메뉴 건너뛰기




Volumn 54, Issue 5, 2010, Pages 1693-1699

Synergy with rifampin and kanamycin enhances potency, kill kinetics, and selectivity of de novo-designed antimicrobial peptides

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; ALPHA,BETA DIDEHYDROPHENYLALANINE; DELTA FM PROTEIN; DELTA FMSCR PROTEIN; DELTA FQ PROTEIN; DENDRIMER; KANAMYCIN; LYSINE; PHENYLALANINE DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; RIFAMPICIN; UD PROTEIN; UNCLASSIFIED DRUG;

EID: 77951251397     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01231-09     Document Type: Article
Times cited : (69)

References (32)
  • 1
    • 33746807690 scopus 로고    scopus 로고
    • Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells
    • Ahmad, A., S. P. Yadav, N. Asthana, K. Mitra, S. P. Srivastava, and J. K. Ghosh. 2006. Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells. J. Biol. Chem. 281:22029-22038.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22029-22038
    • Ahmad, A.1    Yadav, S.P.2    Asthana, N.3    Mitra, K.4    Srivastava, S.P.5    Ghosh, J.K.6
  • 2
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin
    • Asthana, N., S. P. Yadav, and J. K. Ghosh. 2004. Dissection of antibacterial and toxic activity of melittin. J. Biol. Chem. 279:55042-55050.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 3
    • 0026757575 scopus 로고
    • Bacterial resistance to beta-lactams and its prevention with combination antimicrobial therapy
    • Barriere, S. L. 1992. Bacterial resistance to beta-lactams and its prevention with combination antimicrobial therapy. Pharmacotherapy 12:397-402.
    • (1992) Pharmacotherapy , vol.12 , pp. 397-402
    • Barriere, S.L.1
  • 4
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet, P., R. Stocklin, and L. Menin. 2004. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198:169-184.
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 7
    • 0037226091 scopus 로고    scopus 로고
    • Vancomycin acts synergistically with gentamicin against penicillin-resistant pneumococci by increasing the intracellular penetration of gentamicin
    • Cottagnoud, P., M. Cottagnoud, and M. G. Täuber. 2003. Vancomycin acts synergistically with gentamicin against penicillin-resistant pneumococci by increasing the intracellular penetration of gentamicin. Antimicrob. Agents Chemother. 47:144-147.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 144-147
    • Cottagnoud, P.1    Cottagnoud, M.2    Täuber, M.G.3
  • 9
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and hemolytic activity of amphipathic helical peptides
    • Dathe, M., T. Wieprecht, H. Nikolenko, L. Handel, W. L. Maloy, D. L. MacDonald, D. L. Beyermann, and M. Bienert. 1997. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and hemolytic activity of amphipathic helical peptides. FEBS Lett. 403:208-212.
    • (1997) FEBS Lett. , vol.403 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    MacDonald, D.L.6    Beyermann, D.L.7    Bienert, M.8
  • 10
    • 67649199172 scopus 로고    scopus 로고
    • Antimicrobial action of prototypic amphipathic cationic decapeptides and their branched dimers
    • Dewan, P. C., A. Anantharaman, V. S. Chauhan, and D. Sahal. 2009. Antimicrobial action of prototypic amphipathic cationic decapeptides and their branched dimers. Biochemistry 48:5642-5657.
    • (2009) Biochemistry , vol.48 , pp. 5642-5657
    • Dewan, P.C.1    Anantharaman, A.2    Chauhan, V.S.3    Sahal, D.4
  • 11
    • 33846618655 scopus 로고    scopus 로고
    • Activities of antimicrobial peptides and synergy with enrofloxacin against Mycoplasma pulmonis
    • Fehri, L. F., H. Wróblewski, and A. Blanchard. 2007. Activities of antimicrobial peptides and synergy with enrofloxacin against Mycoplasma pulmonis. Antimicrob. Agent Chemother. 51:468-474.
    • (2007) Antimicrob. Agent Chemother. , vol.51 , pp. 468-474
    • Fehri, L.F.1    Wróblewski, H.2    Blanchard, A.3
  • 12
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides. A systematic study of the effects of structural and physical properties on biological activity
    • Giangaspero, A., L. Sandri, and A. Tossi. 2001. Amphipathic alpha helical antimicrobial peptides. A systematic study of the effects of structural and physical properties on biological activity. Eur. J. Biochem. 268:5589-5600.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 13
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale, J. D. F., and R. E. W. Hancock. 2007. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 5:951-959.
