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Volumn 54, Issue 8, 2010, Pages 3132-3142

Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA HELIX PEPTIDYLGLYCYLLEUCINE CARBOXYAMIDE; ANTIINFECTIVE AGENT; GRAMICIDIN S; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 77955377305     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00124-10     Document Type: Article
Times cited : (422)

References (58)
  • 1
    • 70350677390 scopus 로고    scopus 로고
    • Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: Concentration-dependent re-alignment and selfassembly as a β-barrel
    • Afonin, S., U. H. N. Dürr, P. Wadhwani, J. B. Salgado, and A. S. Ulrich. 2008. Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: concentration-dependent re-alignment and selfassembly as a β-barrel. Top. Curr. Chem. 273:139-154.
    • (2008) Top. Curr. Chem. , vol.273 , pp. 139-154
    • Afonin, S.1    Dürr, U.H.N.2    Wadhwani, P.3    Salgado, J.B.4    Ulrich, A.S.5
  • 3
    • 57549112908 scopus 로고    scopus 로고
    • Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state (19)F NMR spectroscopy
    • Afonin, S., S. L. Grage, M. Ieronimo, P. Wadhwani, and A. S. Ulrich. 2008. Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state (19)F NMR spectroscopy. J. Am. Chem. Soc. 130:16512-16514.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16512-16514
    • Afonin, S.1    Grage, S.L.2    Ieronimo, M.3    Wadhwani, P.4    Ulrich, A.S.5
  • 4
    • 0001994881 scopus 로고    scopus 로고
    • Susceptibility testing of antimicrobials in liquid media
    • V. Lorian (ed.), 4th ed. Williams & Wilkins, Baltimore, MD
    • Amsterdam, D. 1996. Susceptibility testing of antimicrobials in liquid media, p. 52-111. In V. Lorian (ed.), Antibiotics in laboratory medicine, 4th ed. Williams & Wilkins, Baltimore, MD.
    • (1996) Antibiotics in Laboratory Medicine , pp. 52-111
    • Amsterdam, D.1
  • 5
    • 7044246109 scopus 로고    scopus 로고
    • Investigation of morphological changes to Staphylococcus aureus induced by ovine-derived antimicrobial peptides using TEM and AFM
    • Anderson, R. C., R. G. Haverkamp, and P. L. Yu. 2004. Investigation of morphological changes to Staphylococcus aureus induced by ovine-derived antimicrobial peptides using TEM and AFM. FEMS Microbiol. Lett. 240:105-110.
    • (2004) FEMS Microbiol. Lett. , vol.240 , pp. 105-110
    • Anderson, R.C.1    Haverkamp, R.G.2    Yu, P.L.3
  • 6
    • 0031903306 scopus 로고    scopus 로고
    • Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., M. Zasloff, and S. J. Opella. 1998. Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy. Biophys. J. 74:981-987. (Pubitemid 28345291)
    • (1998) Biophysical Journal , vol.74 , Issue.2 I , pp. 981-987
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 7
    • 35448957629 scopus 로고    scopus 로고
    • The ability of Aneurinibacillus migulanus (Bacillus brevis) to produce the antibiotic gramicidin S is correlated with phenotype variation
    • Berditsch, M., S. Afonin, and A. S. Ulrich. 2007. The ability of Aneurinibacillus migulanus (Bacillus brevis) to produce the antibiotic gramicidin S is correlated with phenotype variation. Appl. Environ. Microbiol. 73:6620-6628.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6620-6628
    • Berditsch, M.1    Afonin, S.2    Ulrich, A.S.3
  • 8
    • 0035958848 scopus 로고    scopus 로고
    • A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids
    • Blazyk, J., R. Wiegand, J. Klein, J. Hammer, R. M. Epand, R. F. Epand, W. L. Maloy, and U. P. Kari. 2001. A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. J. Biol. Chem. 276:27899-27906.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27899-27906
    • Blazyk, J.1    Wiegand, R.2    Klein, J.3    Hammer, J.4    Epand, R.M.5    Epand, R.F.6    Maloy, W.L.7    Kari, U.P.8
  • 9
    • 0030660573 scopus 로고    scopus 로고
    • The effect of gramicidin, a topical contraceptive and antimicrobial agent with anti-HIV activity, against herpes simplex viruses type 1 and 2 in vitro
    • Bourinbaiar, A. S., and C. F. Coleman. 1997. The effect of gramicidin, a topical contraceptive and antimicrobial agent with anti-HIV activity, against herpes simplex viruses type 1 and 2 in vitro. Arch. Virol. 142:2225-2235.
