnikov, E. S.; Friedrich, H.; Li, X.; Bertani, P.; Reissmann, S.; Hertweck, C.; O'Neil, J. D. J.; Raap, J.; Bechinger, B. Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented N-15 and P-31 Solid-State NMR Spectroscopy. Biophys. J., 2009, 96, 86-100.
    • (2009) Biophys. J , vol.96 , pp. 86-100
    • Salnikov, E.S.1    Friedrich, H.2    Li, X.3    Bertani, P.4    Reissmann, S.5    Hertweck, C.6    O'Neil, J.D.J.7    Raap, J.8    Bechinger, B.9
  • 64
    • 60849120099 scopus 로고    scopus 로고
    • How does the Bax-alpha 1 targeting sequence interact with mitochondrial membranes? The role of cardiolipin
    • Sani, M. A.; Dufourc, E. J.; Grobner, G. How does the Bax-alpha 1 targeting sequence interact with mitochondrial membranes? The role of cardiolipin. Biochim. Biophys. Acta-Biomembr., 2009, 1788, 623-631.
    • (2009) Biochim. Biophys. Acta-Biomembr , vol.1788 , pp. 623-631
    • Sani, M.A.1    Dufourc, E.J.2    Grobner, G.3
  • 66
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Defensins, cathelicidins and histatins
    • De Smet, K.; Contreras, R. Human antimicrobial peptides: defensins, cathelicidins and histatins. Biotechnol. Lett., 2005, 27, 1337-1347.
    • (2005) Biotechnol. Lett , vol.27 , pp. 1337-1347
    • de Smet, K.1    Contreras, R.2
  • 67
    • 62949097134 scopus 로고    scopus 로고
    • Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy
    • Tang, M.; Hong, M. Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy. Mol. Biosyst., 2009, 5, 317-322.
    • (2009) Mol. Biosyst , vol.5 , pp. 317-322
    • Tang, M.1    Hong, M.2
  • 69
    • 38549120838 scopus 로고    scopus 로고
    • The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties
    • Helle, K. B.; Corti, A.; Metz-Boutigue, M. H.; Tota, B. The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties. Cell. Mol. Life Sci., 2007, 64, 2863-2886.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 2863-2886
    • Helle, K.B.1    Corti, A.2    Metz-Boutigue, M.H.3    Tota, B.4
  • 71
    • 45749113323 scopus 로고    scopus 로고
    • Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?
    • Jean-Francois, F.; Castano, S.; Desbat, B.; Odaert, B.; Roux, M.; Metz-Boutigue, M. H.; Dufourc, E. J. Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides? Biochemistry, 2008, 47, 6394-6402.
    • (2008) Biochemistry , vol.47 , pp. 6394-6402
    • Jean-Francois, F.1    Castano, S.2    Desbat, B.3    Odaert, B.4    Roux, M.5    Metz-Boutigue, M.H.6    Dufourc, E.J.7
  • 72
    • 84874883578 scopus 로고    scopus 로고
    • Disordered Pore Formation At Rigid/Fluid Boundary Zones As A New Mechanism For Peptide-Membrane Interaction With The Beta-sheeted Antimicrobial Peptide Cateslytin In
    • Jean-François, F.; Elezgaray, J.; Metz-Boutigue, M. H.; Dufourc, E. J. Disordered Pore Formation At Rigid/Fluid Boundary Zones As A New Mechanism For Peptide-Membrane Interaction With The Beta-sheeted Antimicrobial Peptide Cateslytin In. Biophys. J., 2009, 96, 390A.
    • (2009) Biophys. J , vol.96
    • Jean-François, F.1    Elezgaray, J.2    Metz-Boutigue, M.H.3    Dufourc, E.J.4
  • 73
    • 70350530629 scopus 로고    scopus 로고
    • Selectivity of cateslytin for fungi: The role of acidic lipid-ergosterol membrane fluidity in antimicrobial action
    • Jean-Francois, F.; Desbat, B.; Dufourc, E. J. Selectivity of cateslytin for fungi: the role of acidic lipid-ergosterol membrane fluidity in antimicrobial action. Faseb J., 2009, 23, 3692-3701.
    • (2009) Faseb J , vol.23 , pp. 3692-3701
    • Jean-Francois, F.1    Desbat, B.2    Dufourc, E.J.3
  • 74
    • 29844450350 scopus 로고    scopus 로고
    • Synthesis and secondary structure in membranes of the Bcl-2 anti-apoptotic domain BH4
    • Khemtemourian, L.; Sani, M. A.; Bathany, K.; Grobner, G.; Dufourc, E. J. Synthesis and secondary structure in membranes of the Bcl-2 anti-apoptotic domain BH4. J. Pept. Sci., 2006, 12, 58-64.
    • (2006) J. Pept. Sci , vol.12 , pp. 58-64
    • Khemtemourian, L.1    Sani, M.A.2    Bathany, K.3    Grobner, G.4    Dufourc, E.J.5
  • 75
    • 38149031026 scopus 로고    scopus 로고
    • Restriction of lipid motion in membranes triggered by beta-sheet aggregation of the anti-apoptotic BH4 domain
    • Sani, M. A.; Castano, S.; Dufourc, E. J.; Grobner, G. Restriction of lipid motion in membranes triggered by beta-sheet aggregation of the anti-apoptotic BH4 domain. Febs J., 2008, 275, 561-572.
    • (2008) Febs J , vol.275 , pp. 561-572
    • Sani, M.A.1    Castano, S.2    Dufourc, E.J.3    Grobner, G.4
  • 76
    • 67349088413 scopus 로고    scopus 로고
    • Plant defensins-Prospects for the biological functions and biotechnological properties
    • Carvalho, A. D.; Gomes, V. M. Plant defensins-Prospects for the biological functions and biotechnological properties. Peptides, 2009, 30, 1007-1020.
