메뉴 건너뛰기




Volumn 49, Issue 43, 2010, Pages 9161-9170

Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-MICROBIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; BACTERIAL MEMBRANES; FUNCTIONAL MOTIFS; GRAM-NEGATIVE BACTERIA; HELICAL STRUCTURES; HEMOLYTIC ASSAYS; HIGH EFFICIENCY; HORSESHOE CRAB; IN-DEPTH STUDY; INNATE IMMUNE SYSTEMS; KEY ELEMENTS; MOLECULAR MECHANISM; RESISTANT BACTERIA; SECONDARY STRUCTURES; SINGLE-MOLECULE; THERAPEUTIC POTENTIALS;

EID: 78049266859     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1011578     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 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
  • 2
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • Wang, G., Li, X., and Wang, Z. (2009) APD2: the updated antimicrobial peptide database and its application in peptide design Nucleic Acids Res. 37, 933-937
    • (2009) Nucleic Acids Res. , vol.37 , pp. 933-937
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 3
    • 0034488452 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides and their multifunctional role in the immune system
    • Scott, M. G. and Hancock, R. E. (2000) Cationic antimicrobial peptides and their multifunctional role in the immune system Crit. Rev. Immunol. 20, 407-431
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 407-431
    • Scott, M.G.1    Hancock, R.E.2
  • 4
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown, K. L. and Hancock, R. E. (2006) Cationic host defense (antimicrobial) peptides Curr. Opin. Immunol. 18, 24-30
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 5
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock, R. E. (2001) Cationic peptides: effectors in innate immunity and novel antimicrobials Lancet Infect. Dis. 1, 156-164
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 6
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies, J. (1994) Inactivation of antibiotics and the dissemination of resistance genes Science 264, 375-382
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 7
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R. and Yount, N. Y. (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
  • 8
    • 66749153183 scopus 로고    scopus 로고
    • Single molecule resolution of the antimicrobial action of quantum dot-labeled sushi peptide on live bacteria
    • Leptihn, S., Har, J. Y., Chen, J., Ho, B., Wohland, T., and Ding, J. L. (2009) Single molecule resolution of the antimicrobial action of quantum dot-labeled sushi peptide on live bacteria BMC Biol. 7, 22
    • (2009) BMC Biol. , vol.7 , pp. 22
    • Leptihn, S.1    Har, J.Y.2    Chen, J.3    Ho, B.4    Wohland, T.5    Ding, J.L.6
  • 9
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy, W. L. and Kari, U. P. (1995) Structure-activity studies on magainins and other host defense peptides Biopolymers 37, 105-122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 10
    • 42449113387 scopus 로고    scopus 로고
    • The Sushi peptides: Structural characterization and mode of action against Gram-negative bacteria
    • Ding, J. L., Li, P., and Ho, B. (2008) The Sushi peptides: structural characterization and mode of action against Gram-negative bacteria Cell. Mol. Life Sci. 65, 1202-1219
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1202-1219
    • Ding, J.L.1    Li, P.2    Ho, B.3
  • 11
    • 0030664760 scopus 로고    scopus 로고
    • Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
    • Wieprecht, T., Dathe, M., Krause, E., Beyermann, M., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997) Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment FEBS Lett. 417, 135-140
    • (1997) FEBS Lett. , vol.417 , pp. 135-140
    • Wieprecht, T.1    Dathe, M.2    Krause, E.3    Beyermann, M.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 12
    • 27744493759 scopus 로고    scopus 로고
    • Correlation between the activities of alpha-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times
    • Kim, S., Kim, S. S., and Lee, B. J. (2005) Correlation between the activities of alpha-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times Peptides 26, 2050-2056
    • (2005) Peptides , vol.26 , pp. 2050-2056
    • Kim, S.1    Kim, S.S.2    Lee, B.J.3
  • 13
    • 67649424250 scopus 로고    scopus 로고
