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Volumn 1668, Issue 2, 2005, Pages 175-189

The interactions of antimicrobial peptides derived from lysozyme with model membrane systems

Author keywords

Antimicrobial peptide; Lysozyme; Membrane mimetic; Phospholipid; Structure

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; ANTIINFECTIVE AGENT; ARGINYLALANYLTRYPTOPHYLVALYLALANYLTRYPTOPHYLARGININAMIDE; ARGINYLALANYLTRYPTOPHYLVALYLALANYLTRYPTOPHYLARGININE; DETERGENT; DIOLEOYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLETHANOLAMINE; DIOLEOYLPHOSPHATIDYLGLYCEROL; DODECYLPHOSPHORYLCHOLINE; FLUORESCEIN; GLYCEROPHOSPHOLIPID; ISOLEUCYLVALYLSERYLASPARTYLGLYCYLASPARAGINYLGLYCYLMETHIONYLASPARAGINYL ALANYLTRYPTOPHYLVALYLALANYLTRYPTOPHYLARGININAMIDE; LYSOZYME; SOLVENT; UNCLASSIFIED DRUG;

EID: 14544293955     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.12.004     Document Type: Article
Times cited : (95)

References (55)
  • 1
    • 0035873909 scopus 로고    scopus 로고
    • Design of Gram-negative selective antimicrobial peptides
    • S.A. Muhle, and J.P. Tam Design of Gram-negative selective antimicrobial peptides Biochemistry 40 2001 5777 5785
    • (2001) Biochemistry , vol.40 , pp. 5777-5785
    • Muhle, S.A.1    Tam, J.P.2
  • 2
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462 1999 1 10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 3
    • 0034691281 scopus 로고    scopus 로고
    • Design of salt-insensitive glycine-rich antimicrobial peptides with cyclic tricystine structures
    • J.P. Tam, Y.A. Lu, and J.L. Yang Design of salt-insensitive glycine-rich antimicrobial peptides with cyclic tricystine structures Biochemistry 39 2000 7159 7169
    • (2000) Biochemistry , vol.39 , pp. 7159-7169
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 5
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • H.W. Huang Action of antimicrobial peptides: two-state model Biochemistry 39 2000 8347 8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 6
    • 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
  • 7
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • P.M. Hwang, and H.J. Vogel Structure-function relationships of antimicrobial peptides Biochem. Cell. Biol. 76 1998 235 246
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 8
    • 0033786504 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Analysis and application
    • A.M. Cole, and T. Ganz Human antimicrobial peptides: analysis and application BioTechniques 29 2000 822 831
    • (2000) BioTechniques , vol.29 , pp. 822-831
    • Cole, A.M.1    Ganz, T.2
  • 9
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • H.J. Vogel, D.J. Schibli, W. Jing, E.M. Lohmeier-Vogel, R.F. Epand, and R.M. Epand Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides Biochem. Cell. Biol. 80 2002 49 63
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Jing, W.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 12
    • 0029966173 scopus 로고    scopus 로고
    • Bactericidal activity of a synthetic peptide (CG 117-136) of human lysosomal cathepsin G is dependent on arginine content
    • W.M. Shafer, F. Hubalek, M. Huang, and J. Pohl Bactericidal activity of a synthetic peptide (CG 117-136) of human lysosomal cathepsin G is dependent on arginine content Infect. Immun. 64 1996 4842 4845
    • (1996) Infect. Immun. , vol.64 , pp. 4842-4845
    • Shafer, W.M.1    Hubalek, F.2    Huang, M.3    Pohl, J.4
  • 13
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • H.R. Ibrahim, U. Thomas, and A. Pellegrini A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action J. Biol. Chem. 276 2001 43767 43774
    • (2001) J. Biol. Chem. , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 14
    • 0033903248 scopus 로고    scopus 로고
    • Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli
    • A. Pellegrini, U. Thomas, P. Wild, E. Schraner, and R. von Fellenberg Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli Microbiol. Res. 155 2000 69 77
    • (2000) Microbiol. Res. , vol.155 , pp. 69-77
    • Pellegrini, A.1    Thomas, U.2    Wild, P.3    Schraner, E.4    Von Fellenberg, R.5
  • 16
    • 1542472187 scopus 로고    scopus 로고
    • On the novel catalytically-independent antimicrobial function of hen egg-white lysozyme: A conformation-dependent activity
    • H.R. Ibrahim On the novel catalytically-independent antimicrobial function of hen egg-white lysozyme: a conformation-dependent activity Nahrung 42 1998 187 193
    • (1998) Nahrung , vol.42 , pp. 187-193
