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Volumn 1818, Issue 12, 2012, Pages 2975-2981

Binding and reorientation of melittin in a POPC bilayer: Computer simulations

Author keywords

Antimicrobial peptides; Lipid bilayers; Melittin; Molecular dynamics simulations; Pores in bilayers

Indexed keywords

MELITTIN; PHOSPHATIDYLCHOLINE; WATER;

EID: 84865318587     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.07.026     Document Type: Article
Times cited : (57)

References (52)
  • 1
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • H.W. Huang Molecular mechanism of antimicrobial peptides: the origin of cooperativity Biochim. Biophys. Acta Biomembr. 1758 9 2006 1292 1302
    • (2006) Biochim. Biophys. Acta Biomembr. , vol.1758 , Issue.9 , pp. 1292-1302
    • Huang, H.W.1
  • 3
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • P.F. Almeida, and A. Pokorny Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics Biochemistry 48 34 2009 8083 8093
    • (2009) Biochemistry , vol.48 , Issue.34 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 4
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • H. Raghuraman, and A. Chattopadhyay Melittin: a membrane-active peptide with diverse functions Biosci. Rep. 27 4-5 2007 189 223
    • (2007) Biosci. Rep. , vol.27 , Issue.45 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 6
    • 77953724763 scopus 로고    scopus 로고
    • Antimicrobial peptides in toroidal and cylindrical pores
    • M. Mihajlovic, and T. Lazaridis Antimicrobial peptides in toroidal and cylindrical pores Biochim. Biophys. Acta 1798 8 2010 1485 1493
    • (2010) Biochim. Biophys. Acta , vol.1798 , Issue.8 , pp. 1485-1493
    • Mihajlovic, M.1    Lazaridis, T.2
  • 7
    • 74949104869 scopus 로고    scopus 로고
    • Cause and effect of melittin-induced pore formation: A computational approach
    • M. Manna, and C. Mukhopadhyay Cause and effect of melittin-induced pore formation: a computational approach Langmuir 25 20 2009 12235 12242
    • (2009) Langmuir , vol.25 , Issue.20 , pp. 12235-12242
    • Manna, M.1    Mukhopadhyay, C.2
  • 8
    • 79959997001 scopus 로고    scopus 로고
    • Influence of the arrangement and secondary structure of melittin peptides on the formation and stability of toroidal pores
    • S.J. Irudayam, and M.L. Berkowitz Influence of the arrangement and secondary structure of melittin peptides on the formation and stability of toroidal pores Biochim. Biophys. Acta Biomembr. 1808 2011 2258 2266
    • (2011) Biochim. Biophys. Acta Biomembr. , vol.1808 , pp. 2258-2266
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 9
    • 0034068919 scopus 로고    scopus 로고
    • Stability of a melittin pore in a lipid bilayer: A molecular dynamics study
    • J.H. Lin, and A. Baumgaertner Stability of a melittin pore in a lipid bilayer: a molecular dynamics study Biophys. J. 78 4 2000 1714 1724
    • (2000) Biophys. J. , vol.78 , Issue.4 , pp. 1714-1724
    • Lin, J.H.1    Baumgaertner, A.2
  • 11
    • 70350238527 scopus 로고    scopus 로고
    • Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions
    • A.J. Rzepiela, D. Sengupta, N. Goga, and S.J. Marrink Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions Faraday Discuss. 144 2010 431 443
    • (2010) Faraday Discuss. , vol.144 , pp. 431-443
    • Rzepiela, A.J.1    Sengupta, D.2    Goga, N.3    Marrink, S.J.4
  • 12
    • 84858027055 scopus 로고    scopus 로고
    • The difference between Magainin-2 and Melittin assemblies in phosphatidylcholine bilayers: Results from coarse-grained simulations
    • K. Santo, and M.L. Berkowitz The difference between Magainin-2 and Melittin assemblies in phosphatidylcholine bilayers: results from coarse-grained simulations J. Phys. Chem. B 116 9 2012 3021 3030
    • (2012) J. Phys. Chem. B , vol.116 , Issue.9 , pp. 3021-3030
    • Santo, K.1    Berkowitz, M.L.2
  • 13
    • 41149175486 scopus 로고    scopus 로고
    • Prediction of binding free energy for adsorption of antimicrobial peptide lactoferricin B on a POPC membrane
    • 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 3 2008 031913
    • (2008) Phys. Rev. e , vol.77 , Issue.3 , pp. 031913