    • Augmentation of the antimicrobial activities of guinea pig cathelicidin CAP11-derived peptides by amino acid substitutions
    • Okuda, D., Yomogida, S., Kuwahara-Arai, K., Hitamatsu, K., Tamura, H., and Nagaoka, I. (2009) Augmentation of the antimicrobial activities of guinea pig cathelicidin CAP11-derived peptides by amino acid substitutions Int. J. Mol. Med. 23, 501-508
    • (2009) Int. J. Mol. Med. , vol.23 , pp. 501-508
    • Okuda, D.1    Yomogida, S.2    Kuwahara-Arai, K.3    Hitamatsu, K.4    Tamura, H.5    Nagaoka, I.6
  • 14
    • 45749084085 scopus 로고    scopus 로고
    • Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides
    • Rosenfeld, Y., Sahl, H. G., and Shai, Y. (2008) Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides Biochemistry 47, 6468-6478
    • (2008) Biochemistry , vol.47 , pp. 6468-6478
    • Rosenfeld, Y.1    Sahl, H.G.2    Shai, Y.3
  • 15
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • Chou, H. T., Kuo, T. Y., Chiang, J. C., Pei, M. J., Yang, W. T., Yu, H. C., Lin, S. B., and Chen, W. J. (2008) Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp Int. J. Antimicrob. Agents 32, 130-138
    • (2008) Int. J. Antimicrob. Agents , vol.32 , pp. 130-138
    • Chou, H.T.1    Kuo, T.Y.2    Chiang, J.C.3    Pei, M.J.4    Yang, W.T.5    Yu, H.C.6    Lin, S.B.7    Chen, W.J.8
  • 17
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima, K., Chikushi, A., Lee, K. K., Yonehara, S., and Matsuzaki, K. (2003) Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes J. Biol. Chem. 278, 1310-1315
    • (2003) J. Biol. Chem. , vol.278 , pp. 1310-1315
    • Takeshima, K.1    Chikushi, A.2    Lee, K.K.3    Yonehara, S.4    Matsuzaki, K.5
  • 18
    • 0029069628 scopus 로고
    • Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides
    • Pathak, N., Salas-Auvert, R., Ruche, G., Janna, M. H., McCarthy, D., and Harrison, R. G. (1995) Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides Proteins 22, 182-186
    • (1995) Proteins , vol.22 , pp. 182-186
    • Pathak, N.1    Salas-Auvert, R.2    Ruche, G.3    Janna, M.H.4    McCarthy, D.5    Harrison, R.G.6
  • 19
    • 75749122220 scopus 로고    scopus 로고
    • Effect of the hydrophobicity to net positive charge ratio on antibacterial and anti-endotoxin activities of structurally similar antimicrobial peptides
    • Rosenfeld, Y., Lev, N., and Shai, Y. (2010) Effect of the hydrophobicity to net positive charge ratio on antibacterial and anti-endotoxin activities of structurally similar antimicrobial peptides Biochemistry 49, 853-861
    • (2010) Biochemistry , vol.49 , pp. 853-861
    • Rosenfeld, Y.1    Lev, N.2    Shai, Y.3
  • 20
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe, M. and Wieprecht, T. (1999) Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells Biochim. Biophys. Acta 1462, 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 21
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • Dathe, M., Wieprecht, T., Nikolenko, H., Handel, L., Maloy, W. L., MacDonald, D. L., Beyermann, M., and Bienert, M. (1997) Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic 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, M.7    Bienert, M.8
  • 22
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • Wieprecht, T., Apostolov, O., Beyermann, M., and Seelig, J. (1999) Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium J. Mol. Biol. 294, 785-794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 23
    • 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, W. L., MacDonald, D. L., and Bienert, M. (1997) Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes Biochemistry 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
  • 24
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht, T., Dathe, M., Epand, R. M., Beyermann, M., Krause, E., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997) Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides Biochemistry 36, 12869-12880
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 25
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. (1999) The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy Biochim. Biophys. Acta 1462, 157-183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 26
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation Biochemistry 35, 11361-11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 27