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.F.1    Hancock, R.E.W.2
  • 15
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. W., and H. Sahl. 2006. Antimicrobial and host defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24: 1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.2
  • 16
    • 0029849456 scopus 로고    scopus 로고
    • Synthetic melittin, its enantio, retro, and retroenantio isomers, and selected chimeric analogs: Their antibacterial, hemolytic, and lipid bilayer action
    • Juvvadi, P., S. Vunnam, and R. B. Merrifield. 1996. Synthetic melittin, its enantio, retro, and retroenantio isomers, and selected chimeric analogs: their antibacterial, hemolytic, and lipid bilayer action. J. Am. Chem. Soc. 118: 8989-8997.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8989-8997
    • Juvvadi, P.1    Vunnam, S.2    Merrifield, R.B.3
  • 17
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E., R. L. Colescott, C. D. Bossinger, and P. I. Cook. 1970. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 34:595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 18
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewskii, L. H., M. J. Niaraki, S. W. Farmer, B. Lix, C. M. Kay, B. D. Sykes, R. E. W. Hancock, and R. S. Hodges. 1999. Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity. J. Biol. Chem. 274:13181-13192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondejewskii, L.H.1    Niaraki, M.J.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.W.7    Hodges, R.S.8
  • 21
    • 3542993844 scopus 로고    scopus 로고
    • Antibacterial synergism of novel antibiotic peptides with chloramphenicol
    • Park, Y., H. J. Kim, and K. Hahm. 2004. Antibacterial synergism of novel antibiotic peptides with chloramphenicol. Biochem. Biophys. Res. Commun. 321:109-115.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 109-115
    • Park, Y.1    Kim, H.J.2    Hahm, K.3
  • 22
    • 33750604952 scopus 로고    scopus 로고
    • Crystal structure, conformation and absolute configuration of kanamycin a
    • Puius, Y. A., T. H. Stievater, and T. Srikrishnan. 2006. Crystal structure, conformation and absolute configuration of kanamycin A. Carbohydr. Res. 341:2871-2875.
    • (2006) Carbohydr. Res. , vol.341 , pp. 2871-2875
    • Puius, Y.A.1    Stievater, T.H.2    Srikrishnan, T.3
  • 24
    • 0035970001 scopus 로고    scopus 로고
    • De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: Compaction mediated by weak interactions
    • Ramagopal, U. A., S. Ramakumar, D. Sahal, and V. S. Chauhan. 2001. De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: compaction mediated by weak interactions. Proc. Natl. Acad. Sci. U. S. A. 98:870-874.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 870-874
    • Ramagopal, U.A.1    Ramakumar, S.2    Sahal, D.3    Chauhan, V.S.4
  • 25
    • 1642389369 scopus 로고    scopus 로고
    • Daptomycin synergy with rifampicin and ampicillin against vancomycin-resistant enterococci
    • Rand, K. H., and H. J. Houck. 2004. Daptomycin synergy with rifampicin and ampicillin against vancomycin-resistant enterococci. J. Antimicrob. Chemother. 53:530-532.
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 530-532
    • Rand, K.H.1    Houck, H.J.2
  • 27
    • 0037240729 scopus 로고    scopus 로고
    • Dead bugs don't mutate: Susceptibility issues in the emergence of bacterial resistance
    • Stratton, C. W. 2003. Dead bugs don't mutate: susceptibility issues in the emergence of bacterial resistance. Emerg. Infect. Dis. 9:10-16.
    • (2003) Emerg. Infect. Dis. , vol.9 , pp. 10-16
    • Stratton, C.W.1
  • 29
    • 0032860408 scopus 로고    scopus 로고
    • Ability of azlocillin and tobramycin in combination to delay or prevent resistance development in Pseudomonas aeruginosa
    • Wu, Y. L., E. M. Scott, A. L. W. Po, and V. N. Tariq. 1999. Ability of azlocillin and tobramycin in combination to delay or prevent resistance development in Pseudomonas aeruginosa. J. Antimicrob. Chemother. 44:389-392.
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 389-392
    • Wu, Y.L.1    Scott, E.M.2    Po, A.L.W.3    Tariq, V.N.4
  • 30
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan, H., and R. E. W. Hancock. 2001. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 45:1558-1560.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.W.2
  • 31
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R., and N. Y. Yount. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55:27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 32
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.