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Volumn 58, Issue 4, 2014, Pages 1987-1996

Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; ENDOTOXIN; INDOLICIDIN; LIPOPOLYSACCHARIDE; MAGAININ DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 84896954250     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02321-13     Document Type: Article
Times cited : (66)

References (69)
  • 1
    • 0025285857 scopus 로고
    • Biochemistry of endotoxins
    • Raetz CRH. 1990. Biochemistry of endotoxins. Annu. Rev. Biochem. 59:129-170. http://dx.doi.org/10.1146/annurev.bi.59.070190.001021.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 129-170
    • Raetz, C.R.H.1
  • 2
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane in Escherichia coli and Salmonella typhimurium
    • Neidhardt NC, Curtiss R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed.), 2nd ed. American Society for Microbiology, Washington, DC
    • Nikaido H. 1999. Outer membrane in Escherichia coli and Salmonella typhimurium, p 29-47. In Neidhardt NC, Curtiss R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, DC.
    • (1999) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 29-47
    • Nikaido, H.1
  • 3
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido H. 1994. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264:382-388. http://dx.doi.org/10.1126/science.8153625. (Pubitemid 24178901)
    • (1994) Science , vol.264 , Issue.5157 , pp. 382-388
    • Nikaido, H.1
  • 4
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H, Vaara M. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32. (Pubitemid 15134118)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 5
    • 0034718563 scopus 로고    scopus 로고
    • The lipopolysaccharide barrier: Correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics
    • Snyder DS, McIntosh TJ. 2000. The lipopolysaccharide barrier: correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics. Biochemistry 39:11777-11787. http://dx.doi.org/10.1021/ bi000810n.
    • (2000) Biochemistry , vol.39 , pp. 11777-11787
    • Snyder, D.S.1    McIntosh, T.J.2
  • 6
    • 0037180768 scopus 로고    scopus 로고
    • The immunopathogenesis of sepsis
    • DOI 10.1038/nature01326
    • Cohen J. 2002. The immunopathogenesis of sepsis. Nature 420:885-891. http://dx.doi.org/10.1038/nature01326. (Pubitemid 36019643)
    • (2002) Nature , vol.420 , Issue.6917 , pp. 885-891
    • Cohen, J.1
  • 7
    • 0037317763 scopus 로고    scopus 로고
    • Innate immune sensing and its roots: The story of endotoxin
    • DOI 10.1038/nri1004
    • Beutler B, Rietschel ET. 2003. Innate immune sensing and its roots: the story of endotoxin. Nat. Rev. Immunol. 3:169-176. http://dx.doi.org/10.1038/ nri1004. (Pubitemid 37328694)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.2 , pp. 169-176
    • Beutler, B.1    Rietschel, E.Th.2
  • 8
    • 1142310879 scopus 로고    scopus 로고
    • The dark side of C5a in sepsis
    • Ward PA. 2004. The dark side of C5a in sepsis. Nat. Rev. Immunol. 4:133-142. http://dx.doi.org/10.1038/nri1269. (Pubitemid 38209207)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.2 , pp. 133-142
    • Ward, P.A.1
  • 9
    • 11144290631 scopus 로고    scopus 로고
    • LPS, TLR4 and infectious disease diversity
    • DOI 10.1038/nrmicro1068
    • Miller SI, Ernst RK, Bader MW. 2005. LPS, TLR4 and infectious disease diversity. Nat. Rev. Microbiol. 3:36-46. http://dx.doi.org/10.1038/nrmicro1068. (Pubitemid 40028467)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.1 , pp. 36-46
    • Miller, S.I.1    Ernst, R.K.2    Bader, M.W.3
  • 10
    • 0035434019 scopus 로고    scopus 로고
    • Sepsis syndromes: Understanding the role of innate and acquired immunity
    • Oberholzer A, Oberholzer C, Moldawer LL. 2001. Sepsis syndromes: understanding the role of innate and acquired immunity. Shock 16:83-96. http://dx.doi.org/10.1097/00024382-200116020-00001. (Pubitemid 33596740)
    • (2001) Shock , vol.16 , Issue.2 , pp. 83-96
    • Oberholzer, A.1    Oberholzer, C.2    Moldawer, L.L.3
  • 11
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • DOI 10.1056/NEJMoa022139
    • Martin GS, Mannino DM, Eaton S, Moss M. 2003. The epidemiology of sepsis in the United States from 1979 through 2000. N. Engl. J. Med. 348:1546-1554. http://dx.doi.org/10.1056/NEJMoa022139. (Pubitemid 36437931)
    • (2003) New England Journal of Medicine , vol.348 , Issue.16 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 12
    • 0034924156 scopus 로고    scopus 로고
    • Epidemiology of sepsis: An update
    • Angus DC, Wax RS. 2001. Epidemiology of sepsis: an update. Crit. Care Med. 29:S109-S116. http://dx.doi.org/10.1097/00003246-200107001-00035. (Pubitemid 32681592)
    • (2001) Critical Care Medicine , vol.29 , Issue.7 SUPPL.
