메뉴 건너뛰기




Volumn 5, Issue 6, 2007, Pages 951-959

Alternative mechanisms of action of cationic antimicrobial peptides on bacteria

Author keywords

Antibacterial; Cationic antimicrobial peptide; Mechanism of action; Synergy

Indexed keywords

ALAMETHICIN; ANTIBIOTIC AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; APIDAECIN; BACTENECIN; BACTERIAL DNA; BACTERIAL RNA; BACTERIOCIN; BETA LACTAM ANTIBIOTIC; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CECROPIN; CP10A; DERMASEPTIN; DROSOCIN; GALLIDERMIN; GALLINACIN; INDOLICIDIN; LACTACIN; LANTIBIOTIC; MACROLIDE; MAGAININ 2; MICROCIN; MUTACIN; NISIN; PEP5 PROTEIN; PLEUROCIDIN DERIVATIVE; PR 39; PROTEGRIN; PYRRHOCORICIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 37349104237     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/14787210.5.6.951     Document Type: Review
Times cited : (480)

References (66)
  • 3
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock REW. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18(1), 24-30 (2006).
    • (2006) Curr. Opin. Immunol , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 4
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers JP, Hancock REW. The relationship between peptide structure and antibacterial activity. Peptides 24(11), 1681-1691 (2003).
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.W.2
  • 5
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock REW, Sahl HG. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24(12), 1551-1557 (2006).
    • (2006) Nat. Biotechnol , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 6
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel A, Sahl HG. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev Microbiol. 4(7), 529-536 (2006).
    • (2006) Nat. Rev Microbiol , vol.4 , Issue.7 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 7
    • 33745194211 scopus 로고    scopus 로고
    • Molecular mechanisms of bacterial resistance to antimicrobial peptides
    • Kraus D, Peschel A. Molecular mechanisms of bacterial resistance to antimicrobial peptides. Curr. Top. Microbiol. Immunol. 306, 231-250 (2006).
    • (2006) Curr. Top. Microbiol. Immunol , vol.306 , pp. 231-250
    • Kraus, D.1    Peschel, A.2
  • 8
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: From natural to novel antibiotics
    • Hancock REW, Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr. Drug Tarqets Infect. Disord. 2(1), 79-83 (2002).
    • (2002) Curr. Drug Tarqets Infect. Disord , vol.2 , Issue.1 , pp. 79-83
    • Hancock, R.E.W.1    Patrzykat, A.2
  • 9
    • 3042781052 scopus 로고    scopus 로고
    • Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology
    • Marshall SH, Arenas G. Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology. Electron. J. Biotechnol. 6(2), 265-272 (2003).
    • (2003) Electron. J. Biotechnol , vol.6 , Issue.2 , pp. 265-272
    • Marshall, S.H.1    Arenas, G.2
  • 10
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: A lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • Gifford JL, Hunter HN, Vogel HJ. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell. Mol. Life Sci. 62(22), 2588-2598 (2005).
    • (2005) Cell. Mol. Life Sci , vol.62 , Issue.22 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 11
    • 26844567701 scopus 로고    scopus 로고
    • Synergistic effect of antibacterial agents human β-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli
    • Chen X, Niyonsaba F, Ushio H et al. Synergistic effect of antibacterial agents human β-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli. J. Dermatol. Sci. 40(2), 123-432 (2005).
    • (2005) J. Dermatol. Sci , vol.40 , Issue.2 , pp. 123-432
    • Chen, X.1    Niyonsaba, F.2    Ushio, H.3
  • 12
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert K, Volkmer-Engert R, Walter T, Hancock REW. High-throughput generation of small antibacterial peptides with improved activity. Nat Biotechnol. 23(8), 1008-1012 (2005).
    • (2005) Nat Biotechnol , vol.23 , Issue.8 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 13
    • 0033863173 scopus 로고    scopus 로고
    • Combinatorial libraries: A tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies
    • Blondelle SE, Lohner K. Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55(1), 74-87 (2000).