    • Ibrahim, H.R.1
  • 17
    • 1542347593 scopus 로고    scopus 로고
    • Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme
    • Y. Mine, F. Ma, and S. Lauriau Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme J. Agric. Food Chem. 52 2004 1088 1094
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1088-1094
    • Mine, Y.1    Ma, F.2    Lauriau, S.3
  • 20
    • 0036158880 scopus 로고    scopus 로고
    • The effects of charge and lipophilicity on the antibacterial activity of undecapeptides derived from bovine lactoferricin
    • M.B. Strom, O. Rekdal, and J.S. Svendsen The effects of charge and lipophilicity on the antibacterial activity of undecapeptides derived from bovine lactoferricin J. Pept. Sci. 8 2002 36 43
    • (2002) J. Pept. Sci. , vol.8 , pp. 36-43
    • Strom, M.B.1    Rekdal, O.2    Svendsen, J.S.3
  • 21
    • 0007781972 scopus 로고
    • Theory of the kinetics of micellar equilibria and quantitative interpretation of chemical relaxation studies of micellar solutions of ionic surfactants
    • E.A.G. Aniansson, S.N. Wall, M. Almgren, H. Hoffman, I. Kielmann, W. Ulbricht, R. Zana, J. Lang, and C. Tondre Theory of the kinetics of micellar equilibria and quantitative interpretation of chemical relaxation studies of micellar solutions of ionic surfactants J. Phys. Chem. 80 1976 905 922
    • (1976) J. Phys. Chem. , vol.80 , pp. 905-922
    • Aniansson, E.A.G.1    Wall, S.N.2    Almgren, M.3    Hoffman, H.4    Kielmann, I.5    Ulbricht, W.6    Zana, R.7    Lang, J.8    Tondre, C.9
  • 23
    • 0034687710 scopus 로고    scopus 로고
    • Interaction of a mitochondrial presequence with lipid membranes: Role of helix formation for membrane binding and perturbation
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation Biochemistry 39 2000 15297 15305
    • (2000) Biochemistry , vol.39 , pp. 15297-15305
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 24
    • 0033009036 scopus 로고    scopus 로고
    • Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes
    • E.J. Prenner, R.N. Lewis, L.H. Kondejewski, R.S. Hodges, and R.N. McElhaney Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes Biochim. Biophys. Acta 1417 1999 211 223
    • (1999) Biochim. Biophys. Acta , vol.1417 , pp. 211-223
    • Prenner, E.J.1    Lewis, R.N.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5
  • 25
    • 79960698472 scopus 로고
    • Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients
    • T.L. Hwang, and A.J. Shaka Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients J. Magn. Reson., A 112 1995 275 279
    • (1995) J. Magn. Reson., a , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 26
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • B.A. Johnson, and R.A. Blevins NMRView: a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 29
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • M. Nilges Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities J. Mol. Biol. 245 1995 645 660
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 30
    • 0347988396 scopus 로고    scopus 로고
    • Ambiguous NOEs and automated NOE assignment
    • M. Nilges, and S.I. O'Donoghue Ambiguous NOEs and automated NOE assignment Prog. NMR Spectrosc. 32 1998 107 115
    • (1998) Prog. NMR Spectrosc. , vol.32 , pp. 107-115
    • Nilges, M.1    O'Donoghue, S.I.2
  • 31
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • J.P. Linge, and M. Nilges Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation J. Biomol. NMR 13 1999 51 59
    • (1999) J. Biomol. NMR , vol.13 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 35
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • C.B. Park, H.S. Kim, and S.C. Kim Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions Biochem. Biophys. Res. Commun. 244 1998 253 257
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 36
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • C.B. Park, K.S. Yi, K. Matsuzaki, M.S. Kim, and S.C. Kim Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II Proc. Natl. Acad. Sci. U. S. A. 97 2000 8245 8250
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 37
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • S.J. Opella NMR and membrane proteins Nat. Struct. Biol. 4 1997 845 848 (Suppl.)
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 845-848
    • Opella, S.J.1
  • 38
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • G.D. Henry, and B.D. Sykes Methods to study membrane protein structure in solution Methods Enzymol. 239 1994 515 535