    • (1997) Arch. Virol. , vol.142 , pp. 2225-2235
    • Bourinbaiar, A.S.1    Coleman, C.F.2
  • 10
    • 2942592590 scopus 로고    scopus 로고
    • Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides
    • Chinchar, V. G., L. Bryan, U. Silphadaung, E. Noga, D. Wade, and L. Rollins-Smith. 2004. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology 323:268-275.
    • (2004) Virology , vol.323 , pp. 268-275
    • Chinchar, V.G.1    Bryan, L.2    Silphadaung, U.3    Noga, E.4    Wade, D.5    Rollins-Smith, L.6
  • 12
    • 0344687481 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide PGLa on live Escherichia coli
    • da Silva, A., Jr., and O. Teschke. 2003. Effects of the antimicrobial peptide PGLa on live Escherichia coli. Biochim. Biophys. Acta 1643:95-103.
    • (2003) Biochim. Biophys. Acta , vol.1643 , pp. 95-103
    • Da Silva Jr., A.1    Teschke, O.2
  • 13
    • 0028327442 scopus 로고
    • Anion pores from magainins and related defensive peptides
    • DOI 10.1016/0300-483X(94)90160-0
    • Duclohier, H. 1994. Anion pores from magainins and related defensive peptides. Toxicology 87:175-188. (Pubitemid 24097460)
    • (1994) Toxicology , vol.87 , Issue.1-3 , pp. 175-188
    • Duclohier, H.1
  • 14
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • Friedrich, C. L., D. Moyles, T. J. Beveridge, and R. E. Hancock. 2000. Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria. Antimicrob. Agents Chemother. 44:2086-2092.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 15
    • 0001131165 scopus 로고
    • Gramicidin S and its use in the treatment of infected wounds
    • Gause, G. F., and M. G. Brazhnikova. 1944. Gramicidin S and its use in the treatment of infected wounds. Nature 154:703.
    • (1944) Nature , vol.154 , pp. 703
    • Gause, G.F.1    Brazhnikova, M.G.2
  • 16
    • 49449117012 scopus 로고
    • Gramicidin S. Origin and mode of action
    • Gause, G. F., and M. G. Brazhnikova. 1944. Gramicidin S. Origin and mode of action. Lancet 247:715-716.
    • (1944) Lancet , vol.247 , pp. 715-716
    • Gause, G.F.1    Brazhnikova, M.G.2
  • 17
    • 1842783092 scopus 로고    scopus 로고
    • Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels
    • Glaser, R. W., C. Sachse, U. H. Durr, P. Wadhwani, and A. S. Ulrich. 2004. Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels. J. Magn. Reson. 168:153-163.
    • (2004) J. Magn. Reson. , vol.168 , pp. 153-163
    • Glaser, R.W.1    Sachse, C.2    Durr, U.H.3    Wadhwani, P.4    Ulrich, A.S.5
  • 19
    • 0011073099 scopus 로고    scopus 로고
    • Microbial membrane-permeating peptides and their applications
    • U. Langel (ed.), CRC Press LLC, Boca Raton, FL
    • Gunaratna, K. R., M. Anderson, and L. Good. 2002. Microbial membrane-permeating peptides and their applications, p. 377-396. In U. Langel (ed.), Cell-penetrating peptides: process and applications. CRC Press LLC, Boca Raton, FL.
    • (2002) Cell-penetrating Peptides: Process and Applications , pp. 377-396
    • Gunaratna, K.R.1    Anderson, M.2    Good, L.3
  • 20
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. 1997. Peptide antibiotics. Lancet 349:418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 21
    • 67649396451 scopus 로고    scopus 로고
    • Free energies of molecular bound states in lipid bilayers: Lethal concentrations of antimicrobial peptides
    • Huang, H. W. 2009. Free energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptides. Biophys. J. 96:3263-3272.
    • (2009) Biophys. J. , vol.96 , pp. 3263-3272
    • Huang, H.W.1
  • 22
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang, H. W., F. Y. Chen, and M. T. Lee. 2004. Molecular mechanism of peptide-induced pores in membranes. Phys. Rev. Lett. 92:198304.