    • Angus, D.C.1    Wax, R.S.2
  • 14
    • 27644577000 scopus 로고    scopus 로고
    • Animal models of sepsis: Setting the stage
    • Buras JA, Holzmann B, Sitkovsky M. 2005. Animal models of sepsis: setting the stage. Nat. Rev. Drug Disc. 4:854-865. http://dx.doi.org/10.1038/nrd1854.
    • (2005) Nat. Rev. Drug Disc. , vol.4 , pp. 854-865
    • Buras, J.A.1    Holzmann, B.2    Sitkovsky, M.3
  • 15
    • 84255183707 scopus 로고    scopus 로고
    • The search for effective therapy for sepsis: Back to the drawing board?
    • Angus DC. 2011. The search for effective therapy for sepsis: back to the drawing board? JAMA 306:2614-2615. http://dx.doi.org/10.1001/jama.2011.1853.
    • (2011) JAMA , vol.306 , pp. 2614-2615
    • Angus, D.C.1
  • 16
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395. http://dx.doi.org/10.1038/415389a. (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 17
    • 84857411069 scopus 로고    scopus 로고
    • Designing antimicrobial peptides: Form follows function
    • Fjell CD, Hiss JA, Hancock RE, Schneider G. 2011. Designing antimicrobial peptides: form follows function. Nat. Rev. Drug Disc. 11:37-51. http://dx.doi.org/10.1038/nrd3591.
    • (2011) Nat. Rev. Drug Disc. , vol.11 , pp. 37-51
    • Fjell, C.D.1    Hiss, J.A.2    Hancock, R.E.3    Schneider, G.4
  • 18
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a come back
    • Fox JL. 2013. Antimicrobial peptides stage a come back. Nat. Biotechnol. 31:379-382. http://dx.doi.org/10.1038/nbt.2572.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 379-382
    • Fox, J.L.1
  • 19
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: Primeval molecules or future drugs?
    • Peters BM, Shirtliff ME, Jabra-Rizk MA. 2010. Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog. 6:e1001067. http://dx.doi.org/10.1371/journal.ppat.1001067.
    • (2010) PLoS Pathog. , vol.6
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 20
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • Yount NY, Yeaman MR. 2013. Peptide antimicrobials: cell wall as a bacterial target Ann. N. Y. Acad. Sci. 1277:127-138. http://dx.doi.org/10.1111/ nyas.12005.
    • (2013) Ann. N. Y. Acad. Sci. , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 21
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • Hancock RE, Sahl HG. 2006. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24:1551-1557. http://dx.doi.org/10.1038/nbt1267. (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 22
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: An overview of a promising class of therapeutics
    • Giuliani A, Pirri G, Nicoletto S. 2007. Antimicrobial peptides: an overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2:1-33. http://dx.doi.org/10.2478/s11535-007-0010-5.