    • (2000) Biopolymers , vol.55 , Issue.1 , pp. 74-87
    • Blondelle, S.E.1    Lohner, K.2
  • 14
    • 33748946749 scopus 로고    scopus 로고
    • Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: Comparison with cationic antimicrobial peptides and lipopeptides
    • Straus SK, Hancock REW. Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides. Biochim. Biophys. Acta 1758(9), 1215-1223 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1215-1223
    • Straus, S.K.1    Hancock, R.E.W.2
  • 15
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock REW. Peptide antibiotics. Lancet 349(9049), 418-422 (1997).
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 16
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3(3), 238-250 (2005).
    • (2005) Nat. Rev. Microbiol , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 17
    • 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, Maier E, Benz R, Hancock REW. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38(22), 7235-7242 (1999).
    • (1999) Biochemistry , vol.38 , Issue.22 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 18
    • 0031849949 scopus 로고    scopus 로고
    • Neutron off-plane scattering of aligned membranes. I. Method of measurement
    • Yang L, Harroun TA, Heller WT, Weiss TM, Huang HW. Neutron off-plane scattering of aligned membranes. I. Method of measurement. Biophis. J. 75 (2), 641-645 (1998).
    • (1998) Biophis. J , vol.75 , Issue.2 , pp. 641-645
    • Yang, L.1    Harroun, T.A.2    Heller, W.T.3    Weiss, T.M.4    Huang, H.W.5
  • 19
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki K, Murase O, Fujii N, Miyajima K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35(35), 11361-11368 (1996).
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 20
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit E, Boman A, Boman HG, Shai Y. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34(36), 11479-11488 (1995).
    • (1995) Biochemistry , vol.34 , Issue.36 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 21
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger B, Lohner K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta 1758(9), 1529-1539 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 22
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai Y. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20(11), 460-464 (1995).
    • (1995) Trends Biochem. Sci , vol.20 , Issue.11 , pp. 460-464
    • Shai, Y.1
  • 23
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal concentrations of pleurocidin-derived antimicrobial pepticles inhibit macromolecular synthesis in Escherichia coli
    • Patrzykat A, Friedrich CL, Zhang L, Mendoza V, Hancock REW. Sublethal concentrations of pleurocidin-derived antimicrobial pepticles inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46(3), 605-614 (2002).
    • (2002) Antimicrob. Agents Chemother , vol.46 , Issue.3 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.W.5
  • 24
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect pepticle cecropin A
    • Hong RW, Shchepetov M, Weiser JN, Axelsen PH. Transcriptional profile of the Escherichia coli response to the antimicrobial insect pepticle cecropin A. Antimicrob. Agents Chemother. 47(1), 1-6 (2003).
    • (2003) Antimicrob. Agents Chemother , vol.47 , Issue.1 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 25
    • 0035941062 scopus 로고    scopus 로고
    • The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
    • Haukland HH, Ulvatne H, Sandvik K, Vorland LH. The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett. 508(3), 389-393 (2001).
    • (2001) FEBS Lett , vol.508 , Issue.3 , pp. 389-393
    • Haukland, H.H.1    Ulvatne, H.2    Sandvik, K.3    Vorland, L.H.4
  • 26
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park CB, Kim MS, Kim SC. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 218(1), 408-413 (1996).
    • (1996) Biochem. Biophys. Res. Commun , vol.218 , Issue.1 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 27
    • 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
    • Park CB, Kim HS, Kim SC. 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(1), 253-257 (1998).
    • (1998) Biochem. Biophys Res. Commun , vol.244 , Issue.1 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 28
    • 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
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. 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. USA 97(15), 8245-8250 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.15 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 29
    • 0000220470 scopus 로고
    • Bactericidal action of histone
    • Hirsch JG. Bactericidal action of histone. J. Exp. Med. 108(6), 925-944 (1958).
    • (1958) J. Exp. Med , vol.108 , Issue.6 , pp. 925-944
    • Hirsch, J.G.1
  • 30
    • 0042121501 scopus 로고    scopus 로고
    • Birkemo GA, Luders, T, Andersen O, Nes IF, Nissen-Meyer J. Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut ( Hippoglossus hippoglossus L.). Biochim. Biophys. Acta 1646(1-2), 207-215 (2003).
    • Birkemo GA, Luders, T, Andersen O, Nes IF, Nissen-Meyer J. Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut ( Hippoglossus hippoglossus L.). Biochim. Biophys. Acta 1646(1-2), 207-215 (2003).