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 23
    • 0034254229 scopus 로고    scopus 로고
    • Diastereoisomeric analogues of gramicidin S: Structure, biological activity and interaction with lipid bilayers
    • Jelokhani-Niaraki, M., L. H. Kondejewski, S. W. Farmer, R. E. Hancock, C. M. Kay, and R. S. Hodges. 2000. Diastereoisomeric analogues of gramicidin S: structure, biological activity and interaction with lipid bilayers. Biochem. J. 349:747-755. (Pubitemid 30609405)
    • (2000) Biochemical Journal , vol.349 , Issue.3 , pp. 747-755
    • Jelokhani-Niaraki, M.1    Kondejewski, L.H.2    Farmer, S.W.3    Hancock, R.E.W.4    Kay, C.M.5    Hodges, R.S.6
  • 24
    • 0141990272 scopus 로고
    • Osmotic regulation and the biosynthesis of membrane-derived oligosaccharides in Escherichia coli
    • Kennedy, E. P. 1982. Osmotic regulation and the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 79:1092-1095.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 1092-1095
    • Kennedy, E.P.1
  • 25
    • 85010292860 scopus 로고    scopus 로고
    • The biophysics of the gram-negative periplasmic space
    • Koch, A. L. 1998. The biophysics of the gram-negative periplasmic space. Crit. Rev. Microbiol. 24:23-59.
    • (1998) Crit. Rev. Microbiol. , vol.24 , pp. 23-59
    • Koch, A.L.1
  • 27
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • Kondejewski, L. H., S. W. Farmer, D. S. Wishart, C. M. Kay, R. E. Hancock, and R. S. Hodges. 1996. Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 271:25261-25268.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.5    Hodges, R.S.6
  • 28
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewski, L. H., M. Jelokhani-Niaraki, S. W. Farmer, B. Lix, C. M. Kay, B. D. Sykes, R. E. 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
    • Kondejewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.7    Hodges, R.S.8
  • 29
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity
    • Lehrer, R. I., A. Barton, K. A. Daher, S. S. Harwig, T. Ganz, and M. E. Selsted. 1989. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J. Clin. Invest. 84:553-561.
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 30
    • 33847019613 scopus 로고    scopus 로고
    • Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria
    • Li, A., P. Y. Lee, B. Ho, J. L. Ding, and C. T. Lim. 2007. Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria. Biochim. Biophys. Acta 1768:411-418.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 411-418
    • Li, A.1    Lee, P.Y.2    Ho, B.3    Ding, J.L.4    Lim, C.T.5
  • 31
    • 33947307138 scopus 로고    scopus 로고
    • Double-stranded helical twisted beta-sheet channels in crystals of gramicidin S grown in the presence of trifluoroacetic and hydrochloric acids
    • Llamas-Saiz, A. L., G. M. Grotenbreg, M. Overhand, and M. J. van Raaij. 2007. Double-stranded helical twisted beta-sheet channels in crystals of gramicidin S grown in the presence of trifluoroacetic and hydrochloric acids. Acta Crystallogr. D Biol. Crystallogr. 63:401-407.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 401-407
    • Llamas-Saiz, A.L.1    Grotenbreg, G.M.2    Overhand, M.3    Van Raaij, M.J.4
  • 32
    • 67649295414 scopus 로고    scopus 로고
    • Biological activity and structural aspects of PGLa interaction with membrane mimetic systems
    • Lohner, K., and F. Prossnigg. 2009. Biological activity and structural aspects of PGLa interaction with membrane mimetic systems. Biochim. Biophys. Acta 1788:1656-1666.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1656-1666
    • Lohner, K.1    Prossnigg, F.2
  • 33
    • 0032049224 scopus 로고    scopus 로고
    • Area expansion and permeation of phospholipid membrane bilayers by influenza fusion peptides and melittin
    • Longo, M. L., A. J. Waring, L. M. Gordon, and D. A. Hammer. 1998. Area expansion and permeation of phospholipid membrane bilayers by influenza fusion peptides and melittin. Langmuir 14:2385-2395.
    • (1998) Langmuir , vol.14 , pp. 2385-2395
    • Longo, M.L.1    Waring, A.J.2    Gordon, L.M.3    Hammer, D.A.4
  • 34
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke, S., K. He, and H. Huang. 1995. Membrane thinning caused by magainin 2. Biochemistry 34:16764-16769.
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 35
    • 25844437587 scopus 로고    scopus 로고
    • Atomic force microscopy study of the effect of antimicrobial peptides on the cell envelope of Escherichia coli
    • DOI 10.1128/AAC.49.10.4085-4092.2005
    • Meincken, M., D. L. Holroyd, and M. Rautenbach. 2005. Atomic force microscopy study of the effect of antimicrobial peptides on the cell envelope of Escherichia coli. Antimicrob. Agents Chemother. 49:4085-4092. (Pubitemid 41400950)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.10 , pp. 4085-4092
    • Meincken, M.1    Holroyd, D.L.2    Rautenbach, M.3
  • 36
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M. N., R. Ferre, and M. A. Castanho. 2009. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7:245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 37
    • 0033303795 scopus 로고    scopus 로고
    • Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities
    • Meury, J., and G. Devilliers. 1999. Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities. Biol. Cell 91:67-75.