    • Vivcharuk, V.1    Tomberli, B.2    Tolokh, I.S.3    Gray, C.G.4
  • 14
    • 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 3 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 17
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O. Berger, O. Edholm, and F. Jahnig Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys. J. 72 5 1997 2002 2013
    • (1997) Biophys. J. , vol.72 , Issue.5 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 18
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • S. Nose A unified formulation of the constant temperature molecular dynamics methods J. Chem. Phys. 81 1984 511
    • (1984) J. Chem. Phys. , vol.81 , pp. 511
    • Nose, S.1
  • 19
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 3 1985 1695
    • (1985) Phys. Rev. A , vol.31 , Issue.3 , pp. 1695
    • Hoover, W.G.1
  • 20
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals - A new molecular-dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single crystals - a new molecular-dynamics method J. Appl. Phys. 52 12 1981 7182 7190
    • (1981) J. Appl. Phys. , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 21
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.Log(N) method of Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald - an N.Log(N) method of Ewald sums in large systems J. Chem. Phys. 98 12 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , Issue.12 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 23
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess, H. Bekker, H.J.C. Berendsen, and J.G.E.M. Fraaije LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 18 12 1997 1463 1472
    • (1997) J. Comput. Chem. , vol.18 , Issue.12 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 24
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free, energy calculations on biomolecules. I. the method
    • S. Kumar, J.M. Rosenberg, D. Bouzida, R.H. Swendsen, and P.A. Kollman The weighted histogram analysis method for free, energy calculations on biomolecules. I. The method J. Comput. Chem. 13 8 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , Issue.8 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 25
    • 78651282170 scopus 로고    scopus 로고
    • G-wham - A free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • J.S. Hub, B.L. de Groot, and D. van der Spoel g-wham - a free weighted histogram analysis implementation including robust error and autocorrelation estimates J. Chem. Theory Comput. 2010
    • (2010) J. Chem. Theory Comput.
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 12 1983 2577 2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0141718686 scopus 로고    scopus 로고
    • Alkane adsorption at the water-vapor interface
    • H.S. Ashbaugh, and B.A. Pethica Alkane adsorption at the water-vapor interface Langmuir 19 18 2003 7638 7645
    • (2003) Langmuir , vol.19 , Issue.18 , pp. 7638-7645
    • Ashbaugh, H.S.1    Pethica, B.A.2
  • 29
    • 70349309310 scopus 로고    scopus 로고
    • How surface wettability affects the binding, folding, and dynamics of hydrophobic polymers at interfaces
    • S.N. Jamadagni, R. Godawat, and S. Garde How surface wettability affects the binding, folding, and dynamics of hydrophobic polymers at interfaces Langmuir 25 22 2009 13092 13099
    • (2009) Langmuir , vol.25 , Issue.22 , pp. 13092-13099
    • Jamadagni, S.N.1    Godawat, R.2    Garde, S.3
  • 30
    • 84861797429 scopus 로고    scopus 로고
    • Antimicrobial selectivity based on zwitterionic lipids and underlying balance of interactions
    • C.I.E. von Deuster, and V. Knecht Antimicrobial selectivity based on zwitterionic lipids and underlying balance of interactions Biochim. Biophys. Acta Biomembr. 1818 2012 2192 2201
    • (2012) Biochim. Biophys. Acta Biomembr. , vol.1818 , pp. 2192-2201
    • Von Deuster, C.I.E.1    Knecht, V.2
  • 31
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin
    • A.S. Ladokhin, and S.H. White Folding of amphipathic alpha-helices on membranes: energetics of helix formation by melittin J. Mol. Biol. 285 4 1999 1363 1369
