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Volumn 52, Issue 12, 2008, Pages 4463-4465

Lysine-enriched cecropin-mellitin antimicrobial peptides with enhanced selectivity

Author keywords

[No Author keywords available]

Indexed keywords

CM 15; K 10; K 1014; K 14; K 4; K 410; K 414; LYSINE; LYSYLTRYPTOPHYLLYSYLLEUCYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLALANYLVALYLLEUCYLLYSYLLYSYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLEUCYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLALANYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLEUCYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLLYSYLVALYLLEUCYLLYSYLLYSYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLEUCYLPHENYLALANYLLYSYLLYSYLISOLEUCYLGLYCYL LYSYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLYSYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLALANYLVALYLLEUCYLLYSYLLYSYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLYSYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLALANYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLTRYPTOPHYLLYSYLLYSYLPHENYLALANYLLYSYLLYSYLISOLEUCYL GLYCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCINE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 57049114502     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00810-08     Document Type: Article
Times cited : (26)

References (22)
  • 2
    • 0026570489 scopus 로고
    • Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity
    • Andreu, D., J. Ubach, A. Boman, B. Wahlin, D. Wade, R. B. Merrifield, and H. G. Boman. 1992. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett. 296:190-194.
    • (1992) FEBS Lett , vol.296 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wahlin, B.4    Wade, D.5    Merrifield, R.B.6    Boman, H.G.7
  • 3
    • 0347319182 scopus 로고    scopus 로고
    • Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: A site-directed spin-labeling study
    • Bhargava, K., and J. B. Feix. 2004. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study. Biophys. J. 86:329-336.
    • (2004) Biophys. J , vol.86 , pp. 329-336
    • Bhargava, K.1    Feix, J.B.2
  • 4
    • 0028890190 scopus 로고
    • Induced conformational states of amphipathic peptides in aqueous/lipid environments
    • Blondelle, S. E., J. M. Ostresh, R. A. Houghten, and E. Perez-Paya. 1995. Induced conformational states of amphipathic peptides in aqueous/lipid environments. Biophys. J. 68:351-359.
    • (1995) Biophys. J , vol.68 , pp. 351-359
    • Blondelle, S.E.1    Ostresh, J.M.2    Houghten, R.A.3    Perez-Paya, E.4
  • 5
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • Boman, H. G., D. Wade, I. A. Boman, B. Wahlin, and R. B. Merrifield. 1989. Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259:103-106.
    • (1989) FEBS Lett , vol.259 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wahlin, B.4    Merrifield, R.B.5
  • 6
    • 20644432642 scopus 로고    scopus 로고
    • The nervous system and innate immunity: The neuropeptide connection
    • Brogden, K. A., J. M. Guthmiller, M. Salzet, and M. Zasloff. 2005. The nervous system and innate immunity: the neuropeptide connection. Nat. Immunol. 6:558-564.
    • (2005) Nat. Immunol , vol.6 , pp. 558-564
    • Brogden, K.A.1    Guthmiller, J.M.2    Salzet, M.3    Zasloff, M.4
  • 7
    • 0034862968 scopus 로고    scopus 로고
    • N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide
    • Chicharro, C., C. Granata, R. Lozano, D. Andreu, and L. Rivas. 2001. N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide. Antimicrob. Agents Chemother. 45:2441-2449.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 2441-2449
    • Chicharro, C.1    Granata, C.2    Lozano, R.3    Andreu, D.4    Rivas, L.5
  • 8
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides
    • Dathe, M., and T. Wieprecht. 1999. Structural features of helical antimicrobial peptides. Biochim. Biophys. Acta 1462:71-87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 9
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M., and H. J. Vogel. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 10
    • 3042758514 scopus 로고    scopus 로고
    • In vitro activity and killing effect of the synthetic hybrid cecropin A-melittin peptide CA(1-7)M(2-9)NH(2) on methicillin-resistant nosocomial isolates of Staphylococcus aureus and interactions with clinically used antibiotics
    • Giacometti, A., O. Cirioni, W. Kamysz, G. D'Amato, C. Silvestri, M. Simona Del Prete, J. Lukasiak, and G. Scalise. 2004. In vitro activity and killing effect of the synthetic hybrid cecropin A-melittin peptide CA(1-7)M(2-9)NH(2) on methicillin-resistant nosocomial isolates of Staphylococcus aureus and interactions with clinically used antibiotics. Diagn. Microbiol. Infect. Dis. 49:197-200.
