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Volumn 1798, Issue 6, 2010, Pages 1254-1262

Thermodynamics of RTA3 peptide binding to membranes and consequences for antimicrobial activity

Author keywords

Amphipathic peptide; Commensal organism; Cysteine; Free energy; Interfacial binding; Phospholipid bilayer

Indexed keywords

COLISTIN; POLYPEPTIDE ANTIBIOTIC AGENT; RTA3 PROTEIN; UNCLASSIFIED DRUG;

EID: 77952554008     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.03.017     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 49649113211 scopus 로고    scopus 로고
    • Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic peptides
    • Hawrani A., Howe R.A., Walsh T.R., Dempsey C.E. Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic peptides. J. Biol. Chem. 2008, 283:18636-18645.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18636-18645
    • Hawrani, A.1    Howe, R.A.2    Walsh, T.R.3    Dempsey, C.E.4
  • 2
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E.W., Lehrer R. Cationic peptides: a new source of antibiotics. Trend. Biotechnol. 1998, 16:82-88.
    • (1998) Trend. Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 1242307397 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides-an update
    • Zhang L.J., Falla T.J. Cationic antimicrobial peptides-an update. Exp. Opin. Invest. Drugs 2004, 13:97-106.
    • (2004) Exp. Opin. Invest. Drugs , vol.13 , pp. 97-106
    • Zhang, L.J.1    Falla, T.J.2
  • 6
    • 33746916083 scopus 로고    scopus 로고
    • Novel therapies based on cationic antimicrobial peptides
    • Pereira H.A. Novel therapies based on cationic antimicrobial peptides. Curr. Pharm. Biotech. 2006, 7:229-234.
    • (2006) Curr. Pharm. Biotech. , vol.7 , pp. 229-234
    • Pereira, H.A.1
  • 7
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • Matsuzaki K. Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta 2009, 1788:1687-1692.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1
  • 8
    • 70349496543 scopus 로고    scopus 로고
    • New approaches in peptide antibiotics
    • Vaara M. New approaches in peptide antibiotics. Curr. Opin. Pharmacol. 2009, 9:571-576.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 571-576
    • Vaara, M.1
  • 9
    • 4444246183 scopus 로고    scopus 로고
    • Increased diversity of intestinal antimicrobial peptides by covalent dimer formation
    • Hornef M.W., Putsep K., Karlsson J., Refai E., Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. Nat. Immunol. 2004, 5:836-843.
    • (2004) Nat. Immunol. , vol.5 , pp. 836-843
    • Hornef, M.W.1    Putsep, K.2    Karlsson, J.3    Refai, E.4    Andersson, M.5
  • 10
    • 0035815466 scopus 로고    scopus 로고
    • A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta
    • Batista C.V.F., Scaloni A., Rigden D.J., et al. A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta. FEBS Lett. 2001, 494:85-89.
    • (2001) FEBS Lett. , vol.494 , pp. 85-89
    • Batista, C.V.F.1    Scaloni, A.2    Rigden, D.J.3
  • 11
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 1995, 13:61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 12
    • 23644438035 scopus 로고    scopus 로고
    • Maximin 9, a novel free thiol containing antimicrobial peptide with antimycoplasma activity from frog Bombina maxima
    • Lee W.H., Zhang H., Zhang Y.X., Jin Y., Lai R., Zhang Y. Maximin 9, a novel free thiol containing antimicrobial peptide with antimycoplasma activity from frog Bombina maxima. FEBS Lett. 2005, 579:4443-4448.
    • (2005) FEBS Lett. , vol.579 , pp. 4443-4448
    • Lee, W.H.1    Zhang, H.2    Zhang, Y.X.3    Jin, Y.4    Lai, R.5    Zhang, Y.6
  • 14
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin A.S., Jayasinghe S., White S.H. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?. Anal. Biochem. 2000, 285:235-245.
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 15
    • 0029283976 scopus 로고
    • The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide membrane interactions
    • Wall J., Golding C.A., van Veen M., O'Shea P. The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide membrane interactions. Mol. Membr. Biol. 1995, 12:183-192.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 183-192
    • Wall, J.1    Golding, C.A.2    van Veen, M.3    O'Shea, P.4
  • 16
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer-membrane permeabilization and bacteriolysis in Escherichia-coli by multiple wavelength spectrophotometry