    • (1999) J. Mol. Biol. , vol.285 , Issue.4 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 32
    • 78650191386 scopus 로고    scopus 로고
    • CD spectroscopy of peptides and proteins bound to large unilamellar vesicles
    • A.S. Ladokhin, M. Fernandez-Vidal, and S.H. White CD spectroscopy of peptides and proteins bound to large unilamellar vesicles J. Membr. Biol. 236 3 2010 247 253
    • (2010) J. Membr. Biol. , vol.236 , Issue.3 , pp. 247-253
    • Ladokhin, A.S.1    Fernandez-Vidal, M.2    White, S.H.3
  • 33
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • K. Hristova, C.E. Dempsey, and S.H. White Structure, location, and lipid perturbations of melittin at the membrane interface Biophys. J. 80 2 2001 801 811
    • (2001) Biophys. J. , vol.80 , Issue.2 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 34
    • 0034023711 scopus 로고    scopus 로고
    • Conformation and dynamics of melittin bound to magnetically oriented lipid bilayers by solid-state 31P and 13C NMR spectroscopy
    • A. Naito, T. Nagao, K. Norisada, T. Mizuno, S. Tuzi, and H. Saito Conformation and dynamics of melittin bound to magnetically oriented lipid bilayers by solid-state 31P and 13C NMR spectroscopy Biophys. J. 78 5 2000 2405 2417
    • (2000) Biophys. J. , vol.78 , Issue.5 , pp. 2405-2417
    • Naito, A.1    Nagao, T.2    Norisada, K.3    Mizuno, T.4    Tuzi, S.5    Saito, H.6
  • 35
    • 34247530728 scopus 로고    scopus 로고
    • Peptide insertion, positioning, and stabilization in a membrane: Insight from an all-atom molecular dynamics simulation
    • A. Babakhani, A.A. Gorfe, J. Gullingsrud, J.E. Kim, and J. Andrew McCammon Peptide insertion, positioning, and stabilization in a membrane: insight from an all-atom molecular dynamics simulation Biopolymers 85 2007 490 497
    • (2007) Biopolymers , vol.85 , pp. 490-497
    • Babakhani, A.1    Gorfe, A.A.2    Gullingsrud, J.3    Kim, J.E.4    Andrew McCammon, J.5
  • 36
    • 56349138757 scopus 로고    scopus 로고
    • Monitoring orientation and dynamics of membrane-bound melittin utilizing dansyl fluorescence
    • S. Haldar, H. Raghuraman, and A. Chattopadhyay Monitoring orientation and dynamics of membrane-bound melittin utilizing dansyl fluorescence J. Phys. Chem. B 112 44 2008 14075 14082
    • (2008) J. Phys. Chem. B , vol.112 , Issue.44 , pp. 14075-14082
    • Haldar, S.1    Raghuraman, H.2    Chattopadhyay, A.3
  • 37
    • 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 3 2006 193 202
    • (2006) J. Membr. Biol. , vol.208 , Issue.3 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 38
    • 37749032412 scopus 로고    scopus 로고
    • Temperature dependence of structure, bending rigidity, and bilayer interactions of dioleoylphosphatidylcholine bilayers
    • J. Pan, S. Tristram-Nagle, N. Kucerka, and J.F. Nagle Temperature dependence of structure, bending rigidity, and bilayer interactions of dioleoylphosphatidylcholine bilayers Biophys. J. 94 1 2008 117 124
    • (2008) Biophys. J. , vol.94 , Issue.1 , pp. 117-124
    • Pan, J.1    Tristram-Nagle, S.2    Kucerka, N.3    Nagle, J.F.4
  • 39
    • 32344447540 scopus 로고    scopus 로고
    • A molecular dynamics study of the bee venom melittin in aqueous solution, in methanol, and inserted in a phospholipid bilayer
    • A. Glattli, I. Chandrasekhar, and W.F. Gunsteren A molecular dynamics study of the bee venom melittin in aqueous solution, in methanol, and inserted in a phospholipid bilayer Eur. Biophys. J. 35 3 2006 255 267
    • (2006) Eur. Biophys. J. , vol.35 , Issue.3 , pp. 255-267
    • Glattli, A.1    Chandrasekhar, I.2    Gunsteren, W.F.3
  • 40
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane
    • S. Berneche, M. Nina, and B. Roux Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane Biophys. J. 75 4 1998 1603 1618
    • (1998) Biophys. J. , vol.75 , Issue.4 , pp. 1603-1618
    • Berneche, S.1    Nina, M.2    Roux, B.3
  • 41
    • 84866519587 scopus 로고    scopus 로고
    • Molecular dynamics studies of transportan 10 (Tp10) interacting with a POPC lipid bilayer
    • C.M. Dunkin, A. Pokorny, P.F. Almeida, and H.S. Lee Molecular dynamics studies of transportan 10 (Tp10) interacting with a POPC lipid bilayer J. Phys. Chem. B 2010