    • (2007) Cent. Eur. J. Biol. , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.3
  • 23
    • 0036257510 scopus 로고    scopus 로고
    • From innate immunity to de-Novo designed antimicrobial peptides
    • DOI 10.2174/1381612023395367
    • Shai Y. 2002. From innate immunity to de novo-designed antimicrobial peptides. Curr. Pharm. Des. 8:715-725. http://dx.doi.org/10.2174/ 1381612023395367. (Pubitemid 34498561)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.9 , pp. 715-725
    • Shai, Y.1
  • 24
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • DOI 10.1021/bi000946l
    • Huang HW. 2000. Action of antimicrobial peptides: two-state model. Biochemistry 39:8347-8352. http://dx.doi.org/10.1021/bi000946l. (Pubitemid 30489931)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 26
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen LT, Haney EF, Vogel HJ. 2011. The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 9:464-472.
    • (2011) Trends Biotechnol. , vol.9 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 27
    • 65649114368 scopus 로고    scopus 로고
    • Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface
    • Harris M, Mora-Montes HM, Gow NA, Coote PJ. 2009. Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface. Microbiology 155:1058-1070. http://dx.doi.org/10.1099/mic.0.026120-0.
    • (2009) Microbiology , vol.155 , pp. 1058-1070
    • Harris, M.1    Mora-Montes, H.M.2    Gow, N.A.3    Coote, P.J.4
  • 28
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides
    • Nicolas P. 2009. Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides. FEBS J. 276:6483-6496. http://dx.doi.org/10.1111/j.1742-4658.2009.07359.x.
    • (2009) FEBS J. , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 29
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • DOI 10.1124/pr.55.1.2
    • Yeaman MR, Yount NY. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55:27-55. http://dx.doi.org/10.1124/pr.55.1.2. (Pubitemid 36268398)
    • (2003) Pharmacological Reviews , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 30
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • DOI 10.1016/S0304-4157(98)00014-8, PII S0304415798000148
    • Matsuzaki K. 1998. Magainins as paradigm for the mode of action of pore-forming polypeptides. Biochim. Biophys. Acta 1376:391-400. http://dx.doi.org/10.1016/S0304-4157(98)00014-8. (Pubitemid 28517888)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 391-400
    • Matsuzaki, K.1
  • 31
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y. 1998. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47:451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 32
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley WC. 2010. Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem. Biol. 5:905-917. http://dx.doi.org/10.1021/cb1001558.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 33
    • 79955637689 scopus 로고    scopus 로고
    • Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
    • Sochacki KA, Barns KJ, Bucki R, Weisshaar JC. 2011. Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37. Proc. Natl. Acad. Sci. U. S. A. 108:e77-e81. http://dx.doi.org/10.1073/pnas. 1101130108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Sochacki, K.A.1    Barns, K.J.2    Bucki, R.3    Weisshaar, J.C.4
  • 34
    • 0033540629 scopus 로고    scopus 로고
    • Incremental conversion of outer-membrane permeabilizers into potent antibiotics for gram-negative bacteria
    • Chunhong Li, Loren PB, Collin DD, Barry MW, Glenn WA, Paul BS. 1999. Incremental conversion of outer-membrane permeabilizers into potent antibiotics for gram-negative bacteria J. Am. Chem. Soc. 121:931-940. http://dx.doi.org/10. 1021/ja982938m.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 931-940
    • Li, C.1    Loren, P.B.2    Collin, D.D.3    Barry, M.W.4    Glenn, W.A.5    Paul, B.S.6
  • 35
    • 0021185399 scopus 로고
    • Alterations in outer membrane permeability
    • Hancock REW. 1984. Alterations in outer membrane permeability. Annu. Rev. Microbiol. 38:237-264. http://dx.doi.org/10.1146/annurev.mi.38.100184.001321.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 237-264
    • Hancock, R.E.W.1
  • 36
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • DOI 10.1021/bi962507l
    • Oren Z, Shai Y. 1997. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36:1826-1835. http://dx.doi.org/10.1021/bi962507l. (Pubitemid 27086279)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 37
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • DOI 10.1038/292246a0
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG. 1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246-248. (Pubitemid 11001840)
    • (1981) Nature , vol.292 , Issue.5820 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3
  • 38
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and normal microflora
    • Boman HG. 2000. Innate immunity and normal microflora. Immunol. Rev. 173:5-16. http://dx.doi.org/10.1034/j.1600-065X.2000.917301.x.
