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Volumn 1808, Issue 12, 2011, Pages 2867-2876

Competing interactions for antimicrobial selectivity based on charge complementarity

Author keywords

Antimicrobial peptide; MD simulation; Membrane; Selectivity; Thermodynamic integration

Indexed keywords

COUNTERION; GLYCEROPHOSPHOLIPID; OLEOYLPALMITOYLLECITHIN; PALMITOYLOLEOYLPHOSPHATIDYLGLYCEROL; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN NK 2; UNCLASSIFIED DRUG;

EID: 80052835357     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.08.005     Document Type: Article
Times cited : (23)

References (41)
  • 2
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α helical antimicrobial peptides: A systematic study of the effects of structural and physical properties on biological activity
    • DOI 10.1046/j.0014-2956.2001.02494.x
    • A. Giangaspero, L. Sandri, and A. Tossi Amphipathic alpha helical antimicrobial peptides-a systematic study of the effects of structural and physical properties on biological activity Eur. J. Biochem. 268 21 2001 5589 5600 (Pubitemid 34183324)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.21 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 3
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • M. Dathe, and T. Wieprecht Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells Biochem. Biophys. Acta 1462 1-2 1999 71 87
    • (1999) Biochem. Biophys. Acta , vol.1462 , Issue.12 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 4
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • DOI 10.1146/annurev.biochem.66.1.199
    • W. Dowhan Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66 1997 199 232 (Pubitemid 27274656)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 5
    • 0025876649 scopus 로고
    • Static and dynamic lipid asymmetry in cell membranes
    • P.F. Devaux Static and dynamic lipid asymmetry in cell membranes Biochemistry 30 1991 1163 1173
    • (1991) Biochemistry , vol.30 , pp. 1163-1173
    • Devaux, P.F.1
  • 7
    • 45749113323 scopus 로고    scopus 로고
    • Aggregation of cateslytin β-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?
    • DOI 10.1021/bi800448h
    • F. Jean-Francois, S. Castano, B. Desbat, B. Odaert, M. Roux, M.H. Metz-Boutigue, and E.J. Dufourc Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides? Biochemistry 47 2008 6394 6402 (Pubitemid 351874231)
    • (2008) Biochemistry , vol.47 , Issue.24 , 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
  • 8
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • DOI 10.1016/S0005-2736(97)00051-5, PII S0005273697000515
    • K. Matsuzaki, K. Sugishita, M. Harada, N. Fujii, and K. Miyajima Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria Biochem. Biophys. Acta 1327 1997 119 130 (Pubitemid 27283405)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1327 , Issue.1 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.-I.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 9
    • 0033369108 scopus 로고    scopus 로고
    • Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin
    • DOI 10.1007/s004300050113
    • J. Andrä, and M. Leippe Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin Med. Microbiol. Immunol. 188 1999 117 124 (Pubitemid 30085357)
    • (1999) Medical Microbiology and Immunology , vol.188 , Issue.3 , pp. 117-124
    • Andra, J.1    Leippe, M.2
  • 10
    • 0037716304 scopus 로고    scopus 로고
    • Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin
    • DOI 10.1016/S0005-2736(03)00115-9
    • H. Schröder-Borm, R. Willumeit, K. Brandenburg, and J. Andrä Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin Biochim. Biophys. Acta-Biomembr. 1612 2003 164 171 (Pubitemid 36629570)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1612 , Issue.2 , pp. 164-171
    • Schroder-Borm, H.1    Willumeit, R.2    Brandenburg, K.3    Andra, J.4
  • 13
    • 73149118069 scopus 로고    scopus 로고
    • Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles
    • A. Sayyed-Ahmad, H. Khandelia, and Y.N. Kaznessis Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles Mol. Simul. 35 2009 986 997
    • (2009) Mol. Simul. , vol.35 , pp. 986-997
    • Sayyed-Ahmad, A.1    Khandelia, H.2    Kaznessis, Y.N.3
  • 15
    • 61549084018 scopus 로고    scopus 로고
    • Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: A molecular dynamics study
    • C.H. Davis, and M.L. Berkowitz Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: a molecular dynamics study Biophys. J. 96 2009 785 797
    • (2009) Biophys. J. , vol.96 , pp. 785-797
    • Davis, C.H.1    Berkowitz, M.L.2
  • 16
    • 41149175486 scopus 로고    scopus 로고
    • Prediction of binding free energy for adsorption of antimicrobial peptide lactoferricin B on a POPC membrane
    • 31913-1-31913-11
    • V. Vivcharuk, B. Tomberli, I.S. Tolokh, and C.G. Gray Prediction of binding free energy for adsorption of antimicrobial peptide lactoferricin B on a POPC membrane Phys. Rev. E 77 2008 31913-1-31913-11
    • (2008) Phys. Rev. e , vol.77
    • Vivcharuk, V.1    Tomberli, B.2    Tolokh, I.S.3    Gray, C.G.4
  • 17
    • 70349944668 scopus 로고    scopus 로고
    • Binding free energy and counterion release for adsorption of the antimicrobial peptide lactoferricin B on POPG membrane
