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Volumn 1758, Issue 9, 2006, Pages 1387-1392

Antimicrobial activity of an abiotic host defense peptide mimic

Author keywords

Antibiotic resistant; Antimicrobial; Foldamer; Magainin; Phenylene ethynylene

Indexed keywords

AMPHOTERICIN; CIPROFLOXACIN; FLUCONAZOLE; LINEZOLID; METICILLIN; NORFLOXACIN; PEXIGANAN ACETATE; PHENYLENE ETHYNYLENE; POLYPEPTIDE ANTIBIOTIC AGENT; QUINOLINE DERIVED ANTIINFECTIVE AGENT; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 33748929145     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.03.001     Document Type: Article
Times cited : (106)

References (34)
  • 1
    • 0028267688 scopus 로고
    • Multiple-antibiotic-resistant pathogenic bacteria-A report on the Rockefeller University Workshop
    • Tomasz A. Multiple-antibiotic-resistant pathogenic bacteria-A report on the Rockefeller University Workshop. New Engl. J. Med. 330 (1994) 1247-1251
    • (1994) New Engl. J. Med. , vol.330 , pp. 1247-1251
    • Tomasz, A.1
  • 2
    • 0034058528 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococcal infections
    • Murray B.E. Vancomycin-resistant enterococcal infections. New Engl. J. Med. 342 (2000) 710-721
    • (2000) New Engl. J. Med. , vol.342 , pp. 710-721
    • Murray, B.E.1
  • 3
    • 0042524191 scopus 로고    scopus 로고
    • Evolution of sporadic isolates of methicillin-resistant staphylococcus aureus (MRSA) in hospitals and their similarities to isolates of community-acquired MRSA
    • Sousa M.A.d., and Lencastre H.d. Evolution of sporadic isolates of methicillin-resistant staphylococcus aureus (MRSA) in hospitals and their similarities to isolates of community-acquired MRSA. J. Clin. Microbiol. 41 (2003) 3806-3815
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 3806-3815
    • Sousa, M.A.d.1    Lencastre, H.d.2
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman H.G. Innate immunity and the normal microflora. Immunol. Rev. 173 (2000) 5-16
    • (2000) Immunol. Rev. , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 6
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16 (1998) 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 7
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 8
    • 0037539998 scopus 로고    scopus 로고
    • Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S
    • Lee D.L., and Hodges R.S. Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S. Biopolymers 2003 (2003) 28-48
    • (2003) Biopolymers , vol.2003 , pp. 28-48
    • Lee, D.L.1    Hodges, R.S.2
  • 9
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipatic helical peptides
    • Dathe M., Wieprecht T., Nikolenko H., Handel L., Maloy W.L., MacDonald D.L., Beyermann M., and Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipatic helical peptides. FEBS Letters 403 (1997) 208-212
    • (1997) FEBS Letters , 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, M.7    Bienert, M.8
  • 10
    • 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
    • Zasloff M. 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. U. S. A. 84 (1987) 5449-5453
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 11
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E.W., Vasil M.L., and Hodges R.S. Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 280 (2005) 12316-12329
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 12
    • 2442475526 scopus 로고    scopus 로고
    • Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5
    • Won H.-S., Jung S.-J., Kim H.E., Seo M.-D., and Lee B.-J. Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5. J. Biol. Chem. 279 (2004) 14784-14791
    • (2004) J. Biol. Chem. , vol.279 , pp. 14784-14791
    • Won, H.-S.1    Jung, S.-J.2    Kim, H.E.3    Seo, M.-D.4    Lee, B.-J.5
  • 13
    • 0033616105 scopus 로고    scopus 로고
    • De novo design of antibacterial beta-peptides
    • Hamuro Y., Schneider J.P., and DeGrado W.F. De novo design of antibacterial beta-peptides. J. Am. Chem. Soc. 121 (1999) 12200-12201
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12200-12201
    • Hamuro, Y.1    Schneider, J.P.2    DeGrado, W.F.3
  • 15
    • 0034802565 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of antimicrobial β-peptides
    • Liu D., and DeGrado W.F. De novo design, synthesis, and characterization of antimicrobial β-peptides. J. Am. Chem. Soc. 123 (2001) 7553-7559
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7553-7559
    • Liu, D.1    DeGrado, W.F.2
  • 16
    • 3242701305 scopus 로고    scopus 로고
    • Antimicrobial 14-Helical β-peptides: potent bilayer disrupting agents
    • Epand R.F., Raguse T.L., Gellman S.H., and Epand R.M. Antimicrobial 14-Helical β-peptides: potent bilayer disrupting agents. Biochemistry 43 (2004) 9527-9535
    • (2004) Biochemistry , vol.43 , pp. 9527-9535
    • Epand, R.F.1    Raguse, T.L.2    Gellman, S.H.3    Epand, R.M.4
  • 17
    • 0141888597 scopus 로고    scopus 로고
    • Helical peptoid mimics of magainin-2 amide
    • Patch J.A., and Barron A.E. Helical peptoid mimics of magainin-2 amide. J. Am. Chem. Soc. 125 (2003) 12092-12093
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12092-12093
    • Patch, J.A.1    Barron, A.E.2
  • 20
    • 17444429937 scopus 로고    scopus 로고
    • Synthesis of urea oligomers and their antibacterial activity
    • Tang H., Doerksen R.J., and Tew G.N. Synthesis of urea oligomers and their antibacterial activity. Chem. Commun. (2005) 1537-1539