    • (2000) Immunol. Rev. , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 39
    • 84864451396 scopus 로고    scopus 로고
    • Ab initio design of potent anti-MRSA peptides based on database filtering technology
    • Biswajit M, Guangshun W. 2012. Ab initio design of potent anti-MRSA peptides based on database filtering technology. J. Am. Chem. Soc. 134:12426-12429. http://dx.doi.org/10.1021/ja305644e.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 12426-12429
    • Biswajit, M.1    Guangshun, W.2
  • 40
    • 84881503329 scopus 로고    scopus 로고
    • Structure, antimicrobial activities and mode of interaction with membranes of bovel phylloseptins from the painted-belly leaf frog, Phyllomedusa sauvagii
    • Raja Z, André S, Piesse C, Sereno D, Nicolas P, Foulon T, Oury B, Ladram A. 2013. Structure, antimicrobial activities and mode of interaction with membranes of bovel phylloseptins from the painted-belly leaf frog, Phyllomedusa sauvagii. PLoS One 8:e70782. http://dx.doi.org/10.1371/journal.pone.0070782.
    • (2013) PLoS One , vol.8
    • Raja, Z.1    André, S.2    Piesse, C.3    Sereno, D.4    Nicolas, P.5    Foulon, T.6    Oury, B.7    Ladram, A.8
  • 41
    • 0033578344 scopus 로고    scopus 로고
    • Lipopolysaccharide bilayer structure: Effect of chemotype, core mutations, divalent cations, and temperature
    • Snyder S, Kim D, McIntosh TJ. 1999. Lipopolysaccharide bilayer structure: effect of chemotype, core mutations, divalent cations, and temperature. Biochemistry 38:10758-10767. http://dx.doi.org/10.1021/bi990867d.
    • (1999) Biochemistry , vol.38 , pp. 10758-10767
    • Snyder, S.1    Kim, D.2    McIntosh, T.J.3
  • 42
    • 0021959566 scopus 로고
    • High state of order of isolated bacterial lipopolysaccharide and its possible contribution to the permeation barrier property of the outer membrane
    • Labischinski H, Barnickel G, Bradaczek H, Naumann D, Rietschel ET, Giesbrecht P. 1985. High state of order of isolated bacterial lipopolysaccharide and its possible contribution to the permeation barrier property of the outer membrane. J. Bacteriol. 162:9-20. (Pubitemid 15095824)
    • (1985) Journal of Bacteriology , vol.162 , Issue.1 , pp. 9-20
    • Labischinski, H.1    Barnickel, G.2    Bradaczek, H.3
  • 43
    • 0037417761 scopus 로고    scopus 로고
    • Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis
    • DOI 10.1021/bi026932s
    • Allende D, McIntosh TJ. 2003. Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis. Biochemistry 42:1101-1108. http://dx.doi.org/10.1021/bi026932s. (Pubitemid 36159545)
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1101-1108
    • Allende, D.1    McIntosh, T.J.2
  • 44
    • 60749118629 scopus 로고    scopus 로고
    • Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy
    • Bhunia A, Ramamoorthy A, Bhattacharjya S. 2009. Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy. Chemistry 15:2036-2040. http://dx.doi.org/10.1002/chem.200802635.
