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Volumn 1798, Issue 10, 2010, Pages 1934-1943

Structural contributions to the intracellular targeting strategies of antimicrobial peptides

Author keywords

Buforin II; CD spectroscopy; DNA binding; Magainin 2; Peptide antibiotics; Pleurocidin

Indexed keywords

BUFORIN 2; BUFORIN 2 AMIDE; DOUBLE STRANDED DNA; MAGAININ 2; MAGAININ 2 AMIDE; PLEUROCIDIN; POLYPEPTIDE ANTIBIOTIC AGENT; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; AMIDE; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; BACTERIAL DNA; BUFORIN II; FISH PROTEIN; MAGAININ DERIVATIVE; PEPTIDE; PROTEIN; PROTEIN BINDING;

EID: 77955655670     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.07.003     Document Type: Article
Times cited : (67)

References (44)
  • 1
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E.W., Sahl H.-G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24:1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 3
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: obstacles and realistic outlook
    • Marr A.K., Gooderham W.J., Hancock R.E.W. Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Curr. Opin. Pharmacol. 2006, 6:468-472.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.W.3
  • 4
    • 23444437935 scopus 로고    scopus 로고
    • A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs
    • Gordon Y.J., Romanowski E.G., McDermott A.M. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs. Curr. Eye Res. 2005, 30:505-515.
    • (2005) Curr. Eye Res. , vol.30 , pp. 505-515
    • Gordon, Y.J.1    Romanowski, E.G.2    McDermott, A.M.3
  • 5
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 2005, 3:238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 6
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale J.D.F., Hancock R.E.W. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 2007, 5:951-959.
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.F.1    Hancock, R.E.W.2
  • 7
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park C.B., Kim H.S., Kim S.C. Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244:253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 8
    • 67650480375 scopus 로고    scopus 로고
    • Therapeutic efficacy of buforin II and rifampin in a rat model of Acinetobacter baumanii sepsis
    • Cirioni O., et al. Therapeutic efficacy of buforin II and rifampin in a rat model of Acinetobacter baumanii sepsis. Crit. Care Med. 2009, 37:1403-1407.
    • (2009) Crit. Care Med. , vol.37 , pp. 1403-1407
    • Cirioni, O.1
  • 9
    • 43549102840 scopus 로고    scopus 로고
    • Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II
    • Uyterhoeven E.T., Butler C.H., Ko D., Elmore D.E. Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II. FEBS Lett. 2008, 582:1715-1718.
    • (2008) FEBS Lett. , vol.582 , pp. 1715-1718
    • Uyterhoeven, E.T.1    Butler, C.H.2    Ko, D.3    Elmore, D.E.4
  • 10
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 11
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • Wiegand I., Hilpert K., Hancock R.E.W. Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat. Protoc. 2008, 3:163-175.
    • (2008) Nat. Protoc. , vol.3 , pp. 163-175
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.W.3
  • 12
    • 0026742166 scopus 로고
    • Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation
    • Bechinger B., Zasloff M., Opella S.J. Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. Biophys. J. 1992, 62:12-14.
    • (1992) Biophys. J. , vol.62 , pp. 12-14
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 13
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger B., Zasloff M., Opella S.J. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 1993, 2:2077-2084.
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 14
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • Bechinger B., Ruysschaert J.M., Goormaghtigh E. Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys. J. 1999, 76:552-563.
    • (1999) Biophys. J. , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 16
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • Ludtke S.J., He K., Wu Y., Huang H.W. Cooperative membrane insertion of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta 1994, 1190:181-184.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 181-184
    • Ludtke, S.J.1    He, K.2    Wu, Y.3    Huang, H.W.4