    • 31911-1-31911-12
    • I.S. Tolokh, V. Vivcharuk, B. Tomberli, and C.G. Gray Binding free energy and counterion release for adsorption of the antimicrobial peptide lactoferricin B on POPG membrane Phys. Rev. E 80 2009 31911-1-31911-12
    • (2009) Phys. Rev. e , vol.80
    • Tolokh, I.S.1    Vivcharuk, V.2    Tomberli, B.3    Gray, C.G.4
  • 18
    • 77749304229 scopus 로고    scopus 로고
    • Free energy profile of the interaction between a monomer or a dimer of protegrin-1 in a specific binding orientation and a model lipid bilayer
    • V. Vivcharuk, and Y. Kaznessis Free energy profile of the interaction between a monomer or a dimer of protegrin-1 in a specific binding orientation and a model lipid bilayer J. Phys. Chem. B 114 2010 2790 2797
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2790-2797
    • Vivcharuk, V.1    Kaznessis, Y.2
  • 19
    • 70449647113 scopus 로고    scopus 로고
    • Membrane association and selectivity of the antimicrobial peptide NK-2: A molecular dynamics simulation study
    • J. Pimthon, R. Willumeit, A. Lendlein, and D. Hofman Membrane association and selectivity of the antimicrobial peptide NK-2: a molecular dynamics simulation study J. Pept. Sci. 15 2009 654 667
    • (2009) J. Pept. Sci. , vol.15 , pp. 654-667
    • Pimthon, J.1    Willumeit, R.2    Lendlein, A.3    Hofman, D.4
  • 25
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 26
    • 35748967575 scopus 로고    scopus 로고
    • 2H NMR experiments
    • DOI 10.1007/s00249-007-0192-9
    • L.S. Vermeer, B.L. de Groot, V. Reat, A. Milon, and J. Czaplicki Acyl chain order parameter profiles in phospholipid bilayers: computation from molecular dynamics simulations and comparison with 2H NMR experiments Eur. Biophys. J. 36 2007 919 931 (Pubitemid 350045041)
    • (2007) European Biophysics Journal , vol.36 , Issue.8 , pp. 919-931
    • Vermeer, L.S.1    De Groot, B.L.2    Reat, V.3    Milon, A.4    Czaplicki, J.5
  • 27
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • M. Nilges, G.M. Clore, and A.M. Gronenborn Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms FEBS Lett. 239 1988 129 136
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 29
    • 60749090161 scopus 로고    scopus 로고
    • All-atom molecular dynamics simulation studies of fully hydrated gel phase DPPG and DPPE bilayers
    • J. Pimthon, R. Willumeit, A. Lendlein, and D. Hofman All-atom molecular dynamics simulation studies of fully hydrated gel phase DPPG and DPPE bilayers J. Mol. Struct. 921 2009 38 50
    • (2009) J. Mol. Struct. , vol.921 , pp. 38-50
    • Pimthon, J.1    Willumeit, R.2    Lendlein, A.3    Hofman, D.4
  • 30
    • 34250315776 scopus 로고    scopus 로고
    • Molecular characterization of gel and liquid-crystalline structures of fully hydrated POPC and POPE bilayers
    • DOI 10.1021/jp0686339
    • S. Leemkujorn, and A.K. Sum Molecular characterization of gel and liquid-crystalline structures of fully hydrated POPC and POPE bilayers J. Phys. Chem. B 111 2007 6026 6033 (Pubitemid 46918233)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.21 , pp. 6026-6033
    • Leekumjorn, S.1    Sum, A.K.2
  • 32
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • N. Kucerka, S. Tristram-Nagle, and J.F. Nagle Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains J. Membr. Biol. 208 2005 193 202
    • (2005) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 33
    • 0027251833 scopus 로고
    • Area lipid of bilayers from NMR
    • J.F. Nagle Area lipid of bilayers from NMR Biophys. J. 64 1993 1476 1481
    • (1993) Biophys. J. , vol.64 , pp. 1476-1481
    • Nagle, J.F.1
  • 34
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • R.P. Rand, and V.A. Parsegian Hydration forces between phospholipid bilayers Biochim. Biophys. Acta 988 1989 351 376
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 36
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • D. Sengupta, H. Leontiadou, A.E. Mark, and S.J. Marrink Toroidal pores formed by antimicrobial peptides show significant disorder Biochim. Biophys. Acta 1778 2008 2308 2317
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.J.4
  • 39
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • DOI 10.1063/1.1401821
    • I. Andricioaei, and M. Karplus On the calculation of entropy from covariance matrices of the atomic fluctuations J. Chem. Phys. 115 2001 6289 6292 (Pubitemid 33046603)
    • (2001) Journal of Chemical Physics , vol.115 , Issue.14 , pp. 6289-6292
    • Andricioaei, I.1    Karplus, M.2
  • 40
    • 0142185062 scopus 로고    scopus 로고
    • Divalent calcium ions inhibit the penetration of protamine through the polysaccharide brush of the outer membrane of gram-negative bacteria
    • D.A. Pink, L.T. Hansen, T.A. Gill, B.E. Quinn, M.H. Jericho, and T.J. Beveridge Divalent calcium ions inhibit the penetration of protamine through the polysaccharide brush of the outer membrane of gram-negative bacteria Langmuir 19 2003 8852 8858
    • (2003) Langmuir , vol.19 , pp. 8852-8858
    • Pink, D.A.1    Hansen, L.T.2    Gill, T.A.3    Quinn, B.E.4    Jericho, M.H.5    Beveridge, T.J.6


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