    • (2009) Chemistry , vol.15 , pp. 2036-2040
    • Bhunia, A.1    Ramamoorthy, A.2    Bhattacharjya, S.3
  • 45
    • 77950515754 scopus 로고    scopus 로고
    • NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: Mechanism of outer membrane permeabilization
    • Bhunia A, Domadia P, Torres J, Hallock KJ, Ramamoorthy A, Bhattacharjya S. 2010. NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization. J. Biol. Chem. 285:3883-3895. http://dx.doi.org/10.1074/jbc.M109.065672.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3883-3895
    • Bhunia, A.1    Domadia, P.2    Torres, J.3    Hallock, K.J.4    Ramamoorthy, A.5    Bhattacharjya, S.6
  • 46
    • 78650599747 scopus 로고    scopus 로고
    • Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: Role of helical hairpin conformation in outer membrane permeabilization
    • Domadia P, Bhunia A, Ramamoorthy A, Bhattacharjya S. 2012. Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: role of helical hairpin conformation in outer membrane permeabilization. J. Am. Chem. Soc. 132:18417-18428.
    • (2012) J. Am. Chem. Soc. , vol.132 , pp. 18417-18428
    • Domadia, P.1    Bhunia, A.2    Ramamoorthy, A.3    Bhattacharjya, S.4
  • 47
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach MA, Walsh CT. 2009. Antibiotics for emerging pathogens. Science 325:1089-1093. http://dx.doi.org/10.1126/science.1176667.
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 48
    • 47749093130 scopus 로고    scopus 로고
    • The bacteria fight back
    • Taubes G. 2008. The bacteria fight back. Science 321:356-361. http://dx.doi.org/10.1126/science.321.5887.356.
    • (2008) Science , vol.321 , pp. 356-361
    • Taubes, G.1
  • 49
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides
    • DOI 10.1074/jbc.M412865200
    • Papo N, Shai Y. 2005. A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides. J. Biol. Chem. 280:10378-10387. http://dx.doi.org/10.1074/jbc.M412865200. (Pubitemid 40395894)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 50
    • 33749376461 scopus 로고    scopus 로고
    • A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer
    • DOI 10.1074/jbc.M606031200
    • Rosenfeld Y, Barra D, Simmaco M, Shai Y, Mangoni ML. 2006. A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer. J. Biol. Chem. 281:28565-28574. http://dx.doi.org/10.1074/jbc.M606031200. (Pubitemid 44506999)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28565-28574
    • Rosenfeld, Y.1    Barra, D.2    Simmaco, M.3    Shai, Y.4    Mangoni, M.L.5
  • 51
    • 53149151881 scopus 로고    scopus 로고
    • Lipopolysaccharide, a key molecule involved in the synergism between temporins in inhibiting bacterial growth and in endotoxin neutralization
    • Mangoni ML, Epand RF, Rosenfeld Y, Peleg A, Barra D, Epand RM, Shai Y. 2008. Lipopolysaccharide, a key molecule involved in the synergism between temporins in inhibiting bacterial growth and in endotoxin neutralization. J. Biol. Chem. 283:22907-22917. http://dx.doi.org/10.1074/jbc.M800495200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22907-22917
    • Mangoni, M.L.1    Epand, R.F.2    Rosenfeld, Y.3    Peleg, A.4    Barra, D.5    Epand, R.M.6    Shai, Y.7
  • 52
    • 67649401884 scopus 로고    scopus 로고
    • Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification
    • Mangoni ML, Shai Y. 2009. Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification. Biochim. Biophys. Acta 1788:1610-1619. http://dx.doi.org/10.1016/j.bbamem.2009.04.021.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1610-1619
    • Mangoni, M.L.1    Shai, Y.2
  • 53
    • 33744459976 scopus 로고    scopus 로고
    • Temporins, anti-infective peptides with expanding properties
    • DOI 10.1007/s00018-005-5536-y
    • Mangoni ML. 2006. Temporins, anti-infective peptides with expanding properties. Cell. Mol. Life Sci. 63:1060-1069. http://dx.doi.org/10.1007/s00018- 005-5536-y. (Pubitemid 43800775)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.9 , pp. 1060-1069
    • Mangoni, M.L.1
  • 54
    • 79959903251 scopus 로고    scopus 로고
    • NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: Mechanistic insights into outer membrane permeabilization and synergistic activity
    • Bhunia A, Saravanan R, Mohanram H, Mangoni ML, Bhattacharjya S. 2011. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J. Biol. Chem. 286:24394-24406. http://dx.doi.org/10.1074/jbc.M110.189662.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24394-24406
    • Bhunia, A.1    Saravanan, R.2    Mohanram, H.3    Mangoni, M.L.4    Bhattacharjya, S.5
  • 55
    • 84883622438 scopus 로고    scopus 로고
    • NMR structure of temporin-1 Ta in lipopolysaccharide micelles: Mechanistic insight into inactivation by outer membrane
    • Saravanan R, Joshi M, Mohanram H, Bhunia A, Mangoni ML, Bhattacharjya S. 2013. NMR structure of temporin-1 Ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane. PLoS One 8:e72718. http://dx.doi.org/10.1371/journal.pone.0072718.
