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Volumn 1838, Issue 9, 2014, Pages 2243-2249

Absorption and folding of melittin onto lipid bilayer membranes via unbiased atomic detail microsecond molecular dynamics simulation

Author keywords

Bilayer; Circular dichroism; Melittin; Membrane; Molecular dynamics; Protein folding

Indexed keywords

AMPHOPHILE; MELITTIN;

EID: 84903696835     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.04.012     Document Type: Article
Times cited : (48)

References (39)
  • 1
    • 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 2010 247 253
    • (2010) J. Membr. Biol. , vol.236 , pp. 247-253
    • Ladokhin, A.S.1    Fernandez-Vidal, M.2    White, S.H.3
  • 2
    • 0019871670 scopus 로고
    • Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes
    • H. Vogel Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes FEBS Lett. 134 1981 37 42
    • (1981) FEBS Lett. , vol.134 , pp. 37-42
    • Vogel, H.1
  • 3
    • 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 2001 801 811 (Pubitemid 32128331)
    • (2001) Biophysical Journal , vol.80 , Issue.2 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 4
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • L. Yang, T.A. Harroun, T.M. Weiss, L. Ding, and H.W. Huang Barrel-stave model or toroidal model? A case study on melittin pores Biophys. J. 81 2001 1475 1485 (Pubitemid 32783588)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 5
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • DOI 10.1007/s10540-006-9030-z
    • H. Raghuraman, and A. Chattopadhyay Melittin: a membrane-active peptide with diverse functions Biosci. Rep. 27 2007 189 223 (Pubitemid 47222897)
    • (2007) Bioscience Reports , vol.27 , Issue.4-5 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 6
    • 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 2009 8083 8093
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 8
    • 0031972614 scopus 로고    scopus 로고
    • Hydrogen bonding in helical polypeptides from molecular dynamics simulations and amide hydrogen exchange analysis: Alamethicin and melittin in methanol
    • R.B. Sessions, C.E. Gibbs, and C.E. Dempsey Hydrogen bonding in helical polypeptides from molecular dynamics simulations and amide hydrogen exchange analysis: alamethicin and melittin in methanol Biophys. J. 74 1998 138 152 (Pubitemid 28041745)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 138-152
    • Sessions, R.B.1    Gibbs, N.2    Dempsey, C.E.3
  • 9
    • 25844479815 scopus 로고    scopus 로고
    • Effect of hexafluoroisopropanol alcohol on the structure of melittin: A molecular dynamics simulation study
    • DOI 10.1110/ps.051426605
    • D. Roccatano, M. Fioroni, M. Zacharias, and G. Colombo Effect of hexafluoroisopropanol alcohol on the structure of melittin: a molecular dynamics simulation study Protein Sci. 14 2005 2582 2589 (Pubitemid 41395585)
    • (2005) Protein Science , vol.14 , Issue.10 , pp. 2582-2589
    • Roccatano, D.1    Fioroni, M.2    Zacharias, M.3    Colombo, G.4
  • 10
    • 0037126023 scopus 로고    scopus 로고
    • Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study
    • D. Roccatano, G. Colombo, M. Fioroni, and A.E. Mark Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study Proc. Natl. Acad. Sci. U. S. A. 99 2002 12179 12184
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12179-12184
    • Roccatano, D.1    Colombo, G.2    Fioroni, M.3    Mark, A.E.4
  • 11
    • 0034091671 scopus 로고    scopus 로고
    • Protein-induced membrane disorder: A molecular dynamics study of melittin in a dipalmitoylphosphatidylcholine bilayer
    • M. Bachar, and O.M. Becker Protein-induced membrane disorder: a molecular dynamics study of melittin in a dipalmitoylphosphatidylcholine bilayer Biophys. J. 78 2000 1359 1375 (Pubitemid 30141561)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1359-1375
    • Bachar, M.1    Becker, O.M.2
  • 12
    • 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
    • DOI 10.1007/s00249-005-0033-7
    • A. Glattli, I. Chandrasekhar, and W.F. van 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 2006 255 267 (Pubitemid 43221186)
    • (2006) European Biophysics Journal , vol.35 , Issue.3 , pp. 255-267
    • Glattli, A.1    Chandrasekhar, I.2    Van Gunsteren, W.F.3
  • 13
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane
    • S. Bernèche, M. Nina, and B. Roux Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane Biophys. J. 75 1998 1603 1618 (Pubitemid 28455158)
    • (1998) Biophysical Journal , vol.75 , Issue.4 , pp. 1603-1618
    • Berneche, S.1    Nina, M.2    Roux, B.3
  • 14
    • 0034068919 scopus 로고    scopus 로고
    • Stability of a melittin pore in a lipid bilayer: A molecular dynamics study
