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Volumn 5, Issue 1, 1999, Pages 32-45

Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity

Author keywords

Antibacterial; Lactoferricin; QSAR; Sequence modification

Indexed keywords

LACTOFERRIN;

EID: 0032924742     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199901)5:1<32::AID-PSC172>3.0.CO;2-9     Document Type: Article
Times cited : (77)

References (47)
  • 1
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics Dermaseptins have overlapping structural features but target specific microorganisms
    • A. Mor, K. Hani and P. Nicolas (1994). The vertebrate peptide antibiotics Dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269, 31635-31641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 2
    • 0029971979 scopus 로고    scopus 로고
    • Peptide antibiotics: Holy or heretic grails of innate immunity? Scand
    • H.G. Boman (1996). Peptide antibiotics: holy or heretic grails of innate immunity? Scand. J. Immunol. 43, 475-482.
    • (1996) J. Immunol. , vol.43 , pp. 475-482
    • Boman, H.G.1
  • 4
    • 0028829183 scopus 로고
    • Peptides an weapons against microorganisms in the chemical defence system of vertebrates
    • P. Nicolas and A. Mor (1995). Peptides an weapons against microorganisms in the chemical defence system of vertebrates. Annu. Rev. Microbiol. 49, 277-304.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 5
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrate antibiotics
    • R.I. Lehrer and T. Ganz (1996). Endogenous vertebrate antibiotics. Ann. N. Y. Acad. Sci. 797, 228-239.
    • (1996) Ann. N. Y. Acad. Sci. , vol.797 , pp. 228-239
    • Lehrer, R.I.1    Ganz, T.2
  • 7
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: Their function, structure, biogenesis, and mechanism of action
    • J. Nissen-Meyer and LF. Nes (1997). Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch. Microbiol. 167, 67-77.
    • (1997) Arch. Microbiol. , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, L.F.2
  • 8
    • 2442741801 scopus 로고
    • H.G. Boman, J. Marsh and J.A. Goode, Eds, Wiley, New York
    • H.-G. Sahl in: Gene-Encoded Antibiotics Made in Bacteria, H.G. Boman, J. Marsh and J.A. Goode, Eds, p. 27-53. Wiley, New York, 1994.
    • (1994) Gene-Encoded Antibiotics Made in Bacteria , pp. 27-53
    • Sahl, H.-G.1
  • 10
    • 0027197728 scopus 로고
    • Purification and characterization of a scorpion defensin, a 4 kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins
    • S. Cociancich, M. Goyffon, F. Bontems, P. Bulet, F. Bouet, A. Menez and J. Hoffmann (1993). Purification and characterization of a scorpion defensin, a 4 kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins. Biochem. Biophys. Res. Commun. 194, 17-22.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 17-22
    • Cociancich, S.1    Goyffon, M.2    Bontems, F.3    Bulet, P.4    Bouet, F.5    Menez, A.6    Hoffmann, J.7
  • 11
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • M. Zasloff (1987). Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 12
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • R.I. Lehrer, A.K. Lichtenstein and T. Ganz (1993). Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 15
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • K. He, S.J. Ludtke, W.T. Heller and H.W. Huang (1996). Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71, 2669-2679.
    • (1996) Biophys. J. , vol.71 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 17
    • 0027232811 scopus 로고
    • Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
    • W. Bellamy, H. Wakabayashi, M. Takase, K. Kawase, S. Shimamura and M. Tomita (1993). Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol. 182, 97-105.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 97-105
    • Bellamy, W.1    Wakabayashi, H.2    Takase, M.3    Kawase, K.4    Shimamura, S.5    Tomita, M.6
  • 20
    • 0023644485 scopus 로고
    • Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrine (flesh fly)
    • Y. Nakajima, X.-M. Qu and S. Natori (1987). Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrine (flesh fly). J. Biol. Chem. 262, 1665-1669.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1665-1669
    • Nakajima, Y.1    Qu, X.-M.2    Natori, S.3
  • 21
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds Incorporated into planar lipid membranes
    • B. Christensen, J. Fink, R.B. Merrifield and D. Mauzerall (1988). Channel-forming properties of cecropins and related model compounds Incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA 85, 5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 22
    • 0026731832 scopus 로고
    • Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
    • M. Jackson, H.H. Mantsch and J.H. Spencer (1992). Conformation of magainin-2 and related peptides In aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy. Biochemistry 31, 7289-7293.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 24
    • 0026293901 scopus 로고
    • Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin
    • M. Tomita, W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi and K. Kwase (1991). Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J. Dairy Sci. 74, 4137-4142.
    • (1991) J. Dairy Sci. , vol.74 , pp. 4137-4142
    • Tomita, M.1    Bellamy, W.2    Takase, M.3    Yamauchi, K.4    Wakabayashi, H.5    Kwase, K.6
  • 26
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-termlnal region of bovine lactoferrin
