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Volumn 105, Issue 10, 2013, Pages 2333-2342

A 2h Solid-state nmr study of lipid clustering by cationic antimicrobial and Cell-penetrating peptides in model bacterial membranes

Author keywords

[No Author keywords available]

Indexed keywords

1-PALMITOYL-2-OLEOYLGLYCERO-3-PHOSPHOGLYCEROL; 1-PALMITOYL-2-OLEOYLPHOSPHATIDYLETHANOLAMINE; ANTIMICROBIAL CATIONIC PEPTIDE; CARRIER PROTEIN; CELL PENETRATING PEPTIDE; PENETRATIN; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; PROTEGRIN-1; TRANSACTIVATOR PROTEIN;

EID: 84887912736     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.08.020     Document Type: Article
Times cited : (33)

References (39)
  • 1
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • D.A. Brown, and E. London Structure and function of sphingolipid- and cholesterol-rich membrane rafts J. Biol. Chem. 275 2000 17221 17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 3
    • 65949090768 scopus 로고    scopus 로고
    • Domains in bacterial membranes and the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Domains in bacterial membranes and the action of antimicrobial agents Mol. Biosyst. 5 2009 580 587
    • (2009) Mol. Biosyst. , vol.5 , pp. 580-587
    • Epand, R.M.1    Epand, R.F.2
  • 4
    • 77952395366 scopus 로고    scopus 로고
    • Probing the "charge cluster mechanism" in amphipathic helical cationic antimicrobial peptides
    • R.F. Epand, and W.L. Maloy R.M. Epand Probing the "charge cluster mechanism" in amphipathic helical cationic antimicrobial peptides Biochemistry 49 2010 4076 4084
    • (2010) Biochemistry , vol.49 , pp. 4076-4084
    • Epand, R.F.1    Maloy, W.L.2    Epand, R.M.3
  • 5
    • 70349119495 scopus 로고    scopus 로고
    • Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37
    • R.F. Epand, and G. Wang R.M. Epand Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37 Antimicrob. Agents Chemother. 53 2009 3705 3714
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3705-3714
    • Epand, R.F.1    Wang, G.2    Epand, R.M.3
  • 6
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Lipid domains in bacterial membranes and the action of antimicrobial agents Biochim. Biophys. Acta 1788 2009 289 294
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 7
    • 44949104715 scopus 로고    scopus 로고
    • HIV TAT forms pores in membranes by inducing saddle-splay curvature: Potential role of bidentate hydrogen bonding
    • A. Mishra, and V.D. Gordon G.C.L. Wong HIV TAT forms pores in membranes by inducing saddle-splay curvature: potential role of bidentate hydrogen bonding Angew. Chem. Int. Ed. Engl. 47 2008 2986 2989
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 2986-2989
    • Mishra, A.1    Gordon, V.D.2    Wong, G.C.L.3
  • 8
    • 79955366494 scopus 로고    scopus 로고
    • Criterion for amino acid composition of defensins and antimicrobial peptides based on geometry of membrane destabilization
    • N.W. Schmidt, and A. Mishra G.C. Wong Criterion for amino acid composition of defensins and antimicrobial peptides based on geometry of membrane destabilization J. Am. Chem. Soc. 133 2011 6720 6727
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6720-6727
    • Schmidt, N.W.1    Mishra, A.2    Wong, G.C.3
  • 9
    • 79953186604 scopus 로고    scopus 로고
    • Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR
    • M. Hong, and Y. Su Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR Protein Sci. 20 2011 641 655
    • (2011) Protein Sci. , vol.20 , pp. 641-655
    • Hong, M.1    Su, Y.2
  • 10
    • 62949097134 scopus 로고    scopus 로고
    • Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy
    • M. Tang, and M. Hong Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy Mol. Biosyst. 5 2009 317 322
    • (2009) Mol. Biosyst. , vol.5 , pp. 317-322
    • Tang, M.1    Hong, M.2
  • 11
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat. Rev. Immunol. 3 2003 710 720
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 12
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 13
    • 31544438701 scopus 로고    scopus 로고
    • Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides
    • R. Fischer, and M. Fotin-Mleczek R. Brock Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides ChemBioChem 6 2005 2126 2142
    • (2005) ChemBioChem , vol.6 , pp. 2126-2142
    • Fischer, R.1    Fotin-Mleczek, M.2    Brock, R.3
  • 14
    • 48749122491 scopus 로고    scopus 로고
    • Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR
    • Y. Su, and R. Mani M. Hong Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR J. Mol. Biol. 381 2008 1133 1144