    • (2013) PLoS One , vol.8
    • Saravanan, R.1    Joshi, M.2    Mohanram, H.3    Bhunia, A.4    Mangoni, M.L.5    Bhattacharjya, S.6
  • 56
    • 34248995513 scopus 로고    scopus 로고
    • High-resolution solution structure of a designed peptide bound to lipopolysaccharide: Transferred nuclear overhauser effects, micelle selectivity, and anti-endotoxic activity
    • DOI 10.1021/bi6025159
    • Bhattacharjya S, Domadia PN, Bhunia A, Malladi S, David SA. 2007. High resolution solution structure of a designed peptide bound to lipopolysaccharide: transferred nuclear Overhauser effects, micelle selectivity and anti-endotoxic activity. Biochemistry 46:5864-5874. http://dx.doi.org/10.1021/bi6025159. (Pubitemid 46799149)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 5864-5874
    • Bhattacharjya, S.1    Domadia, P.N.2    Bhunia, A.3    Malladi, S.4    David, S.A.5
  • 57
    • 69249119005 scopus 로고    scopus 로고
    • Designed beta-boomerang antiendotoxic and antimicrobial peptides: Structures and activities in lipopolysaccharide
    • Bhunia A, Mohanram H, Domadia PN, Torres J, Bhattacharjya S. 2009. Designed beta-boomerang antiendotoxic and antimicrobial peptides: structures and activities in lipopolysaccharide. J. Biol. Chem. 284:21991-22004. http://dx.doi.org/10.1074/jbc.M109.013573.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21991-22004
    • Bhunia, A.1    Mohanram, H.2    Domadia, P.N.3    Torres, J.4    Bhattacharjya, S.5
  • 58
    • 0030437748 scopus 로고    scopus 로고
    • Temporins, antimicrobial peptides from the European red frog Rana temporaria
    • Maurizio S, Giuseppina M, Silvia C, Rossella M, Mangoni ML, Donatella B. 1996. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur. J. Biochem. 242:788-792. http://dx.doi.org/10.1111/j.1432-1033. 1996.0788r.x. (Pubitemid 27121165)
    • (1996) European Journal of Biochemistry , vol.242 , Issue.3 , pp. 788-792
    • Simmaco, M.1    Mignogna, G.2    Canofeni, S.3    Miele, R.4    Mangoni, M.L.5    Barra, D.6
  • 59
    • 0030949875 scopus 로고    scopus 로고
    • Human - Defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • DOI 10.1016/S0092-8674(00)81895-4
    • Goldman MJ, Anderson GM, Stolzenberg DE, Kari UP, Zasloff M, Wilson MJ. 1997. Human - defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88:553-560. http://dx.doi.org/10.1016/ S0092-8674(00)81895-4. (Pubitemid 27154420)
    • (1997) Cell , vol.88 , Issue.4 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 60
    • 1842373858 scopus 로고    scopus 로고
    • Effects of pH and salinity on the antimicrobial properties of clavanins
    • Lee IH, Cho Y, Lehrer RI. 1997. Effects of pH and salinity on the antimicrobial properties of clavanins. Infect. Immun. 65:2898-2903. (Pubitemid 27264123)
    • (1997) Infection and Immunity , vol.65 , Issue.7 , pp. 2898-2903
    • Hee, L.I.N.1    Cho, Y.2    Lehrer, R.I.3
  • 61
    • 1842639632 scopus 로고    scopus 로고
    • Helix Stability Confers Salt Resistance upon Helical Antimicrobial Peptides
    • DOI 10.1074/jbc.M311418200
