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Volumn 380, Issue 3, 2004, Pages 859-865

Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli

Author keywords

Amphibian skin; Antimicrobial peptide; Escherichia coli; Fluorescence microscopy; Membrane permeability; Temporin L.

Indexed keywords

CELL MEMBRANES; CELLS; ELECTRON MICROSCOPY; ESCHERICHIA COLI; MECHANICAL PERMEABILITY; POLYPEPTIDES; SKIN;

EID: 3042743487     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031975     Document Type: Article
Times cited : (149)

References (55)
  • 1
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer, R. I. and Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 2
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock, R. E. and Diamond, G. (2000) The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol. 8, 402-410
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 3
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • Rinaldi, A. C. (2002) Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6, 799-804
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature (London) 415, 389-395
    • (2002) Nature (London) , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0142183723 scopus 로고    scopus 로고
    • Ribosomally synthesized peptides with antimicrobial properties: Biosynthesis, structure, function, and applications
    • Papagianni, M. (2003) Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol. Adv. 21, 465-499
    • (2003) Biotechnol. Adv. , vol.21 , pp. 465-499
    • Papagianni, M.1
  • 6
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 7
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: An update review
    • Boman, H. G. (1998) Gene-encoded peptide antibiotics and the concept of innate immunity: an update review. Scand. J. Immunol. 48, 15-25
    • (1998) Scand. J. Immunol. , vol.48 , pp. 15-25
    • Boman, H.G.1
  • 8
    • 0035321067 scopus 로고    scopus 로고
    • The evolution and genetics of innate immunity
    • Kimbrell, D. A. and Beutler, B. (2001) The evolution and genetics of innate immunity. Nat. Rev. Genet. 2, 256-267
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 256-267
    • Kimbrell, D.A.1    Beutler, B.2
  • 9
    • 0033168860 scopus 로고    scopus 로고
    • Antibiotic peptides from higher eukaryotes: Biology and applications
    • Ganz, T. and Lehrer, R. I. (1999) Antibiotic peptides from higher eukaryotes: biology and applications. Mol. Med. Today 5, 292-297
    • (1999) Mol. Med. Today , vol.5 , pp. 292-297
    • Ganz, T.1    Lehrer, R.I.2
  • 10
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E. W. and Scott, M. G. (2000) The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Svi. U.S.A. 97, 8856-8861
    • (2000) Proc. Natl. Acad. Svi. U.S.A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 11
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H. G. (2003) Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254, 197-215
    • (2003) J. Intern. Med. , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 12
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock, R. E. W. (2001) Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1, 156-164
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.W.1
  • 13
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion, and destabilization of phospholipids bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion, and destabilization of phospholipids bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 14
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. (2002) Mode of action of membrane active antimicrobial peptides. Biopolymers 66, 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 15
    • 0003228776 scopus 로고    scopus 로고
    • Structural and charge requirements for antimicrobial peptide insertion into biological and model membranes
    • Menestrina, G., Dalla Serra, M. and Lazarovici, P., eds., Harwood Academic Publishers, New York
    • Zhao, H. X., Rinaldi, A. C., Rufo, A., Bozzi, A., Kinnunen, P. K. J. and Di Giulio, A. (2003) Structural and charge requirements for antimicrobial peptide insertion into biological and model membranes. In Pore-Forming Peptides and Protein Toxins (Menestrina, G., Dalla Serra, M. and Lazarovici, P., eds.), pp. 151-177, Harwood Academic Publishers, New York
