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Volumn 17, Issue 5, 2011, Pages 358-365

Alanine scanning analysis and structure-function relationships of the frog-skin antimicrobial peptide temporin-1Ta

Author keywords

Alanine scanning; Antimicrobial peptides; Frog skin; Temporin

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; TEMPORIN 1TA; TEMPORIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79953787474     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1350     Document Type: Article
Times cited : (37)

References (53)
  • 1
    • 0034960109 scopus 로고    scopus 로고
    • The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity
    • Yang D, Chertov O, Oppenheim JJ. The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity. Cell. Mol. Life Sci. 2001; 58: 978-989.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 978-989
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 2
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 3
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P, Mor A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbiol. 1995; 49: 277-304.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 4
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003; 55: 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 6
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics
    • Hancock REW, Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr. Drug. Targets Infect. Disord. 2002; 2: 79-83.
    • (2002) Curr. Drug. Targets Infect. Disord. , vol.2 , pp. 79-83
    • Hancock, R.E.W.1    Patrzykat, A.2
  • 7
    • 69949086979 scopus 로고    scopus 로고
    • Potential of immunomodulatory host defense peptides as novel anti-infectives
    • Easton DM, Nijnik A, Mayer ML, Hancock RE. Potential of immunomodulatory host defense peptides as novel anti-infectives. Trends Biotechnol. 2009; 27: 582-590.
    • (2009) Trends Biotechnol. , vol.27 , pp. 582-590
    • Easton, D.M.1    Nijnik, A.2    Mayer, M.L.3    Hancock, R.E.4
  • 8
    • 78649922290 scopus 로고    scopus 로고
    • Strategies for the discovery and advancement of novel cationic antimicrobial peptides
    • Hadley EB, Hancock RE. Strategies for the discovery and advancement of novel cationic antimicrobial peptides. Curr. Top. Med. Chem. 2010; 8: 1872-1881.
    • (2010) Curr. Top. Med. Chem. , vol.8 , pp. 1872-1881
    • Hadley, E.B.1    Hancock, R.E.2
  • 9
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee N, Hancock RE. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell. Mol. Life Sci. 2007; 64: 922-933.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 10
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: a family of endogenous antimicrobial peptides
    • Lehrer RI, Ganz T. Cathelicidins: a family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 2002; 9: 18-22.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 11
    • 16844377323 scopus 로고    scopus 로고
    • Defensins and other antimicrobial peptides: a historical perspective and an update
    • Ganz T. Defensins and other antimicrobial peptides: a historical perspective and an update. Comb. Chem. High Throughput Screen. 2005; 8: 209-217.
    • (2005) Comb. Chem. High Throughput Screen. , vol.8 , pp. 209-217
    • Ganz, T.1
  • 13
    • 0037180768 scopus 로고    scopus 로고
    • The immunopathogenesis of sepsis
    • Cohen J. The immunopathogenesis of sepsis. Nature 2002; 420: 885-891.
    • (2002) Nature , vol.420 , pp. 885-891
    • Cohen, J.1
  • 14
    • 0034650823 scopus 로고    scopus 로고
    • Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein
    • Scott MG, Vreugdenhil AC, Buurman WA, Hancock RE, Gold MR. Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein. J. Immunol. 2000; 164: 549-553.
    • (2000) J. Immunol. , vol.164 , pp. 549-553
    • Scott, M.G.1    Vreugdenhil, A.C.2    Buurman, W.A.3    Hancock, R.E.4    Gold, M.R.5
  • 16
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1999; 1462: 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 17