  • 31
    • 0032561422 scopus 로고    scopus 로고
    • Parasin I, an antimicrobial peptide derived from histone H2A in the catfish
    • Park IY, Park CB, Kim MS, Kim SC. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437(3), 258-262 (1998).
    • (1998) Parasilurus asotus. FEBS Lett , vol.437 , Issue.3 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 32
    • 23044452974 scopus 로고    scopus 로고
    • Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: Evidence for multiple conformations involved in binding to membranes and DNA
    • Hsu C-H, Chen C, Jou M-L et al. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucl. Acids Res. 33(13), 4053-4064 (2005).
    • (2005) Nucl. Acids Res , vol.33 , Issue.13 , pp. 4053-4064
    • Hsu, C.-H.1    Chen, C.2    Jou, M.-L.3
  • 33
    • 13844322065 scopus 로고    scopus 로고
    • The cathelicidins - structure, function and evolution
    • Tomasinsig L, Zanetti M. The cathelicidins - structure, function and evolution. Curr. Protein Pept. Sci. 6(1), 23-34 (2005).
    • (2005) Curr. Protein Pept. Sci , vol.6 , Issue.1 , pp. 23-34
    • Tomasinsig, L.1    Zanetti, M.2
  • 34
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla TJ, Karunaratne DN, Hancock RE. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271(32), 19298-19303 (1996).
    • (1996) J. Biol. Chem , vol.271 , Issue.32 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.3
  • 35
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshrni C, Sitaram N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160(1), 91-96 (1998).
    • (1998) FEMS Microbiol. Lett , vol.160 , Issue.1 , pp. 91-96
    • Subbalakshrni, C.1    Sitaram, N.2
  • 36
    • 33750971755 scopus 로고    scopus 로고
    • Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites
    • Marchand C, Krajewski K, Lee HF et al. Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites. Nucl. Acids Res. 34(18), 5157-5165 (2006).
    • (2006) Nucl. Acids Res , vol.34 , Issue.18 , pp. 5157-5165
    • Marchand, C.1    Krajewski, K.2    Lee, H.F.3
  • 37
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria
    • Friedrich CL, Rozek A, Patrzykat A, Hancock REW. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria. J. Biol. Chem. 276(26), 24015-24022 (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.26 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.W.4
  • 38
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Ageroerth B, Lee JY, Bergman T et al. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem. 202(3), 849-854 (1991).
    • (1991) Eur. J. Biochem , vol.202 , Issue.3 , pp. 849-854
    • Ageroerth, B.1    Lee, J.Y.2    Bergman, T.3
  • 39
    • 0028585933 scopus 로고
    • Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine
    • Shi J, Ross CR, Chengappa MM, Blecha F. Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine. J. Leukoc. Biol. 56(6), 807-811 (1994).
    • (1994) J. Leukoc. Biol , vol.56 , Issue.6 , pp. 807-811
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Blecha, F.4
  • 40
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61(7), 2978-2984 (1993).
    • (1993) Infect. Immun , vol.61 , Issue.7 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 41
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole AM, Weis P, Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J. Biol. Chem. 272(18), 12008-12013 (1997).
    • (1997) J. Biol. Chem , vol.272 , Issue.18 , pp. 12008-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 42
    • 0034700271 scopus 로고    scopus 로고
    • Otvos L Jr, O I, Rogers ME et al. Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39(46), 14150-14159 (2000).
    • Otvos L Jr, O I, Rogers ME et al. Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39(46), 14150-14159 (2000).
  • 43
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol G, Lovas S, Varadi G et al. The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 40(10), 3016-3026 (2001).
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3
  • 44
    • 0026526445 scopus 로고
    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
    • Salomon RA, Farias RN. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J. Bacteriol. 174(22), 7428-7435 (1992).
    • (1992) J. Bacteriol , vol.174 , Issue.22 , pp. 7428-7435
    • Salomon, R.A.1    Farias, R.N.2
  • 45
    • 16844373436 scopus 로고    scopus 로고
    • Mammalian defensins: Structures and mechanism of antibiotic activity
    • Sahl HG, Pag U, Bonness S et al. Mammalian defensins: structures and mechanism of antibiotic activity. J. Leukoc. Biol. 77(4), 466-475 (2005).