    • (1999) Biol. Cell , vol.91 , pp. 67-75
    • Meury, J.1    Devilliers, G.2
  • 38
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykovskaya, E., and W. Dowhan. 2000. Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182:1172-1175.
    • (2000) J. Bacteriol. , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 39
    • 0022628194 scopus 로고
    • Osmotic adaptation by gram-negative bacteria: Possible role for periplasmic oligosaccharides
    • Miller, K. J., E. P. Kennedy, and V. N. Reinhold. 1986. Osmotic adaptation by gram-negative bacteria: possible role for periplasmic oligosaccharides. Science 231:48-51.
    • (1986) Science , vol.231 , pp. 48-51
    • Miller, K.J.1    Kennedy, E.P.2    Reinhold, V.N.3
  • 40
    • 0036904138 scopus 로고    scopus 로고
    • Body shaping under water stress: Osmosensing and osmoregulation of solute transport in bacteria
    • DOI 10.1002/1439-7633(20020503)3:5<384::AID-CBIC384>3.0.CO;2-H
    • Morbach, S., and R. Kramer. 2002. Body shaping under water stress: osmosensing and osmoregulation of solute transport in bacteria. Chembiochem 3:384-397. (Pubitemid 36002281)
    • (2002) ChemBioChem , vol.3 , Issue.5 , pp. 384-397
    • Morbach, S.1    Kramer, R.2
  • 41
    • 0036241412 scopus 로고    scopus 로고
    • Susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to membrane-active peptides and enrofloxacin in human tissue cell cultures
    • Nir-Paz, R., M. C. Prevost, P. Nicolas, A. Blanchard, and H. Wroblewski. 2002. Susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to membrane-active peptides and enrofloxacin in human tissue cell cultures. Antimicrob. Agents Chemother. 46:1218-1225.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1218-1225
    • Nir-Paz, R.1    Prevost, M.C.2    Nicolas, P.3    Blanchard, A.4    Wroblewski, H.5
  • 42
    • 38349116218 scopus 로고    scopus 로고
    • Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template.'
    • Pag, U., M. Oedenkoven, V. Sass, Y. Shai, O. Shamova, N. Antcheva, A. Tossi, and H. G. Sahl. 2008. Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template.' J. Antimicrob. Chemother. 61:341-352.
    • (2008) J. Antimicrob. Chemother. , vol.61 , pp. 341-352
    • Pag, U.1    Oedenkoven, M.2    Sass, V.3    Shai, Y.4    Shamova, O.5    Antcheva, N.6    Tossi, A.7    Sahl, H.G.8
  • 43
    • 0001545743 scopus 로고
    • Series in optical sciences
    • Springer-Verlag, New York, NY
    • Reimer, L. (ed.). 1995. Series in optical sciences, vol. 71. Energy-filtering transmission electron microscopy, p. 347-400. Springer-Verlag, New York, NY.
    • (1995) Energy-filtering Transmission Electron Microscopy , vol.71 , pp. 347-400
    • Reimer, L.1
  • 45
    • 67749143910 scopus 로고    scopus 로고
    • Synergistic interaction between silver nanoparticles and membrane-permeabilizing antimicrobial peptides
    • Ruden, S., K. Hilpert, M. Berditsch, P. Wadhwani, and A. S. Ulrich. 2009. Synergistic interaction between silver nanoparticles and membrane- permeabilizing antimicrobial peptides. Antimicrob. Agents Chemother. 53:3538-3540.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3538-3540
    • Ruden, S.1    Hilpert, K.2    Berditsch, M.3    Wadhwani, P.4    Ulrich, A.S.5
  • 46
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell nonselective membrane-lytic peptides
    • Shai, Y. 1999. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell nonselective membrane-lytic peptides. Biochim. Biophys. Acta 1462:55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 47
    • 0029099061 scopus 로고
    • Morphology of defensin-treated Staphylococcus aureus
    • Shimoda, M., K. Ohki, Y. Shimamoto, and O. Kohashi. 1995. Morphology of defensin-treated Staphylococcus aureus. Infect. Immun. 63:2886-2891.