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002; 66: 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 18
    • 32944471770 scopus 로고    scopus 로고
    • Antimicrobial peptides (AMPs): peptide structure and mode of action
    • Park Y, Hahm KS. Antimicrobial peptides (AMPs): peptide structure and mode of action. J. Biochem. Mol. Biol. 2005; 38: 507-516.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 507-516
    • Park, Y.1    Hahm, K.S.2
  • 20
    • 33744459976 scopus 로고    scopus 로고
    • Temporins, anti-infective peptides with expanding properties
    • Mangoni ML. Temporins, anti-infective peptides with expanding properties. Cell. Mol. Life Sci. 2006; 63: 1060-1069.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1060-1069
    • Mangoni, M.L.1
  • 22
    • 58149505744 scopus 로고    scopus 로고
    • The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae)
    • Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). Peptides 2009; 30: 273-282.
    • (2009) Peptides , vol.30 , pp. 273-282
    • Wang, H.1    Lu, Y.2    Zhang, X.3    Hu, Y.4    Yu, H.5    Liu, J.6    Sun, J.7
  • 23
    • 24744448697 scopus 로고    scopus 로고
    • Paneth cell alpha-defensins: peptide mediators of innate immunity in the small intestine
    • Ouellette AJ. Paneth cell alpha-defensins: peptide mediators of innate immunity in the small intestine. Springer Semin. Immunopathol. 2005; 27: 133-146.
    • (2005) Springer Semin. Immunopathol. , vol.27 , pp. 133-146
    • Ouellette, A.J.1
  • 24
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 2004; 75: 39-48.
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 25
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: what do they tell us?
    • Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? Biopolymers 1998; 47: 435-450.
    • (1998) Biopolymers , vol.47 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 26
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim. Biophys. Acta 2004; 1696: 1-14.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 30
    • 34848841823 scopus 로고    scopus 로고
    • Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti-microbial peptides from amphibian skin
    • Mangoni ML, Marcellini HG, Simmaco M. Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti-microbial peptides from amphibian skin. J. Pept. Sci. 2007; 13: 603-613.
    • (2007) J. Pept. Sci. , vol.13 , pp. 603-613
    • Mangoni, M.L.1    Marcellini, H.G.2    Simmaco, M.3
  • 31
    • 33749376461 scopus 로고    scopus 로고
    • A synergism between temporins toward gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer
    • Rosenfeld Y, Barra D, Simmaco M, Shai Y, Mangoni ML. A synergism between temporins toward gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer. J. Biol. Chem. 2006; 281: 28565-28574.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28565-28574
    • Rosenfeld, Y.1    Barra, D.2    Simmaco, M.3    Shai, Y.4    Mangoni, M.L.5
  • 32
    • 53149151881 scopus 로고    scopus 로고
    • Lipopolysaccharide, a key molecule involved in the synergism between temporinsin inhibiting bacterial growth and in endotoxin neutralization
    • Mangoni ML, Epand RF, Rosenfeld Y, Peleg A, Barra D, Epand RM, Shai Y. Lipopolysaccharide, a key molecule involved in the synergism between temporinsin inhibiting bacterial growth and in endotoxin neutralization. J. Biol. Chem. 2008; 283: 22907-229017.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22907-229017
    • Mangoni, M.L.1    Epand, R.F.2    Rosenfeld, Y.3    Peleg, A.4    Barra, D.5    Epand, R.M.6    Shai, Y.7
  • 33
    • 67649401884 scopus 로고    scopus 로고
    • Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification
    • Mangoni ML, Shai Y. Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification. Biochim. Biophys. Acta 2009; 1788: 1610-1619.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1610-1619
    • Mangoni, M.L.1    Shai, Y.2
  • 36
    • 0021989787 scopus 로고
    • Antifungal activity of ovotransferrin towards genus Candida
    • Valenti P, Visca P, Antonini G, Orsi N. Antifungal activity of ovotransferrin towards genus Candida. Mycopathologia 1985; 89: 169-175.
