메뉴 건너뛰기




Volumn 117, Issue 17, 2013, Pages 5031-5042

Melittin creates transient pores in a lipid bilayer: Results from computer simulations

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; CONFORMATIONS; LIPID BILAYERS; MOLECULAR DYNAMICS; PHOSPHOLIPIDS;

EID: 84877033658     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp312328n     Document Type: Article
Times cited : (59)

References (44)
  • 1
    • 77958085274 scopus 로고    scopus 로고
    • Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model
    • Wimley, W. C. Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model ACS Chem. Biol. 2010, 5, 905-917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 2
    • 79955669580 scopus 로고    scopus 로고
    • Antimicrobial Peptides: Successes, Challenges and Unanswered Questions
    • Wimley, W. C.; Hristova, K. Antimicrobial Peptides: Successes, Challenges and Unanswered Questions J. Membr. Biol. 2011, 239, 27-34
    • (2011) J. Membr. Biol. , vol.239 , pp. 27-34
    • Wimley, W.C.1    Hristova, K.2
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial Peptides: Pore Formers or Metabolic Inhibitors in Bacteria?
    • Brogden, K. A. Antimicrobial Peptides: Pore Formers or Metabolic Inhibitors in Bacteria? Nat. Rev. Microbiol. 2005, 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 33748950268 scopus 로고    scopus 로고
    • Molecular Mechanism of Antimicrobial Peptides: The Origin of Cooperativity
    • Huang, H. W. Molecular Mechanism of Antimicrobial Peptides: The Origin of Cooperativity Biochim. Biophys. Acta, Biomembr. 2006, 1758, 1292-1302
    • (2006) Biochim. Biophys. Acta, Biomembr. , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 5
    • 0029873933 scopus 로고    scopus 로고
    • Structure and Orientation of the Mammalian Antibacterial Peptide Cecropin P1 within Phospholipid Membranes
    • Gazit, E.; Miller, I. R.; Biggin, P. C.; Sansom, M. S. P.; Shai, Y. Structure and Orientation of the Mammalian Antibacterial Peptide Cecropin P1 within Phospholipid Membranes J. Mol. Biol. 1996, 258, 860-870
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.P.4    Shai, Y.5
  • 6
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics
    • Almeida, P. F.; Pokorny, A. Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics Biochemistry 2009, 48, 8083-8093
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 7
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of Dye Efflux and Lipid Flip-Flop Induced by Delta-Lysin in Phosphatidylcholine Vesicles and the Mechanism of Graded Release by Amphipathic, Alpha-Helical Peptides
    • Pokorny, A.; Almeida, P. F. F. Kinetics of Dye Efflux and Lipid Flip-Flop Induced by Delta-Lysin in Phosphatidylcholine Vesicles and the Mechanism of Graded Release by Amphipathic, Alpha-Helical Peptides Biochemistry 2004, 43, 8846-8857
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 8
    • 77956761543 scopus 로고    scopus 로고
    • Kinetic Pathway of Antimicrobial Peptide Magainin 2-Induced Pore Formation in Lipid Membranes
    • Tamba, Y.; Ariyama, H.; Levadny, V.; Yamazaki, M. Kinetic Pathway of Antimicrobial Peptide Magainin 2-Induced Pore Formation in Lipid Membranes J. Phys. Chem. B 2010, 114, 12018-12026
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12018-12026
    • Tamba, Y.1    Ariyama, H.2    Levadny, V.3    Yamazaki, M.4
  • 9
    • 70350238527 scopus 로고    scopus 로고
    • Membrane Poration by Antimicrobial Peptides Combining Atomistic and Coarse-Grained Descriptions
    • Rzepiela, A. J.; Sengupta, D.; Goga, N.; Marrink, S. J. Membrane Poration by Antimicrobial Peptides Combining Atomistic and Coarse-Grained Descriptions Faraday Discuss. 2010, 144, 431-443
    • (2010) Faraday Discuss. , vol.144 , pp. 431-443
    • Rzepiela, A.J.1    Sengupta, D.2    Goga, N.3    Marrink, S.J.4
  • 10
    • 74949104869 scopus 로고    scopus 로고
    • Cause and Effect of Melittin-Induced Pore Formation: A Computational Approach
    • Manna, M.; Mukhopadhyay, C. Cause and Effect of Melittin-Induced Pore Formation: A Computational Approach Langmuir 2009, 25, 12235-12242
    • (2009) Langmuir , vol.25 , pp. 12235-12242
    • Manna, M.1    Mukhopadhyay, C.2
  • 11
    • 77953724763 scopus 로고    scopus 로고
    • Antimicrobial Peptides in Toroidal and Cylindrical Pores
    • Mihajlovic, M.; Lazaridis, T. Antimicrobial Peptides in Toroidal and Cylindrical Pores Biochim. Biophys. Acta, Biomembr. 2010, 1798, 1485-1493
    • (2010) Biochim. Biophys. Acta, Biomembr. , vol.1798 , pp. 1485-1493
    • Mihajlovic, M.1    Lazaridis, T.2
  • 12
    • 79959997001 scopus 로고    scopus 로고