    • (2009) Peptides , vol.30 , pp. 1007-1020
    • Carvalho, A.D.1    Gomes, V.M.2
  • 77
    • 13844322064 scopus 로고    scopus 로고
    • Defensins -Components of the innate immune system in plants
    • Lay, F. T.; Anderson, M. A. Defensins -Components of the innate immune system in plants. Curr. Protein Pept. Sci., 2005, 6, 85-101.
    • (2005) Curr. Protein Pept. Sci , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.A.2
  • 78
    • 70349206320 scopus 로고    scopus 로고
    • Drosomycin, an essential component of antifungal defence in Drosophila
    • Zhang, Z. T.; Zhu, S. Y. Drosomycin, an essential component of antifungal defence in Drosophila. Insect Mol. Biol., 2009, 18, 549-556.
    • (2009) Insect Mol. Biol , vol.18 , pp. 549-556
    • Zhang, Z.T.1    Zhu, S.Y.2
  • 81
    • 0014409012 scopus 로고
    • Surfactin a crystalline peptidelipid surfactant produced by bacillus subtilis -Isolation characterization and its inhibition of fibrin clot formation
    • Arima, K.; Kakinuma, A.; Tamura, G. Surfactin a crystalline peptidelipid surfactant produced by bacillus subtilis -Isolation characterization and its inhibition of fibrin clot formation. Biochem. Biophys. Res. Commun., 1968, 31, 488-494.
    • (1968) Biochem. Biophys. Res. Commun , vol.31 , pp. 488-494
    • Arima, K.1    Kakinuma, A.2    Tamura, G.3
  • 82
    • 0037742621 scopus 로고    scopus 로고
    • A novel lytic peptide composed of DL-Amino acids selectively kills cancer cells in culture and in mice
    • Papo, N.; Shahar, M.; Eisenbach, L.; Shai, Y. A novel lytic peptide composed of DL-Amino acids selectively kills cancer cells in culture and in mice. J. Biol. Chem., 2003, 278, 21018-21023.
    • (2003) J. Biol. Chem , vol.278 , pp. 21018-21023
    • Papo, N.1    Shahar, M.2    Eisenbach, L.3    Shai, Y.4
  • 83
    • 68749115077 scopus 로고    scopus 로고
    • Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape
    • Bechinger, B. Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape. Curr. Opin. Colloid Interface Sci., 2009, 14, 349-355.
    • (2009) Curr. Opin. Colloid Interface Sci , vol.14 , pp. 349-355
    • Bechinger, B.1
  • 84
    • 0037636145 scopus 로고    scopus 로고
    • Interaction of the neuropeptide Met-enkephalin with zwitterionic and negatively charged bicelles as viewed by P-31 and H-2 solid-state NMR
    • Marcotte, I.; Dufourc, E. J.; Ouellet, M.; Auger, M. Interaction of the neuropeptide Met-enkephalin with zwitterionic and negatively charged bicelles as viewed by P-31 and H-2 solid-state NMR. Biophys. J., 2003, 85, 328-339.
    • (2003) Biophys. J , vol.85 , pp. 328-339
    • Marcotte, I.1    Dufourc, E.J.2    Ouellet, M.3    Auger, M.4
  • 85
    • 0347914575 scopus 로고    scopus 로고
    • Insights, on the interaction of met-enkephalin with negatively charged membranes -an infrared and solid-state NMR spectroscopic study
    • Marcotte, I.; Ouellet, M.; Auger, M. Insights, on the interaction of met-enkephalin with negatively charged membranes -an infrared and solid-state NMR spectroscopic study. Chem. Phys. Lipids, 2004, 127, 175-187.
    • (2004) Chem. Phys. Lipids , vol.127 , pp. 175-187
    • Marcotte, I.1    Ouellet, M.2    Auger, M.3
  • 87
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 1982, 157, 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 88
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C.; White, S. H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol., 1996, 3, 842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 90
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broadspectrum antimicrobial peptide from porcine leukocytes
    • Fahrner, R. L.; Dieckmann, T.; Harwig, S. S. L.; Lehrer, R. I.; Eisenberg, D.; Feigon, J. Solution structure of protegrin-1, a broadspectrum antimicrobial peptide from porcine leukocytes. Chem. Biol., 1996, 3, 543-550.
    • (1996) Chem. Biol , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.L.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 91
    • 0036772907 scopus 로고    scopus 로고
    • Structure of the cathelicidin motif of protegrin-3 precursor: Structural insights into the activation mechanism of an antimicrobial protein
    • Sanchez, J. F.; Hoh, F.; Strub, M. P.; Aumelas, A.; Dumas, C. Structure of the cathelicidin motif of protegrin-3 precursor: Structural insights into the activation mechanism of an antimicrobial protein. Structure, 2002, 10, 1363-1370.
    • (2002) Structure , vol.10 , pp. 1363-1370
    • Sanchez, J.F.1    Hoh, F.2    Strub, M.P.3    Aumelas, A.4    Dumas, C.5
  • 92
    • 33847316946 scopus 로고    scopus 로고
    • Structure and dynamics of surfactin studied by NMR in micellar media
    • Tsan, P.; Volpon, L.; Besson, F.; Lancelin, J. M. Structure and dynamics of surfactin studied by NMR in micellar media. J. Am. Chem. Soc., 2007, 129, 1968-1977.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 1968-1977
    • Tsan, P.1    Volpon, L.2    Besson, F.3    Lancelin, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.