    • (1985) Mycopathologia , vol.89 , pp. 169-175
    • Valenti, P.1    Visca, P.2    Antonini, G.3    Orsi, N.4
  • 37
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg D. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 1984; 53: 595-623.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 38
    • 0035283168 scopus 로고    scopus 로고
    • SOMCD: method for evaluating protein secondary structure from UV circular dichroism spectra
    • Unneberg P, Merelo JJ, Chacon P, Moran F. SOMCD: method for evaluating protein secondary structure from UV circular dichroism spectra. Proteins 2001; 42: 460-470.
    • (2001) Proteins , vol.42 , pp. 460-470
    • Unneberg, P.1    Merelo, J.J.2    Chacon, P.3    Moran, F.4
  • 41
    • 0023446047 scopus 로고
    • Health and economic impacts of antimicrobial resistance
    • Holmberg SD, Solomon SL, Blake PA. Health and economic impacts of antimicrobial resistance. Rev. Infect. Dis. 1987; 9: 1065-1078.
    • (1987) Rev. Infect. Dis. , vol.9 , pp. 1065-1078
    • Holmberg, S.D.1    Solomon, S.L.2    Blake, P.A.3
  • 42
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: an expanding scenario
    • Rinaldi AC. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 2002; 6: 799-804.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 43
    • 0032504056 scopus 로고    scopus 로고
    • Molecular cloning of a bombinin gene from Bombina orientalis: detection of NF-kappaB and NF-IL6 binding sites in its promoter
    • Miele R, Ponti D, Boman HG, Barra D, Simmaco M. Molecular cloning of a bombinin gene from Bombina orientalis: detection of NF-kappaB and NF-IL6 binding sites in its promoter. FEBS Lett. 1998; 431: 23-28.
    • (1998) FEBS Lett. , vol.431 , pp. 23-28
    • Miele, R.1    Ponti, D.2    Boman, H.G.3    Barra, D.4    Simmaco, M.5
  • 44
    • 0035380623 scopus 로고    scopus 로고
    • The synthesis of antimicrobial peptides in the skin of Rana esculenta is stimulated by microorganisms
    • Mangoni ML, Miele R, Renda TG, Barra D, Simmaco M. The synthesis of antimicrobial peptides in the skin of Rana esculenta is stimulated by microorganisms. FASEB J. 2001; 15: 1431-1432.
    • (2001) FASEB J. , vol.15 , pp. 1431-1432
    • Mangoni, M.L.1    Miele, R.2    Renda, T.G.3    Barra, D.4    Simmaco, M.5
  • 46
    • 4043156313 scopus 로고    scopus 로고
    • Temporin A and related frog antimicrobial peptides use formyl peptide receptor-like 1 as a receptor to chemoattract phagocytes
    • Chen Q, Wade D, Kurosaka K, Wang ZY, Oppenheim JJ, Yang D. Temporin A and related frog antimicrobial peptides use formyl peptide receptor-like 1 as a receptor to chemoattract phagocytes. J. Immunol. 2004; 173: 2652-2659.
    • (2004) J. Immunol. , vol.173 , pp. 2652-2659
    • Chen, Q.1    Wade, D.2    Kurosaka, K.3    Wang, Z.Y.4    Oppenheim, J.J.5    Yang, D.6
  • 47
    • 0032501406 scopus 로고    scopus 로고
    • Critical aggregation concentrations of gram-negative bacterial lipopolysaccharides (LPS)
    • Aurell CA, Wistrom AO. Critical aggregation concentrations of gram-negative bacterial lipopolysaccharides (LPS). Biochem. Biophys. Res. Commun. 1998; 253: 119-123.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 119-123
    • Aurell, C.A.1    Wistrom, A.O.2
  • 48
    • 34248352027 scopus 로고    scopus 로고
    • Conformational solution studies of the anti-microbial temporin A retro-analogues by using NMR spectroscopy
    • Kamysz W, Mickiewicz B, Greber K, Rodziewicz-Motowidlo S. Conformational solution studies of the anti-microbial temporin A retro-analogues by using NMR spectroscopy. J. Pept. Sci. 2007; 13: 327-333.
    • (2007) J. Pept. Sci. , vol.13 , pp. 327-333
    • Kamysz, W.1    Mickiewicz, B.2    Greber, K.3    Rodziewicz-Motowidlo, S.4
  • 52
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T, Dathe M, Beyermann M, Krause E, Maloy WL, MacDonald DL, Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 1997; 36: 6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7


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