    • (2003) Pore-Forming Peptides and Protein Toxins , pp. 151-177
    • Zhao, H.X.1    Rinaldi, A.C.2    Rufo, A.3    Bozzi, A.4    Kinnunen, P.K.J.5    Di Giulio, A.6
  • 16
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren, Z. and Shai, Y. (1998) Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 47, 451-463
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 17
    • 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, C. B., Kim, H. S. and Kim, S. C. (1998) 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, 253-257
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 18
    • 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. and Hancock, R. E. (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38, 7235-7242
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 19
    • 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, C. B., Yi, K. S., Matsuzaki, K., Kim, M. S. and Kim, S. C. (2000) 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, 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
  • 20
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman, H. G., Agerberth, B. and Boman, A. (1993) Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61, 2978-2984
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 21
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins
    • Skerlavaj, B., Romeo, D. and Gennaro, R. (1990) Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins. Infect. Immun. 58, 3724-3730
    • (1990) Infect. Immun. , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 22
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria
    • Friedrich, C. L., Moyles, D., Beveridge, T. J. and Hancock, R. E. (2000) Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria. Antimicrob. Agents Chemother. 44, 2086-2092
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 23
    • 0030437748 scopus 로고    scopus 로고
    • Temporins, novel antimicrobial peptides from the European red frog Rana temporaria
    • Simmaco, M., Mignogna, G., Canofeni, S., Miele, R., Mangoni, M. L. and Barra, D. (1996) Temporins, novel antimicrobial peptides from the European red frog Rana temporaria. Eur. J. Biochem. 242, 788-792
    • (1996) Eur. J. Biochem. , vol.242 , pp. 788-792
    • Simmaco, M.1    Mignogna, G.2    Canofeni, S.3    Miele, R.4    Mangoni, M.L.5    Barra, D.6
  • 24
    • 0001440605 scopus 로고    scopus 로고
    • Temporin antibiotic peptides: A review and derivation of a consensus sequence
    • Wade, D., Silveira, A., Silberring, J., Kuusela, P. and Lankinen, H. (2000) Temporin antibiotic peptides: a review and derivation of a consensus sequence. Protein Pept. Lett. 7, 349-357
    • (2000) Protein Pept. Lett. , vol.7 , pp. 349-357
    • Wade, D.1    Silveira, A.2    Silberring, J.3    Kuusela, P.4    Lankinen, H.5
  • 25
    • 0348116801 scopus 로고    scopus 로고
    • Unambiguous consensus sequences for temporin-like peptides
    • Wade, D. (2002) Unambiguous consensus sequences for temporin-like peptides. Internet J. Chem. 5, 5 http://www.ijc.com:8000/articies/2002v5/94/
    • (2002) Internet J. Chem. , vol.5 , pp. 5
    • Wade, D.1
  • 27
    • 0037007001 scopus 로고    scopus 로고
    • Interactions of the antimicrobial peptides temporins with model biomembranes. Comparison of temporins B and L.
    • Zhao, H., Rinaldi, A. C., Di Giulio, A., Simmaco, M. and Kinnunen, P. K. (2002) Interactions of the antimicrobial peptides temporins with model biomembranes. Comparison of temporins B and L. Biochemistry 41, 4425-4436
    • (2002) Biochemistry , vol.41 , pp. 4425-4436
    • Zhao, H.1    Rinaldi, A.C.2    Di Giulio, A.3    Simmaco, M.4    Kinnunen, P.K.5
  • 28
  • 29
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • Lehrer, R. I., Barton, A. and Ganz, T. (1988) Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. J. Immunol. Methods 108, 153-158
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 30
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla, T. J., Karunaratne, D. N. and Hancock, R. E. (1996) Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271, 19298-19303
    • (1996) J. Biol. Chem. , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.3
  • 31
    • 0031019137 scopus 로고    scopus 로고
    • Protamine-induced permeabilization of cell envelopes of Gram-positive and Gram-negative bacteria