    • (2004) Diagn. Microbiol. Infect. Dis , vol.49 , pp. 197-200
    • Giacometti, A.1    Cirioni, O.2    Kamysz, W.3    D'Amato, G.4    Silvestri, C.5    Simona Del Prete, M.6    Lukasiak, J.7    Scalise, G.8
  • 11
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha-helical antimicrobial peptides
    • Giangaspero, A., L. Sandri, and A. Tossi. 2001. Amphipathic alpha-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
  • 12
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: A nuclear magnetic resonance and dynamical simulated annealing study
    • Holak, T. A., A. Engstrom, P. J. Kraulis, G. Lindeberg, H. Bennich, T. A. Jones, A. M. Gronenborn, and G. M. Clore. 1988. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27:7620-7629.
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engstrom, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 14
    • 0030178188 scopus 로고    scopus 로고
    • Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids
    • Juvvadi, P., S. Vunnam, E. L. Merrifield, H. G. Boman, and R. B. Merrifield. 1996. Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids. J. Pep. Sci. 2:223-232.
    • (1996) J. Pep. Sci , vol.2 , pp. 223-232
    • Juvvadi, P.1    Vunnam, S.2    Merrifield, E.L.3    Boman, H.G.4    Merrifield, R.B.5
  • 15
    • 34548650215 scopus 로고    scopus 로고
    • Membrane insertion and bilayer perturbation by antimicrobial peptide CM15
    • Pistolesi, S., R. Pogni, and J. B. Feix. 2007. Membrane insertion and bilayer perturbation by antimicrobial peptide CM15. Biophys. J. 93:1651-1660.
    • (2007) Biophys. J , vol.93 , pp. 1651-1660
    • Pistolesi, S.1    Pogni, R.2    Feix, J.B.3
  • 16
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides
    • Sato, H., and J. B. Feix. 2006. Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides. Biochim. Biophys. Acta 1758:1245-1256.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 17
    • 33747484924 scopus 로고    scopus 로고
    • Osmoprotection of bacterial cells from toxicity caused by antimicrobial hybrid peptide CM15
    • Sato, H., and J. B. Feix. 2006. Osmoprotection of bacterial cells from toxicity caused by antimicrobial hybrid peptide CM15. Biochemistry 45:9997-10007.
    • (2006) Biochemistry , vol.45 , pp. 9997-10007
    • Sato, H.1    Feix, J.B.2
  • 18
    • 33645794536 scopus 로고    scopus 로고
    • Activity of cecropin A-melittin hybrid peptides against colistin-resistant clinical strains of Acinetobacter baumannii: Molecular basis for the differential mechanisms of action
    • Saugar, J. M., M. J. Rodriguez-Hernandez, B. G. de la Torre, M. E. Pachon-Ibanez, M. Fernandez-Reyes, D. Andreu, J. Pachon, and L. Rivas. 2006. Activity of cecropin A-melittin hybrid peptides against colistin-resistant clinical strains of Acinetobacter baumannii: molecular basis for the differential mechanisms of action. Antimicrob. Agents Chemother. 50:1251-1256.
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 1251-1256
    • Saugar, J.M.1    Rodriguez-Hernandez, M.J.2    de la Torre, B.G.3    Pachon-Ibanez, M.E.4    Fernandez-Reyes, M.5    Andreu, D.6    Pachon, J.7    Rivas, L.8
  • 19
    • 0026738175 scopus 로고
    • The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR
    • Sipos, D., M. Andersson, and A. Ehrenberg. 1992. The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR. Eur. J. Biochem. 209:163-169.
    • (1992) Eur. J. Biochem , vol.209 , pp. 163-169
    • Sipos, D.1    Andersson, M.2    Ehrenberg, A.3
  • 20
    • 0025908464 scopus 로고
    • Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin. Resonance assignments and secondary structure
    • Sipos, D., K. Chandrasekhar, K. Arvidsson, A. Engstrom, and A. Ehrenberg. 1991. Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin. Resonance assignments and secondary structure. Eur. J. Biochem. 199:285-291.
    • (1991) Eur. J. Biochem , vol.199 , pp. 285-291
    • Sipos, D.1    Chandrasekhar, K.2    Arvidsson, K.3    Engstrom, A.4    Ehrenberg, A.5
  • 21
    • 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
  • 22
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides: Using a sequence template to guide structure-activity relationship studies
    • Zelezetsky, I., and A. Tossi. 2006. Alpha-helical antimicrobial peptides: using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta 1758:1436-1449.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2


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