메뉴 건너뛰기




Volumn 414, Issue 1, 2008, Pages 143-150

Probing structure-activity relationships in bactericidal peptide βpep-25

Author keywords

Bactericidal; Endotoxin neutralizing; Lipopolysaccharide; Peptide

Indexed keywords

ALKYLATION; AMINO ACIDS; BACTERIA; BACTERIOLOGY; BIOCHEMISTRY; DYES; ESCHERICHIA COLI; HEALTH; HYDROPHOBICITY; ORGANIC ACIDS; ORGANIC POLYMERS; POLYSACCHARIDES;

EID: 49649110753     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20080506     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0346993728 scopus 로고    scopus 로고
    • The future of antibiotics: Bacterial membrane disintegrators
    • Lockwood, N. A. and Mayo, K. H. (2003) The future of antibiotics: bacterial membrane disintegrators. Drug Future 28, 911-923
    • (2003) Drug Future , vol.28 , pp. 911-923
    • Lockwood, N.A.1    Mayo, K.H.2
  • 3
    • 0033754189 scopus 로고    scopus 로고
    • Antibacterial peptides isolated from insects
    • Otvos, Jr. L. (2000) Antibacterial peptides isolated from insects. J. Pept. Sci. 6, 497-511
    • (2000) J. Pept. Sci , vol.6 , pp. 497-511
    • Otvos Jr., L.1
  • 4
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet, P., Hetru, C., Dimarcq, J. L. and Hoffmann, D. (1999) Antimicrobial peptides in insects; structure and function. Dev. Comp. Immunol. 23, 329-344
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 5
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptices from amphibian skin: What do they tell us?
    • Simmaco, M., Mignogna, G. and Barra, D. (1998) Antimicrobial peptices from amphibian skin: what do they tell us? Biopolymers 47, 435-450
    • (1998) Biopolymers , vol.47 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 6
    • 0030861378 scopus 로고    scopus 로고
    • Antimicrobial peptices of phagocytes and epithelia
    • Ganz, T. and Weiss, J. (1997) Antimicrobial peptices of phagocytes and epithelia. Semin. Hematol. 34, 343-354
    • (1997) Semin. Hematol , vol.34 , pp. 343-354
    • Ganz, T.1    Weiss, J.2
  • 7
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz, T. and Lehrer, R. I. (1997) Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4, 53-58
    • (1997) Curr. Opin. Hematol , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 8
    • 0034667551 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides of blood: Templates for novel antimicrobial agents
    • Levy, O. (2000) Antimicrobial proteins and peptides of blood: templates for novel antimicrobial agents. Blood 96, 2664-2672
    • (2000) Blood , vol.96 , pp. 2664-2672
    • Levy, O.1
  • 9
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptice, 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 peptice, 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
  • 10
    • 0021949580 scopus 로고
    • N-terminal analogues of cecropin A: Synthesis, antibacterial activity, and conformational properties
    • Andreu, D., Merrifield, R. B., Steiner, H. and Boman, H. G. (1985) N-terminal analogues of cecropin A: synthesis, antibacterial activity, and conformational properties. Biochemistry 24, 1683-1688
    • (1985) Biochemistry , vol.24 , pp. 1683-1688
    • Andreu, D.1    Merrifield, R.B.2    Steiner, H.3    Boman, H.G.4
  • 11
    • 49649124786 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 12
    • 49649106410 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 13
    • 1542344948 scopus 로고    scopus 로고
    • Acylation of SC4 dodecaptide increases bactericidal potency against Gram-positive bacteria, including drug-resistant strains