    • Park IY, Cho JH, Kim KS, Kim YB, Kim MS, Kim SC. 2004. Helix stability confers salt resistance upon helical antimicrobial peptides. J. Biol. Chem. 279:13896-13901. http://dx.doi.org/10.1074/jbc.M311418200. (Pubitemid 38468922)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13896-13901
    • Park, I.Y.1    Cho, J.H.2    Kim, K.S.3    Kim, Y.-B.4    Kim, M.S.5    Kim, S.C.6
  • 64
    • 3142770748 scopus 로고    scopus 로고
    • Endotoxin neutralizing peptides
    • DOI 10.2174/1568026043388079
    • Jerala R, Porro M. 2004. Endotoxin neutralizing peptides. Curr. Top. Med. Chem. 4:1173-1184. http://dx.doi.org/10.2174/1568026043388079. (Pubitemid 38923440)
    • (2004) Current Topics in Medicinal Chemistry , vol.4 , Issue.11 , pp. 1173-1184
    • Jerala, R.1    Porro, M.2
  • 65
    • 77955600292 scopus 로고    scopus 로고
    • De novo designed lipopolysaccharide binding peptides: Structure based development of antiendotoxic and antimicrobial drugs
    • Bhattacharjya S. 2010. De novo designed lipopolysaccharide binding peptides: structure based development of antiendotoxic and antimicrobial drugs. Curr. Med. Chem. 17:3080-3093. http://dx.doi.org/10.2174/092986710791959756.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3080-3093
    • Bhattacharjya, S.1
  • 66
    • 0029870193 scopus 로고    scopus 로고
    • Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A
    • Srimal S, Surolia N, Balasubramanian S, Surolia A. 1996. Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A. Biochem. J. 315:679-686.
    • (1996) Biochem. J. , vol.315 , pp. 679-686
    • Srimal, S.1    Surolia, N.2    Balasubramanian, S.3    Surolia, A.4
  • 67
    • 34147162786 scopus 로고    scopus 로고
    • Thermodynamic analysis of the lipopolysaccharide-dependent resistance of Gram-negative bacteria against polymyxin B
    • DOI 10.1529/biophysj.106.095711
    • Howe J, Andra J, Conde R, Iriarte M, Garidel P, Koch MH, Gutsmann T, Moriyon I, Brandenburg K. 2007. Thermodynamic analysis of the lipopolysaccharide dependent resistance of Gram-negative bacteria against polymyxin B Biophys. J. 92:2796-2805. (Pubitemid 46557854)
    • (2007) Biophysical Journal , vol.92 , Issue.8 , pp. 2796-2805
    • Howe, J.1    Andra, J.2    Conde, R.3    Iriarte, M.4    Garidel, P.5    Koch, M.H.J.6    Gutsmann, T.7    Moriyon, I.8    Brandenburg, K.9
  • 68
    • 0028924539 scopus 로고
    • Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14
    • Tobias PS, Soldau K, Gegner JA, Mintz D, Ulevitch RJ. 1995. Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14. J. Biol. Chem. 270:10482-10488. http://dx.doi.org/10.1074/ jbc.270.18.10482.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10482-10488
    • Tobias, P.S.1    Soldau, K.2    Gegner, J.A.3    Mintz, D.4    Ulevitch, R.J.5
  • 69
    • 45749084085 scopus 로고    scopus 로고
    • Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides
    • DOI 10.1021/bi800450f
    • Rosenfeld Y, Sahl HG, Shai Y. 2008. Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides. Biochemistry 47:6468-6478. http://dx.doi.org/10.1021/bi800450f. (Pubitemid 351874238)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6468-6478
    • Rosenfeld, Y.1    Sahl, H.-G.2    Shai, Y.3


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