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 39
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • D.S. Wishart, B.D. Sykes, and F.M. Richards The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry 31 1992 1647 1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 40
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
    • M. Nilges, M.J. Macias, S.I. O'Donoghue, and H. Oschkinat Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin J. Mol. Biol. 269 1997 408 422
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    MacIas, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 41
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritrpticin bound to micelles: A distinct membrane-bound peptide fold
    • D.J. Schibli, P.M. Hwang, and H.J. Vogel Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold Biochemistry 38 1999 16749 16755
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 42
    • 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 1999 1363 1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 44
    • 0027375156 scopus 로고
    • The use of differential scanning calorimetry as a tool to characterize liposome preparations
    • R.L. Biltonen, and D. Lichtenberg The use of differential scanning calorimetry as a tool to characterize liposome preparations Chem. Phys. Lipids 64 1993 129 142
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 129-142
    • Biltonen, R.L.1    Lichtenberg, D.2
  • 46
    • 0030863833 scopus 로고    scopus 로고
    • Structural aspects of the interaction of peptidyl-glycylleucine- carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids
    • A. Latal, G. Degovics, R.F. Epand, R.M. Epand, and K. Lohner Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids Eur. J. Biochem. 248 1997 938 946
    • (1997) Eur. J. Biochem. , vol.248 , pp. 938-946
    • Latal, A.1    Degovics, G.2    Epand, R.F.3    Epand, R.M.4    Lohner, K.5
  • 47
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • K. Lohner, A. Latal, R.I. Lehrer, and T. Ganz Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems Biochemistry 36 1997 1525 1531
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 48
    • 0034707081 scopus 로고    scopus 로고
    • Titration calorimetry of surfactant-membrane partitioning and membrane solubilization
    • H. Heerklotz, and J. Seelig Titration calorimetry of surfactant-membrane partitioning and membrane solubilization Biochim. Biophys. Acta 1508 2000 69 85
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 69-85
    • Heerklotz, H.1    Seelig, J.2
  • 49
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects Biochemistry 39 2000 442 452
    • (2000) Biochemistry , vol.39 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 50
    • 0023056958 scopus 로고
    • Thermodynamic analysis of incorporation and aggregation in a membrane: Application to the pore-forming peptide alamethicin
    • G. Schwarz, S. Stankowski, and V. Rizzo Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin Biochim. Biophys. Acta 861 1986 141 151
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 141-151
    • Schwarz, G.1    Stankowski, S.2    Rizzo, V.3
  • 51
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium J. Mol. Biol. 294 1999 785 794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 52
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity
    • P. Casteels, and P. Tempst Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity Biochem. Biophys. Res. Commun. 199 1994 339 345
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 53
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Y. Shai Molecular recognition between membrane-spanning polypeptides Trends Biochem. Sci. 20 1995 460 464
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 54
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • D. Derossi, S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing, and A. Prochiantz Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent J. Biol. Chem. 271 1996 18188 18193
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 55
    • 0032582684 scopus 로고    scopus 로고
    • PR-39, a syndecan-inducing antimicrobial peptide, binds and affects p130(Cas)
    • Y.R. Chan, and R.L. Gallo PR-39, a syndecan-inducing antimicrobial peptide, binds and affects p130(Cas) J. Biol. Chem. 273 1998 28978 28985
    • (1998) J. Biol. Chem. , vol.273 , pp. 28978-28985
    • Chan, Y.R.1    Gallo, R.L.2


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