    • Lockwood, N. A., Haseman, J, R., Tirrell, M. V. and Mayo, K. H. (2004) Acylation of SC4 dodecaptide increases bactericidal potency against Gram-positive bacteria, including drug-resistant strains. Biochem. J. 378, 93-103
    • (2004) Biochem. J , vol.378 , pp. 93-103
    • Lockwood, N.A.1    Haseman, J.R.2    Tirrell, M.V.3    Mayo, K.H.4
  • 14
    • 0030757152 scopus 로고    scopus 로고
    • Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog
    • Matsuzaki, K., Yoneyama, S., Fujii, N., Miyajima, K., Yamada, K., Kirino, Y. and Anzai, K. (1997) Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog. Biochemistry 36, 9799-9806
    • (1997) Biochemistry , vol.36 , pp. 9799-9806
    • Matsuzaki, K.1    Yoneyama, S.2    Fujii, N.3    Miyajima, K.4    Yamada, K.5    Kirino, Y.6    Anzai, K.7
  • 16
    • 0029900401 scopus 로고    scopus 로고
    • Antiestrogens inhibit endothelial cell growth stimulated by angiogenic growth factors
    • Gagliardi, A. R., Hennig, B. and Collins, D. C. (1996) Antiestrogens inhibit endothelial cell growth stimulated by angiogenic growth factors. Anticancer Res. 16, 1101-1106
    • (1996) Anticancer Res , vol.16 , pp. 1101-1106
    • Gagliardi, A.R.1    Hennig, B.2    Collins, D.C.3
  • 18
    • 33749046904 scopus 로고    scopus 로고
    • Diversity of endotoxin and its impact on pathogenesis
    • Trent, M. S., Stead, C. M., Tran, A. X. and Hankins, J. V. (2006) Diversity of endotoxin and its impact on pathogenesis. J. Endotoxin Res. 12, 205-223
    • (2006) J. Endotoxin Res , vol.12 , pp. 205-223
    • Trent, M.S.1    Stead, C.M.2    Tran, A.X.3    Hankins, J.V.4
  • 19
    • 0028965644 scopus 로고
    • Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin
    • Ulevitch, R. J. and Tobias, P. S. (1995) Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13, 437-457
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 437-457
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 20
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel, A. (2002) How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10, 179-186
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 21
    • 0032538127 scopus 로고    scopus 로고
    • Designed β-sheet-forming peptide 33mers with potent human bactericidal/ permeability increasing protein-like bactericidal and endotoxin neutralizing activities
    • Mayo, K. H., Haseman, J., Ilyina. E. and Gray, B. (1998) Designed β-sheet-forming peptide 33mers with potent human bactericidal/ permeability increasing protein-like bactericidal and endotoxin neutralizing activities. Biochim. Biophys. Acta 1425, 81-92
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 81-92
    • Mayo, K.H.1    Haseman, J.2    Ilyina, E.3    Gray, B.4
  • 22
    • 0029927321 scopus 로고    scopus 로고
    • A recipe for designing water-soluble, β-sheet-forming peptides
    • Mayo, K. H., Ilyina, E. and Park, H. (1996) A recipe for designing water-soluble, β-sheet-forming peptides. Protein Sci. 5, 1301-1315
    • (1996) Protein Sci , vol.5 , pp. 1301-1315
    • Mayo, K.H.1    Ilyina, E.2    Park, H.3
  • 24
    • 0037439824 scopus 로고    scopus 로고
    • The designed angiostatic pepticle anginex synergistically improves chemotherapy and antiangiogenesis therapy with angiostatin
    • Dings, R. P., Yokoyama, Y., Ramakrishnan, S., Griffioen, A. W. and Mayo, K. H. (2003) The designed angiostatic pepticle anginex synergistically improves chemotherapy and antiangiogenesis therapy with angiostatin. Cancer Res. 63, 382-385
    • (2003) Cancer Res , vol.63 , pp. 382-385
    • Dings, R.P.1    Yokoyama, Y.2    Ramakrishnan, S.3    Griffioen, A.W.4    Mayo, K.H.5