    • (2008) J. Mol. Biol. , vol.381 , pp. 1133-1144
    • Su, Y.1    Mani, R.2    Hong, M.3
  • 15
    • 77954831684 scopus 로고    scopus 로고
    • Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR
    • Y. Su, and A.J. Waring M. Hong Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR Biochemistry 49 2010 6009 6020
    • (2010) Biochemistry , vol.49 , pp. 6009-6020
    • Su, Y.1    Waring, A.J.2    Hong, M.3
  • 16
    • 77949795332 scopus 로고    scopus 로고
    • Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy
    • S. Li, and Y. Su M. Hong Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy J. Phys. Chem. B 114 2010 4063 4069
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4063-4069
    • Li, S.1    Su, Y.2    Hong, M.3
  • 17
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • M. Tang, A.J. Waring, and M. Hong Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR J. Am. Chem. Soc. 129 2007 11438 11446
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 18
    • 58149311146 scopus 로고    scopus 로고
    • Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels
    • H. Jang, and B. Ma R. Nussinov Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels Biophys. J. 95 2008 4631 4642
    • (2008) Biophys. J. , vol.95 , pp. 4631-4642
    • Jang, H.1    Ma, B.2    Nussinov, R.3
  • 19
    • 41549125949 scopus 로고    scopus 로고
    • On the nature of antimicrobial activity: A model for protegrin-1 pores
    • A.A. Langham, A.S. Ahmad, and Y.N. Kaznessis On the nature of antimicrobial activity: a model for protegrin-1 pores J. Am. Chem. Soc. 130 2008 4338 4346
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4338-4346
    • Langham, A.A.1    Ahmad, A.S.2    Kaznessis, Y.N.3
  • 20
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • R. Mani, and S.D. Cady M. Hong Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR Proc. Natl. Acad. Sci. USA 103 2006 16242 16247
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Hong, M.3
  • 21
    • 33745855891 scopus 로고    scopus 로고
    • Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR
    • R. Mani, and M. Tang M. Hong Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR Biochemistry 45 2006 8341 8349
    • (2006) Biochemistry , vol.45 , pp. 8341-8349
    • Mani, R.1    Tang, M.2    Hong, M.3
  • 22
    • 45549085024 scopus 로고    scopus 로고
    • Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy
    • M. Tang, and A.J. Waring M. Hong Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy Angew. Chem. Int. Ed. Engl. 47 2008 3202 3205
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 3202-3205
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 23
    • 0033858613 scopus 로고    scopus 로고
    • Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues
    • J. Chen, and T.J. Falla J.C. Fiddes Development of protegrins for the treatment and prevention of oral mucositis: structure-activity relationships of synthetic protegrin analogues Biopolymers 55 2000 88 98
    • (2000) Biopolymers , vol.55 , pp. 88-98
    • Chen, J.1    Falla, T.J.2    Fiddes, J.C.3
  • 24
    • 0028785466 scopus 로고
    • Study of phospholipid structure by 1H, 13C, and 31P dipolar couplings from two-dimensional NMR
    • M. Hong, K. Schmidt-Rohr, and D. Nanz Study of phospholipid structure by 1H, 13C, and 31P dipolar couplings from two-dimensional NMR Biophys. J. 69 1995 1939 1950
    • (1995) Biophys. J. , vol.69 , pp. 1939-1950
    • Hong, M.1    Schmidt-Rohr, K.2    Nanz, D.3
  • 25
    • 0029274597 scopus 로고
    • Measurement of signs and magnitudes of C-H dipolar couplings in lecithin
    • M. Hong, K. Schmidt-Rohr, and A. Pines Measurement of signs and magnitudes of C-H dipolar couplings in lecithin J. Am. Chem. Soc. 117 1995 3310 3311
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3310-3311
    • Hong, M.1    Schmidt-Rohr, K.2    Pines, A.3
  • 26
    • 0346213760 scopus 로고
    • Direct determination of the oriented sample NMR-spectrum from the powder spectrum for systems with local axial symmetry
    • M. Bloom, J.H. Davis, and A.L. Mackay Direct determination of the oriented sample NMR-spectrum from the powder spectrum for systems with local axial symmetry Chem. Phys. Lett. 80 1981 198 202
    • (1981) Chem. Phys. Lett. , vol.80 , pp. 198-202
    • Bloom, M.1    Davis, J.H.2    MacKay, A.L.3
  • 27
    • 0031283262 scopus 로고    scopus 로고
    • Rapid deconvolution of NMR powder spectra by weighted fast Fourier transformation
    • M.A. McCabe, and S.R. Wassall Rapid deconvolution of NMR powder spectra by weighted fast Fourier transformation Solid State Nucl. Magn. Reson. 10 1997 53 61