    • J.-H. Lin, and A. Baumgartner Stability of a melittin pore in a lipid bilayer: a molecular dynamics study Biophys. J. 78 2000 1714 1724 (Pubitemid 30183570)
    • (2000) Biophysical Journal , vol.78 , Issue.4 , pp. 1714-1724
    • Lin, J.-H.1    Baumgaertner, A.2
  • 15
    • 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 1808 2011 2258 2266
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2258-2266
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 16
    • 24344448662 scopus 로고    scopus 로고
    • Observation of a dewetting transition in the collapse of the melittin tetramer
    • DOI 10.1038/nature03926, PII N03926
    • P. Liu, X. Huang, R. Zhou, and B.J. Berne Observation of a dewetting transition in the collapse of the melittin tetramer Nature 437 2005 159 162 (Pubitemid 41613444)
    • (2005) Nature , vol.437 , Issue.7055 , pp. 159-162
    • Liu, P.1    Huang, X.2    Zhou, R.3    Berne, B.J.4
  • 17
    • 84865318587 scopus 로고    scopus 로고
    • Binding and reorientation of melittin in a POPC bilayer: Computer simulations
    • S.J. Irudayam, and M.L. Berkowitz Binding and reorientation of melittin in a POPC bilayer: computer simulations Biochim. Biophys. Acta 1808 2011 2975 2981
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2975-2981
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 19
    • 80053306385 scopus 로고    scopus 로고
    • In silico partitioning and transmembrane insertion of hydrophobic peptides under equilibrium conditions
    • J.P. Ulmschneider, J.C. Smith, S.H. White, and M.B. Ulmschneider In silico partitioning and transmembrane insertion of hydrophobic peptides under equilibrium conditions J. Am. Chem. Soc. 133 2011 15487 15495
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15487-15495
    • Ulmschneider, J.P.1    Smith, J.C.2    White, S.H.3    Ulmschneider, M.B.4
  • 22
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin
    • DOI 10.1006/jmbi.1998.2346
    • A.S. Ladokhin, and S.H. White Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin J. Mol. Biol. 285 1999 1363 1369 (Pubitemid 29060439)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 23
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • H. Vogel, and F. Jähnig The structure of melittin in membranes Biophys. J. 50 1986 573 582
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jähnig, F.2
  • 24
    • 0026746013 scopus 로고
    • Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ
    • DOI 10.1021/bi00163a003
    • C.E. Dempsey, and G.S. Butler Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ Biochemistry 31 1992 11973 11977 (Pubitemid 23011338)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 11973-11977
    • Dempsey, C.E.1    Butler, G.S.2
  • 25
    • 77949399840 scopus 로고    scopus 로고
    • Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides
    • M.B. Ulmschneider, J.P. Doux, J.A. Killian, J.C. Smith, and J.P. Ulmschneider Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides J. Am. Chem. Soc. 132 2010 3452 3460
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3452-3460
    • Ulmschneider, M.B.1    Doux, J.P.2    Killian, J.A.3    Smith, J.C.4    Ulmschneider, J.P.5
  • 26
    • 77953598334 scopus 로고    scopus 로고
    • Peptide partitioning properties from direct insertion studies
    • M.B. Ulmschneider, J.C. Smith, and J.P. Ulmschneider Peptide partitioning properties from direct insertion studies Biophys. J. 98 2010 L60 L62
    • (2010) Biophys. J. , vol.98
    • Ulmschneider, M.B.1    Smith, J.C.2    Ulmschneider, J.P.3
  • 28
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining energetics of peptide-bilayer interactions
    • DOI 10.1016/S0076-6879(98)95035-2
    • S.H. White, W.C. Wimley, A.S. Ladokhin, and K. Hristova Protein folding in membranes: determining energetics of peptide-bilayer interactions Methods Enzymol. 295 1998 62 87 (Pubitemid 29349909)
    • (1998) Methods in Enzymology , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 35
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • G. Bussi, D. Donadio, and M. Parrinello Canonical sampling through velocity rescaling J. Chem. Phys. 126 2007 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 38
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • DOI 10.1021/bi000804r
    • M.R.R. de Planque, E. Goormaghtigh, D.V. Greathouse, R.E. Koeppe, J.A.W. Kruijtzer, R.M.J. Liskamp, B. de Kruijff, and J.A. Killian Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation Biochemistry 40 2001 5000 5010 (Pubitemid 32332546)
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 5000-5010
    • De Planque, M.R.R.1    Goormaghtigh, E.2    Greathouse, D.V.3    Koeppe II, R.E.4    Kruijtzer, J.A.W.5    Liskamp, R.M.J.6    De Kruijff, B.7    Killian, J.A.8
  • 39
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5


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