    • Lehrer R.I., Barton A., Ganz T. Concurrent assessment of inner and outer-membrane permeabilization and bacteriolysis in Escherichia-coli by multiple wavelength spectrophotometry. J. Immunol. Met. 1988, 108:153-158.
    • (1988) J. Immunol. Met. , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 17
    • 0344625371 scopus 로고    scopus 로고
    • Self-association of disulphide-dimerised melittin analogues
    • Takei J., Remenyi A., Clarke A.R., Dempsey C.E. Self-association of disulphide-dimerised melittin analogues. Biochem. 1998, 37:5699-5708.
    • (1998) Biochem. , vol.37 , pp. 5699-5708
    • Takei, J.1    Remenyi, A.2    Clarke, A.R.3    Dempsey, C.E.4
  • 18
    • 0037457904 scopus 로고    scopus 로고
    • Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue
    • Dempsey C.E., Ueno S., Avison M.B. Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue. Biochem. 2003, 42:402-409.
    • (2003) Biochem. , vol.42 , pp. 402-409
    • Dempsey, C.E.1    Ueno, S.2    Avison, M.B.3
  • 19
    • 34250195381 scopus 로고    scopus 로고
    • Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity
    • Fernandez-Vidall M., Jayasinghe S., Ladokhin A.S., White S.H. Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity. J. Mol. Biol. 2007, 370:459-470.
    • (2007) J. Mol. Biol. , vol.370 , pp. 459-470
    • Fernandez-Vidall, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4
  • 20
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara M. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 1992, 56:395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 21
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu M.H., Maier E., Benz R., Hancock R.E.W. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochem. 1999, 38:7235-7242.
    • (1999) Biochem. , vol.38 , pp. 7235-7242
    • Wu, M.H.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 22
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 1996, 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 23
    • 34247595392 scopus 로고    scopus 로고
    • Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins
    • Wolfenden R. Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins. J. Gen. Physiol. 2007, 129:357-362.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 357-362
    • Wolfenden, R.1
  • 25
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and membrane perturbations of melittin at the membrane interface
    • Hristova K., Dempsey C.E., White S.H. Structure, location, and membrane 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
  • 26
    • 0032932914 scopus 로고    scopus 로고
    • Generalized bilayer perturbation from peptide helix dimerisation at membrane surfaces: vesicle lysis induced by disulphide-dimerised melittin analogues
    • Takei J., Remenyi A., Dempsey C.E. Generalized bilayer perturbation from peptide helix dimerisation at membrane surfaces: vesicle lysis induced by disulphide-dimerised melittin analogues. FEBS Lett. 1999, 442:11-14.
    • (1999) FEBS Lett. , vol.442 , pp. 11-14
    • Takei, J.1    Remenyi, A.2    Dempsey, C.E.3
  • 27
    • 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
  • 29
    • 38349116218 scopus 로고    scopus 로고
    • Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'
    • Pag U., Oedenkoven M., Sass V., Shai Y., Shamova O., Antcheva N., Tossi A., Sahl H.G. Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'. J. Antimicrob. Chemother. 2008, 61:341-352.
    • (2008) J. Antimicrob. Chemother. , vol.61 , pp. 341-352
    • Pag, U.1    Oedenkoven, M.2    Sass, V.3    Shai, Y.4    Shamova, O.5    Antcheva, N.6    Tossi, A.7    Sahl, H.G.8
  • 30
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima K., Chikushi A., Lee K.-K., Yonehara S., Matsuzaki K. Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes. J. Biol. Chem. 2003, 278:1310-1315.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1310-1315
    • Takeshima, K.1    Chikushi, A.2    Lee, K.-K.3    Yonehara, S.4    Matsuzaki, K.5
  • 31
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides
    • Nicolas P. Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides. FEBS J. 2009, 276:6483-6496.
    • (2009) FEBS J. , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 32
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of amino acids in a lipid bilayer from computer simulations
    • MacCallum J.L., Bennett W.F.D., Tieleman D.P. Distribution of amino acids in a lipid bilayer from computer simulations. Biophys. J. 2008, 94:3393-3404.
    • (2008) Biophys. J. , vol.94 , pp. 3393-3404
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.