    • (2010) J. Phys. Chem. B
    • Dunkin, C.M.1    Pokorny, A.2    Almeida, P.F.3    Lee, H.S.4
  • 42
    • 16344384943 scopus 로고    scopus 로고
    • Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR
    • S. Toraya, K. Nishimura, and A. Naito Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR Biophys. J. 87 5 2004 3323 3335
    • (2004) Biophys. J. , vol.87 , Issue.5 , pp. 3323-3335
    • Toraya, S.1    Nishimura, K.2    Naito, A.3
  • 43
    • 34547653932 scopus 로고    scopus 로고
    • Real-time structural investigation of a lipid bilayer during its interaction with melittin using sum frequency generation vibrational spectroscopy
    • X. Chen, J. Wang, C.B. Kristalyn, and Z. Chen Real-time structural investigation of a lipid bilayer during its interaction with melittin using sum frequency generation vibrational spectroscopy Biophys. J. 93 3 2007 866 875
    • (2007) Biophys. J. , vol.93 , Issue.3 , pp. 866-875
    • Chen, X.1    Wang, J.2    Kristalyn, C.B.3    Chen, Z.4
  • 44
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • F.Y. Chen, M.T. Lee, and H.W. Huang Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 84 6 2003 3751 3758
    • (2003) Biophys. J. , vol.84 , Issue.6 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 45
    • 33846818748 scopus 로고    scopus 로고
    • Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies
    • X. Chen, J. Wang, A.P. Boughton, C.B. Kristalyn, and Z. Chen Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies J. Am. Chem. Soc. 129 5 2007 1420 1427
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.5 , pp. 1420-1427
    • Chen, X.1    Wang, J.2    Boughton, A.P.3    Kristalyn, C.B.4    Chen, Z.5
  • 46
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • S. Frey, and L.K. Tamm Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study Biophys. J. 60 4 1991 922 930
    • (1991) Biophys. J. , vol.60 , Issue.4 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 47
    • 0028415140 scopus 로고
    • A combined X-ray and neutron-diffraction study of selectively deuterated melittin in phospholipid-bilayers - Effect of pH
    • J.P. Bradshaw, C.E. Dempsey, and A. Watts A combined X-ray and neutron-diffraction study of selectively deuterated melittin in phospholipid-bilayers - effect of pH Mol. Membr. Biol. 11 2 1994 79 86
    • (1994) Mol. Membr. Biol. , vol.11 , Issue.2 , pp. 79-86
    • Bradshaw, J.P.1    Dempsey, C.E.2    Watts, A.3
  • 49
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • T. Lazaridis Effective energy function for proteins in lipid membranes Proteins Struct. Funct. Bioinformatics 52 2 2003 176 192
    • (2003) Proteins Struct. Funct. Bioinformatics , vol.52 , Issue.2 , pp. 176-192
    • Lazaridis, T.1
  • 50
    • 0020079526 scopus 로고
    • The structure of melittin in the form i crystals and its implication for melittin's lytic and surface activities
    • T.C. Terwilliger, L. Weissman, and D. Eisenberg The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities Biophys. J. 37 1 1982 353 361
    • (1982) Biophys. J. , vol.37 , Issue.1 , pp. 353-361
    • Terwilliger, T.C.1    Weissman, L.2    Eisenberg, D.3
  • 51
    • 0021097003 scopus 로고
    • The orientation of melittin in lipid membranes. A polarized infrared spectroscopy study
    • H. Vogel, F. Jahnig, V. Hoffmann, and J. Stumpel The orientation of melittin in lipid membranes. A polarized infrared spectroscopy study Biochim. Biophys. Acta Biomembr. 733 2 1983 201 209
    • (1983) Biochim. Biophys. Acta Biomembr. , vol.733 , Issue.2 , pp. 201-209
    • Vogel, H.1    Jahnig, F.2    Hoffmann, V.3    Stumpel, J.4
  • 52
    • 84864227931 scopus 로고    scopus 로고
    • Multiscale simulations of the antimicrobial peptide maculatin 1.1: Water permeation through disordered aggregates
    • D. Parton, E. Akhmatskaya, and M.S.P. Sansom Multiscale simulations of the antimicrobial peptide maculatin 1.1: water permeation through disordered aggregates J. Phys. Chem. B 2012
    • (2012) J. Phys. Chem. B
    • Parton, D.1    Akhmatskaya, E.2    Sansom, M.S.P.3


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