    • (1997) Solid State Nucl. Magn. Reson. , vol.10 , pp. 53-61
    • McCabe, M.A.1    Wassall, S.R.2
  • 28
    • 25444445004 scopus 로고    scopus 로고
    • Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system
    • B. Pozo Navas, and K. Lohner G. Pabst Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system Biochim. Biophys. Acta 1716 2005 40 48
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 40-48
    • Pozo Navas, B.1    Lohner, K.2    Pabst, G.3
  • 29
    • 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
    • F. Aussenac, and M. Laguerre E.J. Dufourc Detailed structure and dynamics of bicelle phospholipids using selectively deuterated and perdeuterated labels. H-2 NMR and molecular mechanics study Langmuir 19 2003 10468 10479
    • (2003) Langmuir , vol.19 , pp. 10468-10479
    • Aussenac, F.1    Laguerre, M.2    Dufourc, E.J.3
  • 30
    • 0344117506 scopus 로고    scopus 로고
    • Ultrasound interaction with large unilamellar vesicles at the phospholipid phase transition: Perturbation by phospholipid side chain substitution with deuterium
    • R.P.D. Morse, and L.D. Ma F. Dunn Ultrasound interaction with large unilamellar vesicles at the phospholipid phase transition: perturbation by phospholipid side chain substitution with deuterium Chem. Phys. Lipids 103 1999 1 10
    • (1999) Chem. Phys. Lipids , vol.103 , pp. 1-10
    • Morse, R.P.D.1    Ma, L.D.2    Dunn, F.3
  • 31
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • M. Edidin The state of lipid rafts: from model membranes to cells Annu. Rev. Biophys. Biomol. Struct. 32 2003 257 283
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 32
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • D.A. Brown, and E. London Functions of lipid rafts in biological membranes Annu. Rev. Cell Dev. Biol. 14 1998 111 136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 33
    • 2142651634 scopus 로고    scopus 로고
    • Liquid domains in vesicles investigated by NMR and fluorescence microscopy
    • S.L. Veatch, and I.V. Polozov S.L. Keller Liquid domains in vesicles investigated by NMR and fluorescence microscopy Biophys. J. 86 2004 2910 2922
    • (2004) Biophys. J. , vol.86 , pp. 2910-2922
    • Veatch, S.L.1    Polozov, I.V.2    Keller, S.L.3
  • 34
    • 36749056331 scopus 로고    scopus 로고
    • Critical fluctuations in domain-forming lipid mixtures
    • S.L. Veatch, and O. Soubias K. Gawrisch Critical fluctuations in domain-forming lipid mixtures Proc. Natl. Acad. Sci. USA 104 2007 17650 17655
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17650-17655
    • Veatch, S.L.1    Soubias, O.2    Gawrisch, K.3
  • 35
    • 0031121546 scopus 로고    scopus 로고
    • Lipid domains as obstacles for lateral diffusion in supported bilayers probed at different time and length scales by two-dimensional exchange and field gradient solid state NMR
    • C. Dolainsky, P. Karakatsanis, and T.M. Bayerl Lipid domains as obstacles for lateral diffusion in supported bilayers probed at different time and length scales by two-dimensional exchange and field gradient solid state NMR Phys. Rev. E 55 1997 4512 4521
    • (1997) Phys. Rev. e , vol.55 , pp. 4512-4521
    • Dolainsky, C.1    Karakatsanis, P.2    Bayerl, T.M.3
  • 36
    • 58149185333 scopus 로고    scopus 로고
    • Lipid lateral diffusion and membrane heterogeneity
    • G. Lindblom, and G. Orädd Lipid lateral diffusion and membrane heterogeneity Biochim. Biophys. Acta 1788 2009 234 244
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 234-244
    • Lindblom, G.1    Orädd, G.2
  • 37
    • 66349138469 scopus 로고    scopus 로고
    • Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR
    • Y. Su, and T. Doherty M. Hong Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR Biochemistry 48 2009 4587 4595
    • (2009) Biochemistry , vol.48 , pp. 4587-4595
    • Su, Y.1    Doherty, T.2    Hong, M.3
  • 38
    • 77955330334 scopus 로고    scopus 로고
    • High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers
    • T. Doherty, Y. Su, and M. Hong High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers J. Mol. Biol. 401 2010 642 652
    • (2010) J. Mol. Biol. , vol.401 , pp. 642-652
    • Doherty, T.1    Su, Y.2    Hong, M.3
  • 39
    • 78149458565 scopus 로고    scopus 로고
    • The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption
    • Y. Zhang, W. Lu, and M. Hong The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption Biochemistry 49 2010 9770 9782.
    • (2010) Biochemistry , vol.49 , pp. 9770-9782
    • Zhang, Y.1    Lu, W.2    Hong, M.3


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