    • (2005) J. Leukoc. Biol , vol.77 , Issue.4 , pp. 466-475
    • Sahl, H.G.1    Pag, U.2    Bonness, S.3
  • 46
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brotz H, Josten M, Wiedemann I et al. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30(2), 317-327 (1998).
    • (1998) Mol. Microbiol , vol.30 , Issue.2 , pp. 317-327
    • Brotz, H.1    Josten, M.2    Wiedemann, I.3
  • 47
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic
    • Breukink E, Wiedemann I, van Kraaij C et al. Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic. Science 286(5448), 2361-2364 (1999).
    • (1999) Science , vol.286 , Issue.5448 , pp. 2361-2364
    • Breukink, E.1    Wiedemann, I.2    van Kraaij, C.3
  • 48
    • 33645474378 scopus 로고    scopus 로고
    • Lipid II as a target for antibiotics
    • Breukink E, de Kruijff B. Lipid II as a target for antibiotics. Nat. Rev. Drug Discov. 5(4), 321-332 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , Issue.4 , pp. 321-332
    • Breukink, E.1    de Kruijff, B.2
  • 49
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: Influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase
    • Bierbaum G, Sahl HG. Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase. J. Bacteriol. 169(12), 5452-5458 (1987).
    • (1987) J. Bacteriol , vol.169 , Issue.12 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 50
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper HE, Kramer NE, Smith JL et al. An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313 (5793), 1636-1637 (2006).
    • (2006) Science , vol.313 , Issue.5793 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3
  • 51
    • 0034887091 scopus 로고    scopus 로고
    • Comparison of the activity spectra against pathogens of bacterial strains producing a mutacin or a lantibiotic
    • Morency H, Mota-Meira M, LaPointe G, Lacroix C, Lavoie MC. Comparison of the activity spectra against pathogens of bacterial strains producing a mutacin or a lantibiotic. Can. J. Microbiol. 47(4), 322-331 (2001).
    • (2001) Can. J. Microbiol , vol.47 , Issue.4 , pp. 322-331
    • Morency, H.1    Mota-Meira, M.2    LaPointe, G.3    Lacroix, C.4    Lavoie, M.C.5
  • 52
    • 0001994881 scopus 로고    scopus 로고
    • Susceptibility testing of antimicrobials in liquid media
    • Lorian V Ed, Williams and Wilkins, MD, USA
    • Amsterdam D. Susceptibility testing of antimicrobials in liquid media. In: Antibiotics in Laboratory Medicine. Lorian V (Ed.). Williams and Wilkins, MD, USA 52-111 (1996).
    • (1996) Antibiotics in Laboratory Medicine , pp. 52-111
    • Amsterdam, D.1
  • 53
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H, Hancock REW. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 45(5), 1558-1560 (2001).
    • (2001) Antimicrob. Agents Chemother , vol.45 , Issue.5 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.W.2
  • 54
    • 33947152401 scopus 로고    scopus 로고
    • The chicken host peptides, gallinacins 4, 7, and 9 have antimicrobial activity against Salmonella serovars
    • Milona P, Townes CL, Bevan RM, Hall J. The chicken host peptides, gallinacins 4, 7, and 9 have antimicrobial activity against Salmonella serovars. Biochem. Biophys. Res. Commun. 356(1), 169-174 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.356 , Issue.1 , pp. 169-174
    • Milona, P.1    Townes, C.L.2    Bevan, R.M.3    Hall, J.4
  • 55
    • 0033003473 scopus 로고    scopus 로고
    • Biological properties of structurally related α-helical cationic antimicrobial peptides
    • Scott MG, Yan H, Hancock REW. Biological properties of structurally related α-helical cationic antimicrobial peptides. Infect. Immun. 67(4), 2005-2009 (1999).
    • (1999) Infect. Immun , vol.67 , Issue.4 , pp. 2005-2009
    • Scott, M.G.1    Yan, H.2    Hancock, R.E.W.3
  • 56
    • 33847398715 scopus 로고    scopus 로고
    • In vitro activities of tachyplesin III against Pseudomonas aeruginosa
    • Cirioni O, Giacometti A, Kamysz W et al. In vitro activities of tachyplesin III against Pseudomonas aeruginosa. Peptides 28(4), 747-751 (2007).