    • Influence of the Arrangement and Secondary Structure of Melittin Peptides on the Formation and Stability of Toroidal Pores
    • Irudayam, S. J.; Berkowitz, M. L. Influence of the Arrangement and Secondary Structure of Melittin Peptides on the Formation and Stability of Toroidal Pores Biochim. Biophys. Acta, Biomembr 2011, 1808, 2258-2266
    • (2011) Biochim. Biophys. Acta, Biomembr , vol.1808 , pp. 2258-2266
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 13
    • 84858027055 scopus 로고    scopus 로고
    • Difference between Magainin-2 and Melittin Assemblies in Phosphatidylcholine Bilayers: Results from Coarse-Grained Simulations
    • Santo, K. P.; Berkowitz, M. L. Difference between Magainin-2 and Melittin Assemblies in Phosphatidylcholine Bilayers: Results from Coarse-Grained Simulations J. Phys. Chem. B 2012, 116, 3021-3030
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3021-3030
    • Santo, K.P.1    Berkowitz, M.L.2
  • 15
    • 80052804796 scopus 로고    scopus 로고
    • Water Defect and Pore Formation in Atomistic and Coarse-Grained Lipid Membranes: Pushing the Limits of Coarse Graining
    • Bennett, W. F. D.; Tieleman, D. P. Water Defect and Pore Formation in Atomistic and Coarse-Grained Lipid Membranes: Pushing the Limits of Coarse Graining J. Chem. Theory Comput. 2011, 7, 2981-2988
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2981-2988
    • Bennett, W.F.D.1    Tieleman, D.P.2
  • 16
    • 84855853473 scopus 로고    scopus 로고
    • Investigation of Model Membrane Disruption Mechanism by Melittin Using Pulse Electron Paramagnetic Resonance Spectroscopy and Cryogenic Transmission Electron Microscopy
    • Gordon-Grossman, M.; Zimmermann, H.; Wolf, S. G.; Shai, Y.; Goldfarb, D. Investigation of Model Membrane Disruption Mechanism by Melittin Using Pulse Electron Paramagnetic Resonance Spectroscopy and Cryogenic Transmission Electron Microscopy J. Phys. Chem. B 2012, 116, 179-188
    • (2012) J. Phys. Chem. B , vol.116 , pp. 179-188
    • Gordon-Grossman, M.1    Zimmermann, H.2    Wolf, S.G.3    Shai, Y.4    Goldfarb, D.5
  • 17
    • 79959572024 scopus 로고    scopus 로고
    • Spontaneous Buckling of Lipid Bilayer and Vesicle Budding Induced by Antimicrobial Peptide Magainin 2: A Coarse-Grained Simulation Study
    • Woo, H. J.; Wallqvist, A. Spontaneous Buckling of Lipid Bilayer and Vesicle Budding Induced by Antimicrobial Peptide Magainin 2: A Coarse-Grained Simulation Study J. Phys. Chem. B 2011, 115, 8122-8129
    • (2011) J. Phys. Chem. B , vol.115 , pp. 8122-8129
    • Woo, H.J.1    Wallqvist, A.2
  • 18
    • 0020479083 scopus 로고
    • The Structure of Melittin 0.1. Structure Determination and Partial Refinement
    • Terwilliger, T. C.; Eisenberg, D. The Structure of Melittin 0.1. Structure Determination and Partial Refinement J. Biol. Chem. 1982, 257, 6010-6015
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 19
    • 0020479123 scopus 로고
    • The Structure of Melittin 0.2. Interpretation of the Structure
    • Terwilliger, T. C.; Eisenberg, D. The Structure of Melittin 0.2. Interpretation of the Structure J. Biol. Chem. 1982, 257, 6016-6022
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 20
    • 1642485164 scopus 로고    scopus 로고
    • Coarse Grained Model for Semiquantitative Lipid Simulations
    • Marrink, S. J.; de Vries, A. H.; Mark, A. E. Coarse Grained Model for Semiquantitative Lipid Simulations J. Phys. Chem. B 2004, 108, 750-760
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 23
    • 84865318587 scopus 로고    scopus 로고
    • Binding and Reorientation of Melittin in a Popc Bilayer: Computer Simulations
    • Irudayam, S. J.; Berkowitz, M. L. Binding and Reorientation of Melittin in a Popc Bilayer: Computer Simulations Biochim. Biophys. Acta, Biomembr. 2012, 1818, 2975-2981
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 2975-2981
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 24
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of Antibacterial and Toxic Activity of Melittin-A Leucine Zipper Motif Plays a Crucial Role in Determining Its Hemolytic Activity but Not Antibacterial Activity
    • Asthana, N.; Yadav, S. P.; Ghosh, J. K. Dissection of Antibacterial and Toxic Activity of Melittin-a Leucine Zipper Motif Plays a Crucial Role in Determining Its Hemolytic Activity but Not Antibacterial Activity J. Biol. Chem. 2004, 279, 55042-55050
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 25
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A Membrane-Active Peptide with Diverse Functions