    • W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase and M. Tomita (1992). Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-termlnal region of bovine lactoferrin. J. Appl. Bacteriol. 73, 472-479.
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 27
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • K. Yamauchi, M. Tomita, T.J. Giehl and R.T. Ellison (1993). Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61, 719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 28
    • 0023664683 scopus 로고
    • Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions
    • B.T. Pentecost and C.T. Teng (1987). Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions. J. Biol. Chem. 262, 10 134-10 139.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10134-10139
    • Pentecost, B.T.1    Teng, C.T.2
  • 29
    • 0028110849 scopus 로고
    • Characterization of the goat lactoferrin cDNA: Assignment of the relevant locus to bovine U12 synteny group
    • F.L. Provost, M. Nocart, G. Guerin and P. Martin (1994). Characterization of the goat lactoferrin cDNA: assignment of the relevant locus to bovine U12 synteny group. Biochem. Biophys. Res. Commun. 203, 1324-1332.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1324-1332
    • Provost, F.L.1    Nocart, M.2    Guerin, G.3    Martin, P.4
  • 32
    • 0028813886 scopus 로고
    • Structure of human diferric lactoferrin refined at 2.2 Å resolution
    • M. Haridas, B.F. Anderson and E.N. Baker (1995). Structure of human diferric lactoferrin refined at 2.2 Å resolution. Acta Cryst. D51, 629-646.
    • (1995) Acta Cryst. , vol.D51 , pp. 629-646
    • Haridas, M.1    Anderson, B.F.2    Baker, E.N.3
  • 33
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • B.F. Anderson, H.M. Baker, G.E. Norris, D.W. Rice and E.N. Baker (1989). Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209, 711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 34
    • 0027236660 scopus 로고
    • Structure of recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution
    • C.L. Day, B.F. Anderson, J.W. Tweedie and E.N. Baker (1993). Structure of recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution. J. Mol. Biol. 232, 1084-1100.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1084-1100
    • Day, C.L.1    Anderson, B.F.2    Tweedie, J.W.3    Baker, E.N.4
  • 35
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of difeeric bovine lactroferrin at 2.8 Å resolution
    • S.A. Moore, B.F. Anderson, C.R. Groom, M. Haridas and E.N. Baker (1997). Three-dimensional structure of difeeric bovine lactroferrin at 2.8 Å resolution. J. Mol. Biol. 274, 222-236.
    • (1997) J. Mol. Biol. , vol.274 , pp. 222-236
    • Moore, S.A.1    Anderson, B.F.2    Groom, C.R.3    Haridas, M.4    Baker, E.N.5
  • 37
    • 0023735907 scopus 로고
    • Synthetic magainin analogoues with improved antimicrobial activity
    • H.C. Chen, J.H. Brown, J.L. Morell and C.M. Huang (1988). Synthetic magainin analogoues with improved antimicrobial activity. FEBS Lett. 236, 462-466.
    • (1988) FEBS Lett. , vol.236 , pp. 462-466
    • Chen, H.C.1    Brown, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 38
    • 0022993071 scopus 로고
    • Relationship between antimicrobial activity and amphiphilic property of basic model peptides
    • S. Lee, H. Mihara, H. Aoyagi, T. Kato, N. Izumiya and N. Yamasaki (1986). Relationship between antimicrobial activity and amphiphilic property of basic model peptides. Biochim. Biophys. Acta 862, 211-219.
    • (1986) Biochim. Biophys. Acta , vol.862 , pp. 211-219
    • Lee, S.1    Mihara, H.2    Aoyagi, H.3    Kato, T.4    Izumiya, N.5    Yamasaki, N.6
  • 39
    • 0027043261 scopus 로고
    • Design of model amphipatic peptides having potent antimicrobial activities
    • A.E. Blondelle and R.A. Houghten (1992). Design of model amphipatic peptides having potent antimicrobial activities. Biochemistry 31, 12 688-12 694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, A.E.1    Houghten, R.A.2
  • 40
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • J.H. Kang, M.K. Lee, K.L. Kim and K.-S. Hahm (1996). Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Peptide Protein Res. 48, 357-363.
    • (1996) Int. J. Peptide Protein Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 41
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • M. Schiffer and A.B. Edmundson (1967). Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J. 7, 121-135.
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2
  • 42
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • J.D. Lear, Z.R. Wasserman and W.F. DeGrado (1988). Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 44
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • D. Eisenberg, E. Schwarz, M. Komaromy and R. Wall (1984). Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 45
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophatic character of a protein
    • J. Kyte and R.F. Doolittle (1982). A simple method for displaying the hydrophatic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 46
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins
    • J. Garnier, D.J. Osguthorpe and B. Robson (1978). Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 47
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • P.Y. Chou and G.D. Fasman (1974). Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2


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