    • Johansen, C., Verheul, A., Gram, L., Gill, T. and Abee, T. (1997) Protamine-induced permeabilization of cell envelopes of Gram-positive and Gram-negative bacteria. Appl. Environ. Microbiol. 63, 1155-1159
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1155-1159
    • Johansen, C.1    Verheul, A.2    Gram, L.3    Gill, T.4    Abee, T.5
  • 32
    • 0034684272 scopus 로고    scopus 로고
    • Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism
    • Ibrahim, H. R., Sugimoto, Y. and Aoki, T. (2000) Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim. Biophys. Acta 1523, 196-205
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 196-205
    • Ibrahim, H.R.1    Sugimoto, Y.2    Aoki, T.3
  • 33
    • 0033696634 scopus 로고    scopus 로고
    • Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions
    • Mangoni, M. L., Grovale, N., Giorgi, A., Mignogna, G., Simmaco, M. and Barra, D. (2000) Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions. Peptides 21, 1673-1679
    • (2000) Peptides , vol.21 , pp. 1673-1679
    • Mangoni, M.L.1    Grovale, N.2    Giorgi, A.3    Mignogna, G.4    Simmaco, M.5    Barra, D.6
  • 34
    • 0033903248 scopus 로고    scopus 로고
    • Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli
    • Pellegrini, A., Thomas, U., Wild, P., Schraner, E. and von Fellenberg, R. (2000) Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli. Microbiol. Res. 155, 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
  • 35
    • 0026642952 scopus 로고
    • Use of a fluorescent redox probe for direct visualization of actively respiring bacteria
    • Rodriguez, G. G., Phipps, D., Ishiguro, K. and Ridgway, H. F. (1992) Use of a fluorescent redox probe for direct visualization of actively respiring bacteria. Appl. Environ. Microbiol. 58, 1801-1808
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1801-1808
    • Rodriguez, G.G.1    Phipps, D.2    Ishiguro, K.3    Ridgway, H.F.4
  • 37
    • 0031261547 scopus 로고    scopus 로고
    • Double staining (CTC-DAPI) for detection and enumeration of viable but non-culturable Campylobacter jejuni cells
    • Cappelier, J. M., Lazaro, B., Rossero, A., Fernandez-Astorga, A. and Federighi, M. (1997) Double staining (CTC-DAPI) for detection and enumeration of viable but non-culturable Campylobacter jejuni cells. Vet. Res. 28, 547-555
    • (1997) Vet. Res. , vol.28 , pp. 547-555
    • Cappelier, J.M.1    Lazaro, B.2    Rossero, A.3    Fernandez-Astorga, A.4    Federighi, M.5
  • 38
    • 0014478053 scopus 로고
    • Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics
    • Normark, S., Boman, H. G. and Matsson, E. (1969) Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics. J. Bacteriol. 97, 1334-1342
    • (1969) J. Bacteriol. , vol.97 , pp. 1334-1342
    • Normark, S.1    Boman, H.G.2    Matsson, E.3
  • 39
    • 0002927343 scopus 로고    scopus 로고
    • The interaction of antimicrobial peptides with model lipid bilayer and biological membranes
    • McElhaney, R. N. and Prenner, E. J. (eds.) (1999) The interaction of antimicrobial peptides with model lipid bilayer and biological membranes. Biochim. Biophys. Acta 1462, 1-234
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-234
    • McElhaney, R.N.1    Prenner, E.J.2
  • 40
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock, R. E. W. and Rozek, A. (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206, 143-149
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 41
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • Zhao, H. and Kinnunen, P. K. (2002) Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 277, 25170-25177
    • (2002) J. Biol. Chem. , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.2
  • 42
    • 0021764030 scopus 로고
    • Mode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae
    • Okada, M. and Natori, S. (1984) Mode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae. Biochem. J. 222, 119-124
    • (1984) Biochem. J. , vol.222 , pp. 119-124
    • Okada, M.1    Natori, S.2
  • 43
    • 0028800158 scopus 로고
    • The morphological effects of two antimicrobial peptides, hecate-1 and melittin, on Escherichia coli
    • Henk, W. G., Todd, W. J., Enright, F. M. and Mitchell, P. S. (1995) The morphological effects of two antimicrobial peptides, hecate-1 and melittin, on Escherichia coli. Scanning Microsc. 9, 501-507