  • 25
    • 34250660932 scopus 로고    scopus 로고
    • Scheduling of radiation with angiogenesis inhibitors Anginex and Avastin improves therapeutic outcome via vessel normalization
    • Dings, R. P. Loren, M., Heun, H., McNiel, E., Griffioen, A. W., Mayo, K. H. and Griffin, R. J. (2007) Scheduling of radiation with angiogenesis inhibitors Anginex and Avastin improves therapeutic outcome via vessel normalization. Clin. Cancer Res. 13, 3395-3402
    • (2007) Clin. Cancer Res , vol.13 , pp. 3395-3402
    • Dings, R.P.1    Loren, M.2    Heun, H.3    McNiel, E.4    Griffioen, A.W.5    Mayo, K.H.6    Griffin, R.J.7
  • 26
    • 17844374383 scopus 로고    scopus 로고
    • Anginex synergizes with radiation therapy to inhibit tumor growth by radiosensitizing enclothelial cells
    • Dings, R. P., Williams, B. W., Song, C. W., Griffioen, A. W., Mayo, K. H. and Griffin, R. J. (2005) Anginex synergizes with radiation therapy to inhibit tumor growth by radiosensitizing enclothelial cells. Int. J. Cancer 115, 312-319
    • (2005) Int. J. Cancer , vol.115 , pp. 312-319
    • Dings, R.P.1    Williams, B.W.2    Song, C.W.3    Griffioen, A.W.4    Mayo, K.H.5    Griffin, R.J.6
  • 27
    • 43949118772 scopus 로고    scopus 로고
    • Ovarian tumor growth regression using a combination of vascular targeting agents anginex or topomimetic 0118 and the chemotherapeutic irofulven
    • Dings, R. P. Laar, E. S., Webber, J., Zhang, Y., Griffin, R. J., Waters, S. J., Macdonald, J. R. and Mayo, K. H. (2008) Ovarian tumor growth regression using a combination of vascular targeting agents anginex or topomimetic 0118 and the chemotherapeutic irofulven. Cancer Lett. 265, 270-280
    • (2008) Cancer Lett , vol.265 , pp. 270-280
    • Dings, R.P.1    Laar, E.S.2    Webber, J.3    Zhang, Y.4    Griffin, R.J.5    Waters, S.J.6    Macdonald, J.R.7    Mayo, K.H.8
  • 29
    • 35948946972 scopus 로고    scopus 로고
    • A journey in structure-based drug discovery: From designed pepticles to protein surface topomimetics as antibiotic and antiangiogenic agents
    • Dings, R. P. and Mayo, K. H. (2007) A journey in structure-based drug discovery: from designed pepticles to protein surface topomimetics as antibiotic and antiangiogenic agents. Accounts Chem. Res. 40, 1057-1065
    • (2007) Accounts Chem. Res , vol.40 , pp. 1057-1065
    • Dings, R.P.1    Mayo, K.H.2
  • 30
    • 0017032226 scopus 로고
    • A new antigenic schema and live-cell slide agglutination procedure for the infrasubspecific serologic classification of Pseudomonas aeruginosa
    • Homma, J. Y. (1976) A new antigenic schema and live-cell slide agglutination procedure for the infrasubspecific serologic classification of Pseudomonas aeruginosa. Jpn. J. Exp. Med. 46, 329-336
    • (1976) Jpn. J. Exp. Med , vol.46 , pp. 329-336
    • Homma, J.Y.1
  • 31
    • 0023262829 scopus 로고
    • Endotoxin neutralization with rabbit antisera to Escherichia coli J5 and other Gram-negative bacteria
    • Warren, H. S., Novitsky, T. J., Bucklin, A., Kania, S. A. and Siber, G. R. (1987) Endotoxin neutralization with rabbit antisera to Escherichia coli J5 and other Gram-negative bacteria. Infect. Immun. 55, 1668-1673
    • (1987) Infect. Immun , vol.55 , pp. 1668-1673
    • Warren, H.S.1    Novitsky, T.J.2    Bucklin, A.3    Kania, S.A.4    Siber, G.R.5
  • 32
    • 0020664177 scopus 로고
    • Production of staphylococcal pyrogenic exotoxin type C: Influence of physical and chemical factors
    • Schlievert, P. M. and Blomster, D. A. (1983) Production of staphylococcal pyrogenic exotoxin type C: influence of physical and chemical factors. J. Infect. Dis. 147, 236-242