  • 17
    • 0030602175 scopus 로고    scopus 로고
    • Solution structure of an antimicrobial peptide buforin II
    • Yi G.-S., Park C.B., Kim S.C., Cheong C. Solution structure of an antimicrobial peptide buforin II. FEBS Lett. 1996, 398:87-90.
    • (1996) FEBS Lett. , vol.398 , pp. 87-90
    • Yi, G.-S.1    Park, C.B.2    Kim, S.C.3    Cheong, C.4
  • 18
    • 0034831435 scopus 로고    scopus 로고
    • Thiazole Orange as the fluorescent intercalator in a high resolution FID assay for determining DNA binding affinity and sequence selectivity of small molecules
    • Boger D.L., Tse W.C. Thiazole Orange as the fluorescent intercalator in a high resolution FID assay for determining DNA binding affinity and sequence selectivity of small molecules. Bioorg. Med. Chem. 2001, 9:2511-2518.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2511-2518
    • Boger, D.L.1    Tse, W.C.2
  • 19
    • 67650526041 scopus 로고    scopus 로고
    • Circular dichroism spectrum of peptides in poly(pro)II conformation
    • Woody R.W. Circular dichroism spectrum of peptides in poly(pro)II conformation. J. Am. Chem. Soc. 2009, 131:8234-8245.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8234-8245
    • Woody, R.W.1
  • 20
    • 41549115091 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse
    • Durfee T., et al. The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J. Bacteriol. 2008, 190:2597-2606.
    • (2008) J. Bacteriol. , vol.190 , pp. 2597-2606
    • Durfee, T.1
  • 21
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park C.B., Kim M.S., Kim S.C. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 1996, 218:408-413.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 23
    • 67650566598 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity
    • Rathinakumar R., Walkenhorst W.F., Wimley W.C. Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity. J. Am. Chem. Soc. 2009, 131:7609-7617.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7609-7617
    • Rathinakumar, R.1    Walkenhorst, W.F.2    Wimley, W.C.3
  • 24
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as predictors of antimicrobial potency
    • Epand R.M., Rotem S., Mor A., Berno B., Epand R.F. Bacterial membranes as predictors of antimicrobial potency. J. Am. Chem. Soc. 2008, 130:14346-14352.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14346-14352
    • Epand, R.M.1    Rotem, S.2    Mor, A.3    Berno, B.4    Epand, R.F.5
  • 25
    • 58849140539 scopus 로고    scopus 로고
    • Magainin 2 revisited: a test of the Quantitative Model for the all-or-none permeabilization of phospholipid vesicles
    • Gregory S.M., Pokorny A., Almeida P.F.F. Magainin 2 revisited: a test of the Quantitative Model for the all-or-none permeabilization of phospholipid vesicles. Biophys. J. 2009, 96:116-131.
    • (2009) Biophys. J. , vol.96 , pp. 116-131
    • Gregory, S.M.1    Pokorny, A.2    Almeida, P.F.F.3
  • 26
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics
    • Almeida P.F.F., Pokorny A. Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry 2009, 48:8083-8093.
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.F.1    Pokorny, A.2
  • 27
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin
    • Gottler L.M., Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim. Biophys. Acta 2009, 1788:1680-1686.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 29
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: the origin of cooperativity
    • Huang H.W. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta 2006, 1758:1292-1302.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 31
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin
    • Mason A.J., Chotimah I.N.H., Bertani P., Bechinger B. A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin. Mol. Membr. Biol. 2006, 23:185-194.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 185-194
    • Mason, A.J.1    Chotimah, I.N.H.2    Bertani, P.3    Bechinger, B.4
  • 32
    • 0037206144 scopus 로고    scopus 로고
    • Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers
    • Saint N., Cadiou H., Bessin Y., Molle G. Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers. Biochim. Biophys. Acta 2002, 1564:359-364.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 359-364
    • Saint, N.1    Cadiou, H.2    Bessin, Y.3    Molle, G.4
  • 33