    • (1995) Scanning Microsc. , vol.9 , pp. 501-507
    • Henk, W.G.1    Todd, W.J.2    Enright, F.M.3    Mitchell, P.S.4
  • 44
    • 0032504531 scopus 로고    scopus 로고
    • Wide-spectrum antibiotic activity of synthetic, amphipathic peptides
    • Tiozzo, E., Rocco, G., Tossi, A. and Romeo, D. (1998) Wide-spectrum antibiotic activity of synthetic, amphipathic peptides. Biochem. Biophys. Res. Commun. 249, 202-206
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 202-206
    • Tiozzo, E.1    Rocco, G.2    Tossi, A.3    Romeo, D.4
  • 45
    • 0033433992 scopus 로고    scopus 로고
    • SMAP-29: A potent antibacterial and antifungal peptide from sheep leukocytes
    • Skerlavaj, B., Benincasa, M., Risso, A., Zanetti, M. and Gennaro, R. (1999) SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett. 463, 58-62
    • (1999) FEBS Lett. , vol.463 , pp. 58-62
    • Skerlavaj, B.1    Benincasa, M.2    Risso, A.3    Zanetti, M.4    Gennaro, R.5
  • 46
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki, K., Sugishita, K., Harada, M., Fujii, N. and Miyajima, K. (1997) Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327, 119-130
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 47
    • 0031005930 scopus 로고    scopus 로고
    • A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity
    • Oren, Z., Hong, J. and Shai, Y. (1997) A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J. Biol. Chem. 272, 14643-14649
    • (1997) J. Biol. Chem. , vol.272 , pp. 14643-14649
    • Oren, Z.1    Hong, J.2    Shai, Y.3
  • 48
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B. and Shai, Y. (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341, 501-513
    • (1999) Biochem. J. , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 49
    • 0029665072 scopus 로고    scopus 로고
    • Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides
    • Shai, Y. and Oren, Z. (1996) Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides. J. Biol. Chem. 271, 7305-7308
    • (1996) J. Biol. Chem. , vol.271 , pp. 7305-7308
    • Shai, Y.1    Oren, Z.2
  • 50
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers
    • Papo, N., Oren, Z., Pag, U., Sahl, H. G. and Shai, Y. (2002) The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 277, 33913-33921
    • (2002) J. Biol. Chem. , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 51
    • 0037016020 scopus 로고    scopus 로고
    • Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7
    • Sadler, K., Eom, K. D., Yang, J. L., Dimitrova, Y. and Tam, J. P. (2002) Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7. Biochemistry 41, 14150-14157
    • (2002) Biochemistry , vol.41 , pp. 14150-14157
    • Sadler, K.1    Eom, K.D.2    Yang, J.L.3    Dimitrova, Y.4    Tam, J.P.5
  • 52
    • 0025058306 scopus 로고
    • Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera)
    • Casteels, P., Ampe, C., Riviere, L., Van Damme, J., Elicone, C., Fleming, M., Jacobs, F. and Tempst, P. (1990) Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Eur. J. Biochem. 187, 381-386
    • (1990) Eur. J. Biochem. , vol.187 , pp. 381-386
    • Casteels, P.1    Ampe, C.2    Riviere, L.3    Van Damme, J.4    Elicone, C.5    Fleming, M.6    Jacobs, F.7    Tempst, P.8
  • 53
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity
    • Casteels, P. and Tempst, P. (1994) Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem. Biophys. Res. Commun. 199, 339-345
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 54
    • 0030032395 scopus 로고    scopus 로고
    • Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide
    • Shi, J., Ross, C. R., Chengappa, M. M., Sylte, M. J., McVey, D. S. and Blecha, F. (1996) Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Antimicrob. Agents Chemother. 40, 115-121
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 115-121
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Sylte, M.J.4    McVey, D.S.5    Blecha, F.6
  • 55
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi, C. and Sitaram, N. (1998) Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160, 91-96
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2


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