    • 0033028126 scopus 로고    scopus 로고
    • Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin, S. Y., Kang, J. H., and Hahm, K. S. (1999) Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides J. Pept. Res. 53, 82-90
    • (1999) J. Pept. Res. , vol.53 , pp. 82-90
    • Shin, S.Y.1    Kang, J.H.2    Hahm, K.S.3
  • 28
    • 0036836642 scopus 로고    scopus 로고
    • Combining the GOR v algorithm with evolutionary information for protein secondary structure prediction from amino acid sequence
    • Kloczkowski, A., Ting, K. L., Jernigan, R. L., and Garnier, J. (2002) Combining the GOR V algorithm with evolutionary information for protein secondary structure prediction from amino acid sequence Proteins 49, 154-166
    • (2002) Proteins , vol.49 , pp. 154-166
    • Kloczkowski, A.1    Ting, K.L.2    Jernigan, R.L.3    Garnier, J.4
  • 29
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
    • Luo, P. and Baldwin, R. L. (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water Biochemistry 36, 8413-8421
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 31
    • 0022423437 scopus 로고
    • Effect of tryptophan derivatives on the phase properties of bilayers
    • Jain, M. K., Rogers, J., Simpson, L., and Gierasch, L. M. (1985) Effect of tryptophan derivatives on the phase properties of bilayers Biochim. Biophys. Acta 816, 153-162
    • (1985) Biochim. Biophys. Acta , vol.816 , pp. 153-162
    • Jain, M.K.1    Rogers, J.2    Simpson, L.3    Gierasch, L.M.4
  • 32
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y. and Barkley, M. D. (1998) Toward understanding tryptophan fluorescence in proteins Biochemistry 37, 9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 33
    • 0029066816 scopus 로고
    • Environments of the four tryptophans in the extracellular domain of human tissue factor: Comparison of results from absorption and fluorescence difference spectra of tryptophan replacement mutants with the crystal structure of the wild-type protein
    • Hasselbacher, C. A., Rusinova, E., Waxman, E., Rusinova, R., Kohanski, R. A., Lam, W., Du Guha, A. J., Lin, T. C., and Polikarpov, I. (1995) Environments of the four tryptophans in the extracellular domain of human tissue factor: comparison of results from absorption and fluorescence difference spectra of tryptophan replacement mutants with the crystal structure of the wild-type protein Biophys. J. 69, 20-29
    • (1995) Biophys. J. , vol.69 , pp. 20-29
    • Hasselbacher, C.A.1    Rusinova, E.2    Waxman, E.3    Rusinova, R.4    Kohanski, R.A.5    Lam, W.6    Du Guha, A.J.7    Lin, T.C.8    Polikarpov, I.9
  • 34
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system: Measurement by fluorescence correlation spectroscopy
    • Magde, D., Elson, E. L., and Webb, W. W. (1972) Thermodynamic fluctuations in a reacting system: measurement by fluorescence correlation spectroscopy Phys. Rev. Lett. 705-708
    • (1972) Phys. Rev. Lett. , pp. 705-708
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 35
    • 0026533988 scopus 로고
    • Augmentation of the antibacterial activity of magainin by positive-charge chain extension
    • Bessalle, R., Haas, H., Goria, A., Shalit, I., and Fridkin, M. (1992) Augmentation of the antibacterial activity of magainin by positive-charge chain extension Antimicrob. Agents Chemother. 36, 313-317
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 313-317
    • Bessalle, R.1    Haas, H.2    Goria, A.3    Shalit, I.4    Fridkin, M.5
  • 36
    • 0039981711 scopus 로고    scopus 로고
    • The tendency of magainin to associate upon binding to phospholipid bilayers
    • Schumann, M., Dathe, M., Wieprecht, T., Beyermann, M., and Bienert, M. (1997) The tendency of magainin to associate upon binding to phospholipid bilayers Biochemistry 36, 4345-4351
    • (1997) Biochemistry , vol.36 , pp. 4345-4351
    • Schumann, M.1    Dathe, M.2    Wieprecht, T.3    Beyermann, M.4    Bienert, M.5
  • 37
    • 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
  • 38
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides
    • Giangaspero, A., Sandri, L., and Tossi, A. (2001) Amphipathic alpha helical antimicrobial peptides Eur. J. Biochem./FEBS 268, 5589-5600
    • (2001) Eur. J. Biochem./FEBS , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.