    • Raghuraman, H.; Chattopadhyay, A. Melittin: A Membrane-Active Peptide with Diverse Functions Biosci. Rep. 2007, 27, 189-223
    • (2007) Biosci. Rep. , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 27
    • 33846823909 scopus 로고
    • Particle Mesh Ewald-an N.Log(N) Method for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald-an N.Log(N) Method for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 31
    • 65249151900 scopus 로고    scopus 로고
    • Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins
    • Kukol, A. Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins J. Chem. Theory Comput. 2009, 5, 615-626
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 615-626
    • Kukol, A.1
  • 32
    • 4444282928 scopus 로고    scopus 로고
    • A Biomolecular Force Field Based on the Free Enthalpy of Hydration and Solvation: The Gromos Force-Field Parameter Sets 53a5 and 53a6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; Van Gunsteren, W. F. A Biomolecular Force Field Based on the Free Enthalpy of Hydration and Solvation: The Gromos Force-Field Parameter Sets 53a5 and 53a6 J. Comput. Chem. 2004, 25, 1656-1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 35
    • 0030790179 scopus 로고    scopus 로고
    • Pore Formation and Translocation of Melittin
    • Matsuzaki, K.; Yoneyama, S.; Miyajima, K. Pore Formation and Translocation of Melittin Biophys. J. 1997, 73, 831-838
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 36
    • 70349298715 scopus 로고    scopus 로고
    • A Combined Pulse Epr and Monte Carlo Simulation Study Provides Molecular Insight on Peptide-Membrane Interactions
    • Gordon-Grossman, M.; Gofman, Y.; Zimmermann, H.; Frydman, V.; Shai, Y.; Ben-Tal, N.; Goldfarb, D. A Combined Pulse Epr and Monte Carlo Simulation Study Provides Molecular Insight on Peptide-Membrane Interactions J. Phys. Chem. B 2009, 113, 12687-12695
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12687-12695
    • Gordon-Grossman, M.1    Gofman, Y.2    Zimmermann, H.3    Frydman, V.4    Shai, Y.5    Ben-Tal, N.6    Goldfarb, D.7
  • 38
    • 56049100497 scopus 로고    scopus 로고
    • Coarse-Grained Simulations of the Membrane-Active Antimicrobial Peptide Maculatin 1.1
    • Bond, P. J.; Parton, D. L.; Clark, J. F.; Sansom, M. S. P. Coarse-Grained Simulations of the Membrane-Active Antimicrobial Peptide Maculatin 1.1 Biophys. J. 2008, 95, 3802-3815
    • (2008) Biophys. J. , vol.95 , pp. 3802-3815
    • Bond, P.J.1    Parton, D.L.2    Clark, J.F.3    Sansom, M.S.P.4
  • 39
    • 84864227931 scopus 로고    scopus 로고
    • Multiscale Simulations of the Antimicrobial Peptide Maculatin 1.1: Water Permeation through Disordered Aggregates
    • Parton, D. L.; Akhmatskaya, E. V.; Sansom, M. S. P. Multiscale Simulations of the Antimicrobial Peptide Maculatin 1.1: Water Permeation through Disordered Aggregates J. Phys. Chem. B 2012, 116, 8485-8493
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8485-8493
    • Parton, D.L.1    Akhmatskaya, E.V.2    Sansom, M.S.P.3
  • 40
    • 0028178521 scopus 로고
    • Pore-Forming Peptides Induce Rapid Phospholipid Flip-Flop in Membranes
    • Fattal, E.; Nir, S.; Parente, R. A.; Szoka, F. C. Pore-Forming Peptides Induce Rapid Phospholipid Flip-Flop in Membranes Biochemistry 1994, 33, 6721-6731
    • (1994) Biochemistry , vol.33 , pp. 6721-6731
    • Fattal, E.1    Nir, S.2    Parente, R.A.3    Szoka, F.C.4
  • 41
    • 0035144532 scopus 로고    scopus 로고
    • Structure, Location, and Lipid Perturbations of Melittin at the Membrane Interface
    • Hristova, K.; Dempsey, C. E.; White, S. H. Structure, Location, and Lipid Perturbations of Melittin at the Membrane Interface Biophys. J. 2001, 80, 801-811
    • (2001) Biophys. J. , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 42
    • 0037961563 scopus 로고    scopus 로고
    • Msi-78, an Analogue of the Magainin Antimicrobial Peptides, Disrupts Lipid Bilayer Structure Via Positive Curvature Strain
    • Hallock, K. J.; Lee, D. K.; Ramamoorthy, A. Msi-78, an Analogue of the Magainin Antimicrobial Peptides, Disrupts Lipid Bilayer Structure Via Positive Curvature Strain Biophys. J. 2003, 84, 3052-3060
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 44
    • 79953862815 scopus 로고    scopus 로고
    • Mechanism of Membrane Curvature Sensing by Amphipathic Helix Containing Proteins
    • Cui, H. S.; Lyman, E.; Voth, G. A. Mechanism of Membrane Curvature Sensing by Amphipathic Helix Containing Proteins Biophys. J. 2011, 100, 1271-1279
    • (2011) Biophys. J. , vol.100 , pp. 1271-1279
    • Cui, H.S.1    Lyman, E.2    Voth, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.