    • (2005) Chem. Commun. , pp. 1537-1539
    • Tang, H.1    Doerksen, R.J.2    Tew, G.N.3
  • 21
    • 16244400792 scopus 로고    scopus 로고
    • Amphiphilic polymethacrylate derivatives as antimicrobial agents
    • Kuroda K., and DeGrado W.F. Amphiphilic polymethacrylate derivatives as antimicrobial agents. J. Am. Chem. Soc. 127 (2005) 4128-4129
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4128-4129
    • Kuroda, K.1    DeGrado, W.F.2
  • 22
    • 10044226415 scopus 로고    scopus 로고
    • Tuning the hemolytic and antibacterial activities of amphiphilic polynorbornene derivatives
    • Ilker M.F., Nusslein K., Tew G.N., and Coughlin E.B. Tuning the hemolytic and antibacterial activities of amphiphilic polynorbornene derivatives. J. Am. Chem. Soc. 126 (2004) 15870-15875
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15870-15875
    • Ilker, M.F.1    Nusslein, K.2    Tew, G.N.3    Coughlin, E.B.4
  • 23
    • 1342290264 scopus 로고    scopus 로고
    • Biocidal activity of polystyrenes that are cationic by virtue of protonation
    • Gelman M.A., Weisblum B., Lynn D.M., and Gellman S.H. Biocidal activity of polystyrenes that are cationic by virtue of protonation. Org. Lett. 6 (2004) 557-560
    • (2004) Org. Lett. , vol.6 , pp. 557-560
    • Gelman, M.A.1    Weisblum, B.2    Lynn, D.M.3    Gellman, S.H.4
  • 24
    • 0037014693 scopus 로고    scopus 로고
    • New Poly(phenyleneethynylene)s with cationic, facially amphiphilic structures
    • Arnt L., and Tew G.N. New Poly(phenyleneethynylene)s with cationic, facially amphiphilic structures. J. Am. Chem. Soc. 124 (2002) 7664-7665
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7664-7665
    • Arnt, L.1    Tew, G.N.2
  • 25
    • 0037453623 scopus 로고    scopus 로고
    • Facially amphiphilic Poly(phenyleneethynylene)s studied at the air-water interface
    • Arnt L., and Tew G.N. Facially amphiphilic Poly(phenyleneethynylene)s studied at the air-water interface. Langmuir 19 (2003) 2404-2408
    • (2003) Langmuir , vol.19 , pp. 2404-2408
    • Arnt, L.1    Tew, G.N.2
  • 26
    • 4043081291 scopus 로고    scopus 로고
    • Nonhemolytic abiogenic polymers as antimicrobial peptide mimics
    • Arnt L., Nusslein K., and Tew G.N. Nonhemolytic abiogenic polymers as antimicrobial peptide mimics. J. Polym. Sci., Polym. Chem. 42 (2004) 3860-3864
    • (2004) J. Polym. Sci., Polym. Chem. , vol.42 , pp. 3860-3864
    • Arnt, L.1    Nusslein, K.2    Tew, G.N.3
  • 27
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host-defense peptides
    • Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host-defense peptides. Biopolymers 37 (1995) 105-122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 28
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers
    • Mecke A., Lee D.K., Ramamoorthy A., Orr B.G., and Holl M.M.B. Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers. Biophys. J. 89 (2005) 4043-4050
    • (2005) Biophys. J. , vol.89 , pp. 4043-4050
    • Mecke, A.1    Lee, D.K.2    Ramamoorthy, A.3    Orr, B.G.4    Holl, M.M.B.5
  • 29
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock K.J., Lee D.K., and Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84 (2003) 3052-3060
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 30
    • 19444376974 scopus 로고    scopus 로고
    • Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843
    • Thennarasu S., Lee D.K., Tan A., Kari U.P., and Ramamoorthy A. Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843. Biochim. Biophys. Acta Biomembr. 1711 (2005) 49-58
    • (2005) Biochim. Biophys. Acta Biomembr. , vol.1711 , pp. 49-58
    • Thennarasu, S.1    Lee, D.K.2    Tan, A.3    Kari, U.P.4    Ramamoorthy, A.5
  • 31
    • 25844458511 scopus 로고    scopus 로고
    • Synthetic and natural polycationic polymer nanoparticles interact selectively with fluid-phase domains of DMPC lipid bilayers
    • Mecke A., Lee D.K., Ramamoorthy A., Orr B.G., and Holl M.M.B. Synthetic and natural polycationic polymer nanoparticles interact selectively with fluid-phase domains of DMPC lipid bilayers. Langmuir 21 (2005) 8588-8590
    • (2005) Langmuir , vol.21 , pp. 8588-8590
    • Mecke, A.1    Lee, D.K.2    Ramamoorthy, A.3    Orr, B.G.4    Holl, M.M.B.5
  • 32
    • 0030795382 scopus 로고    scopus 로고
    • Levofloxacin versus ciprofloxacin, flucloxacillin, or vancomycin for treatment of experimental endocarditis due to methicillin-susceptible or -resistant staphylococcus aureus
    • Entenza J.M., Vouillamoz J., Glauser M.P., and Moreillon P. Levofloxacin versus ciprofloxacin, flucloxacillin, or vancomycin for treatment of experimental endocarditis due to methicillin-susceptible or -resistant staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 1662-1667
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1662-1667
    • Entenza, J.M.1    Vouillamoz, J.2    Glauser, M.P.3    Moreillon, P.4
  • 33
    • 33644886043 scopus 로고    scopus 로고
    • Membrane activity of biomimetic facially amphiphilic antibiotics
    • Arnt L., Rennie J., Linser S., Willumeit R., and Tew G.N. Membrane activity of biomimetic facially amphiphilic antibiotics. J. Phys. Chem. B. 110 (2006) 3527-3532
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 3527-3532
    • Arnt, L.1    Rennie, J.2    Linser, S.3    Willumeit, R.4    Tew, G.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.