    • (2007) Peptides , vol.28 , Issue.4 , pp. 747-751
    • Cirioni, O.1    Giacometti, A.2    Kamysz, W.3
  • 57
    • 33748693942 scopus 로고    scopus 로고
    • Prior antibacterial peptide-mediated inhibition of protein folding in bacteria mutes resistance enzymes
    • Otvos L Jr, de Olivier Inacio V, Wade JD, Cudic P. Prior antibacterial peptide-mediated inhibition of protein folding in bacteria mutes resistance enzymes. Antimicrob. Agents Chemother. 50(9), 3146-3149 (2006).
    • (2006) Antimicrob. Agents Chemother , vol.50 , Issue.9 , pp. 3146-3149
    • Otvos Jr, L.1    de Olivier Inacio, V.2    Wade, J.D.3    Cudic, P.4
  • 58
    • 30044433704 scopus 로고    scopus 로고
    • Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37
    • Mookherjee N, Brown KL, Bowdish DM et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J. Immunol. 176(4), 2455-2464 (2006).
    • (2006) J. Immunol , vol.176 , Issue.4 , pp. 2455-2464
    • Mookherjee, N.1    Brown, K.L.2    Bowdish, D.M.3
  • 59
    • 0025869402 scopus 로고
    • Role of phospholipase in generating lipid second messengers in signal transduction
    • Dennis EA, Rhee SG, Billah MM, Hannun YA. Role of phospholipase in generating lipid second messengers in signal transduction. FASEB J. 5(7), 2068-2077 (1991).
    • (1991) FASEB J , vol.5 , Issue.7 , pp. 2068-2077
    • Dennis, E.A.1    Rhee, S.G.2    Billah, M.M.3    Hannun, Y.A.4
  • 60
    • 0031596818 scopus 로고    scopus 로고
    • Secretory phospholipase A2 is the principal bactericide for staphylococci and other Gram-positive bacteria in human tears
    • Qu XD, Lehrer RI. Secretory phospholipase A2 is the principal bactericide for staphylococci and other Gram-positive bacteria in human tears. Infect. Immun. 66(6), 2791-2797 (1998).
    • (1998) Infect. Immun , vol.66 , Issue.6 , pp. 2791-2797
    • Qu, X.D.1    Lehrer, R.I.2
  • 61
    • 0037416988 scopus 로고    scopus 로고
    • Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides
    • Zhao H, Kinnunen PK. Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides. Antimicrob. Agents Chemother. 47(3), 965-971 (2003).
    • (2003) Antimicrob. Agents Chemother , vol.47 , Issue.3 , pp. 965-971
    • Zhao, H.1    Kinnunen, P.K.2
  • 62
    • 0034016235 scopus 로고    scopus 로고
    • Antimicrobial peptides protect coho salmon from Vibrio anguillarum infections
    • Jia X, Patrzykat A, Devlin RH et al. Antimicrobial peptides protect coho salmon from Vibrio anguillarum infections. Appl. Environ. Microbiol. 66(5), 1928-1932 (2000).
    • (2000) Appl. Environ. Microbiol , vol.66 , Issue.5 , pp. 1928-1932
    • Jia, X.1    Patrzykat, A.2    Devlin, R.H.3
  • 63
    • 0029867221 scopus 로고    scopus 로고
    • Synthetic combinatorial libraries: Novel discovery strategy for identification of antimicrobial agents
    • Blondelle SE, Perez-Paya E, Houghten RA. Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents. Antimicrob. Agents Chemother. 40(5), 1067-1071 (1996).
    • (1996) Antimicrob. Agents Chemother , vol.40 , Issue.5 , pp. 1067-1071
    • Blondelle, S.E.1    Perez-Paya, E.2    Houghten, R.A.3
  • 64
    • 33750304297 scopus 로고    scopus 로고
    • A linguistic model for the rational design of antimicrobial peptides
    • Loose C, Jensen K, Rigoutsos I, Stephanopoulos G. A linguistic model for the rational design of antimicrobial peptides. Nature 443(7113), 867-869 (2006).
    • (2006) Nature , vol.443 , Issue.7113 , pp. 867-869
    • Loose, C.1    Jensen, K.2    Rigoutsos, I.3    Stephanopoulos, G.4
  • 65
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415(6870), 389-395 (2002).
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 66
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462(1-2), 157-183 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , Issue.1-2 , pp. 157-183
    • Bechinger, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.