    • (1983) J. Infect. Dis , vol.147 , pp. 236-242
    • Schlievert, P.M.1    Blomster, D.A.2
  • 33
    • 0034254333 scopus 로고    scopus 로고
    • Structure-function relationships in novel peptide dodecamers with broad-spectrum bactericidal and endotoxin-neutralizing activities
    • Mayo, K. H., Haseman, J., Young, H. C. and Mayo, J. W. (2000) Structure-function relationships in novel peptide dodecamers with broad-spectrum bactericidal and endotoxin-neutralizing activities. Biochem. J. 349, 717-728
    • (2000) Biochem. J , vol.349 , pp. 717-728
    • Mayo, K.H.1    Haseman, J.2    Young, H.C.3    Mayo, J.W.4
  • 34
    • 33846027521 scopus 로고    scopus 로고
    • Topomimetics of amphipathic β-sheet and helix-forming bactericidal pepticles neutralize lipopolysaccharide enclotoxins
    • Chen, X., Dings, R. P., Nesmelova, I., Debbert, S., Haseman, J. R., Maxwell, J., Hoye, T. R. and Mayo, K. H. (2006) Topomimetics of amphipathic β-sheet and helix-forming bactericidal pepticles neutralize lipopolysaccharide enclotoxins. J. Med. Chem. 49, 7754-7765
    • (2006) J. Med. Chem , vol.49 , pp. 7754-7765
    • Chen, X.1    Dings, R.P.2    Nesmelova, I.3    Debbert, S.4    Haseman, J.R.5    Maxwell, J.6    Hoye, T.R.7    Mayo, K.H.8
  • 35
    • 0015365688 scopus 로고
    • An invertebrate coagulation system activated by endotoxin: Evidence for enzymatic mediation
    • Young, N. S., Levin, J. and Prendergast, R. A. (1972) An invertebrate coagulation system activated by endotoxin: evidence for enzymatic mediation. J. Clin. Invest. 51, 1790-1797
    • (1972) J. Clin. Invest , vol.51 , pp. 1790-1797
    • Young, N.S.1    Levin, J.2    Prendergast, R.A.3
  • 36
    • 34247581863 scopus 로고    scopus 로고
    • NMR solution structure of the angiostatic peptice anginex
    • Arroyo, M. M. and Mayo, K. H. (2007) NMR solution structure of the angiostatic peptice anginex. Biochim. Biophys. Acta 1774, 645-651
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 645-651
    • Arroyo, M.M.1    Mayo, K.H.2
  • 38
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic a a helical antimicrobial peptides
    • Giangaspero, A., Sandri, L. and Tossi, A. (2001) Amphipathic a a helical antimicrobial peptides. Eur. J. Biochem. 268, 5589-5600
    • (2001) Eur. J. Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 39
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K. and Welte, W. (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282, 2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 40
    • 0033524028 scopus 로고    scopus 로고
    • Solution structure of polymyxins B and E and effect of binding to lipopolysaccharide: An NMR and molecular modeling study
    • Pristovsek, P. and Kidric, J. (1999) Solution structure of polymyxins B and E and effect of binding to lipopolysaccharide: an NMR and molecular modeling study. J. Med. Chem. 42, 4604-4613
    • (1999) J. Med. Chem , vol.42 , pp. 4604-4613
    • Pristovsek, P.1    Kidric, J.2
  • 41
    • 20444505207 scopus 로고    scopus 로고
    • Structural origin of endotoxin neutralization and antimicrobial activity of a lactoterrin-based peptide
    • Japelj, B., Pristovsek, R, Majerle, A. and Jerala, R. (2005) Structural origin of endotoxin neutralization and antimicrobial activity of a lactoterrin-based peptide. J. Biol. Chem. 280, 16955-16961
    • (2005) J. Biol. Chem , vol.280 , pp. 16955-16961
    • Japelj, B.1    Pristovsek, R.2    Majerle, A.3    Jerala, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.