    • (1995) Infect. Immun. , vol.63 , pp. 2886-2891
    • Shimoda, M.1    Ohki, K.2    Shimamoto, Y.3    Kohashi, O.4
  • 48
    • 0033433992 scopus 로고    scopus 로고
    • SMAP-29: A potent antibacterial and antifungal peptide from sheep leukocytes
    • DOI 10.1016/S0014-5793(99)01600-2, PII S0014579399016002
    • Skerlavaj, B., M. Benincasa, A. Risso, M. Zanetti, and R. Gennaro. 1999. SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett. 463:58-62. (Pubitemid 30001718)
    • (1999) FEBS Letters , vol.463 , Issue.1-2 , pp. 58-62
    • Skerlavaj, B.1    Benincasa, M.2    Risso, A.3    Zanetti, M.4    Gennaro, R.5
  • 49
    • 0024286949 scopus 로고
    • Antimicrobial properties of peptides from Xenopus granular gland secretions
    • Soravia, E., G. Martini, and M. Zasloff. 1988. Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228:337-340.
    • (1988) FEBS Lett. , vol.228 , pp. 337-340
    • Soravia, E.1    Martini, G.2    Zasloff, M.3
  • 50
    • 28444479815 scopus 로고    scopus 로고
    • Molecular evolution of animal antimicrobial peptides: Widespread moderate positive selection
    • Tennessen, J. A. 2005. Molecular evolution of animal antimicrobial peptides: widespread moderate positive selection. J. Evol. Biol. 18:1387-1394.
    • (2005) J. Evol. Biol. , vol.18 , pp. 1387-1394
    • Tennessen, J.A.1
  • 51
    • 0032504531 scopus 로고    scopus 로고
    • Wide-spectrum antibiotic activity of synthetic, amphipathic peptides
    • Tiozzo, E., G. Rocco, A. Tossi, and D. Romeo. 1998. Wide-spectrum antibiotic activity of synthetic, amphipathic peptides. Biochem. Biophys. Res. Commun. 249:202-206.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 202-206
    • Tiozzo, E.1    Rocco, G.2    Tossi, A.3    Romeo, D.4
  • 52
    • 52349123671 scopus 로고    scopus 로고
    • Pore structure, thinning effect, and lateral diffusive dynamics of oriented lipid membranes interacting with antimicrobial peptide protegrin-1: 31P and 2H solid-state NMR study
    • Wi, S., and C. Kim. 2008. Pore structure, thinning effect, and lateral diffusive dynamics of oriented lipid membranes interacting with antimicrobial peptide protegrin-1: 31P and 2H solid-state NMR study. J. Phys. Chem. B 112:11402-11414.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 11402-11414
    • Wi, S.1    Kim, C.2
  • 53
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • Wu, M., and R. E. Hancock. 1999. Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274:29-35.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.2
  • 54
    • 0037059160 scopus 로고    scopus 로고
    • Shape changes of giant unilamellar vesicles of phosphatidylcholine induced by a de novo designed peptide interacting with their membrane interface
    • Yamashita, Y., S. M. Masum, T. Tanaka, and M. Yamazaki. 2002. Shape changes of giant unilamellar vesicles of phosphatidylcholine induced by a de novo designed peptide interacting with their membrane interface. Langmuir 18:9638-9641.
    • (2002) Langmuir , vol.18 , pp. 9638-9641
    • Yamashita, Y.1    Masum, S.M.2    Tanaka, T.3    Yamazaki, M.4
  • 55
    • 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
  • 56
    • 18144381988 scopus 로고    scopus 로고
    • Antimicrobial actions of the human epididymis 2 (HE2) protein isoforms, HE2alpha, HE2beta1 and HE2beta2
    • Yenugu, S., K. G. Hamil, F. S. French, and S. H. Hall. 2004. Antimicrobial actions of the human epididymis 2 (HE2) protein isoforms, HE2alpha, HE2beta1 and HE2beta2. Reprod. Biol. Endocrinol. 2:61.
    • (2004) Reprod. Biol. Endocrinol. , vol.2 , pp. 61
    • Yenugu, S.1    Hamil, K.G.2    French, F.S.3    Hall, S.H.4
  • 57
    • 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
  • 58
    • 0034424412 scopus 로고    scopus 로고
    • Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa
    • DOI 10.1128/AAC.44.12.3317-3321.2000
    • Zhang, L., P. Dhillon, H. Yan, S. Farmer, and R. E. Hancock. 2000. Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 44:3317-3321. (Pubitemid 33014325)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.12 , pp. 3317-3321
    • Zhang, L.1    Dhillon, P.2    Yan, H.3    Farmer, S.4    Hancock, R.E.W.5


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