    • 58649107151 scopus 로고    scopus 로고
    • Structural determinants of antimicrobial and antiplasmodial activity and selectivity in histidine-rich amphipathic cationic peptides
    • Mason A.J., et al. Structural determinants of antimicrobial and antiplasmodial activity and selectivity in histidine-rich amphipathic cationic peptides. J. Biol. Chem. 2009, 284:119-133.
    • (2009) J. Biol. Chem. , vol.284 , pp. 119-133
    • Mason, A.J.1
  • 34
    • 67649406168 scopus 로고    scopus 로고
    • Buforins: histone H2A-derived antimicrobial peptides from toad stomach
    • Cho J.H., Sung B.H., Kim S.C. Buforins: histone H2A-derived antimicrobial peptides from toad stomach. Biochim. Biophys. Acta 2009, 1788:1564-1569.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1564-1569
    • Cho, J.H.1    Sung, B.H.2    Kim, S.C.3
  • 35
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide Buforin 2 with lipid bilayers: proline as a translocation promoting factor
    • Kobayashi S., Takeshima K., Park C.B., Kim S.C., Matsuzaki K. Interactions of the novel antimicrobial peptide Buforin 2 with lipid bilayers: proline as a translocation promoting factor. Biochemistry 2000, 39(2000):8648-8654.
    • (2000) Biochemistry , vol.39 , Issue.2000 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 36
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell penetrating ability of buforin II
    • Park C.B., Yi K.-S., Matsuzaki K., Kim M.S., Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell penetrating ability of buforin II. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:8245-8250.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.-S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 37
    • 52249094601 scopus 로고    scopus 로고
    • Effect of lipid composition on buforin II structure and membrane entry
    • Fleming E., Maharaj N.P., Chen J.L., Nelson R.B., Elmore D.E. Effect of lipid composition on buforin II structure and membrane entry. Proteins 2008, 73:480-491.
    • (2008) Proteins , vol.73 , pp. 480-491
    • Fleming, E.1    Maharaj, N.P.2    Chen, J.L.3    Nelson, R.B.4    Elmore, D.E.5
  • 38
    • 37349002470 scopus 로고    scopus 로고
    • Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization
    • Mason A.J., Marquette A., Bechinger B. Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization. Biophys. J. 2007, 93:4289-4299.
    • (2007) Biophys. J. , vol.93 , pp. 4289-4299
    • Mason, A.J.1    Marquette, A.2    Bechinger, B.3
  • 39
    • 0028564769 scopus 로고
    • 2H-NMR studies of phospholipids differing in headgroup structure and chain length
    • 2H-NMR studies of phospholipids differing in headgroup structure and chain length. Eur. Biophys. J. 1994, 23:323-335.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 323-335
    • Tuchtenhagen, J.1    Ziegler, W.2    Blume, A.3
  • 40
    • 34147135478 scopus 로고    scopus 로고
    • Characterization of the structure and membrane interaction of the antimicrobial peptides Aurein 2.2 and 2.3 from Australian southern bell frogs
    • Pan Y.-L., Cheng J.T.-J., Hale J., Pan J., Hancock R.E.W., Straus S.K. Characterization of the structure and membrane interaction of the antimicrobial peptides Aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys. J. 2007, 92:2854-2864.
    • (2007) Biophys. J. , vol.92 , pp. 2854-2864
    • Pan, Y.-L.1    Cheng, J.T.-J.2    Hale, J.3    Pan, J.4    Hancock, R.E.W.5    Straus, S.K.6
  • 42
    • 0022893917 scopus 로고
    • Circular differential scattering and circular differential absorption of DNA-protein condensates and of dyes bound to DNA-protein condensates
    • Phillips C.L., Mickols W.E., Maestre M.F., Tinoco I. Circular differential scattering and circular differential absorption of DNA-protein condensates and of dyes bound to DNA-protein condensates. Biochemistry 1986, 25:7803-7811.
    • (1986) Biochemistry , vol.25 , pp. 7803-7811
    • Phillips, C.L.1    Mickols, W.E.2    Maestre, M.F.3    Tinoco, I.4
  • 43
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal concentrations of Pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli
    • Patrzykat A., Friedrich C.L., Zhang L., Mendoza V., Hancock R.E.W. Sublethal concentrations of Pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 2002, 46:605-614.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.W.5


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