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Volumn 18, Issue 3, 2011, Pages 241-252

Anti-Tuberculosis Activity of α -Helical Antimicrobial Peptides: De Novo Designed L- and D-Enantiomers Versus L- and D-LL37

Author keywords

All D enantiomer; Antimicrobial peptides; Hemolysis; Mycobacterium tuberculosis

Indexed keywords

CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE; TUBERCULOSTATIC AGENT;

EID: 79951634149     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986611794578288     Document Type: Article
Times cited : (52)

References (31)
  • 2
    • 78650246775 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization Update Tuberculosis Facts, 2009.
    • (2009) Update Tuberculosis Facts
  • 3
    • 0037741082 scopus 로고    scopus 로고
    • The capsule of Mycobacterium tuberculosis and its implications for pathogenicity
    • DOI 10.1054/tuld.1998.0200
    • Daffe, M.; Etienne, G. The capsule of Mycobacterium tuberculosis and its implications for pathogenicity. Tuber Lung Dis., 1999, 79, 153-69. (Pubitemid 29348506)
    • (1999) Tubercle and Lung Disease , vol.79 , Issue.3 , pp. 153-169
    • Daffe, M.1    Etienne, G.2
  • 4
    • 52049122588 scopus 로고    scopus 로고
    • Role of antimicrobial peptides in host defense against mycobacterial infections
    • Mendez-Samperio, P. Role of antimicrobial peptides in host defense against mycobacterial infections. Peptides, 2008, 29, 1836-41.
    • (2008) Peptides , vol.29 , pp. 1836-1841
    • Mendez-Samperio, P.1
  • 5
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y.; Mant, C. T.; Farmer, S. W.; Hancock, R. E.; Vasil, M. L.; Hodges, R. S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem., 2005, 280, 12316-29.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 7
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides
    • DOI 10.1128/AAC.00925-06
    • Chen, Y.; Guarnieri, M. T.; Vasil, A. I.; Vasil, M. L.; Mant, C. T.; Hodges, R. S. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. Antimicrob Agents Chemother., 2007, 51, 1398-406. (Pubitemid 46586822)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.4 , pp. 1398-1406
    • Chen, Y.1    Guarnieri, M.T.2    Vasil, A.I.3    Vasil, M.L.4    Mant, C.T.5    Hodges, R.S.6
  • 9
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alphahelical cationic antimicrobial peptides
    • Jiang, Z.; Vasil, A. I.; Hale, J. D.; Hancock, R. E.; Vasil, M. L.; Hodges, R. S. Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alphahelical cationic antimicrobial peptides. Biopolymers (Peptide science), 2008, 90, 369-83.
    • (2008) Biopolymers (Peptide Science) , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 10
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.03.030, PII S000527360600126X
    • Durr, U. H.; Sudheendra, U. S.; Ramamoorthy, A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta, 2006, 1758, 1408-25. (Pubitemid 44436081)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 11
    • 51649127792 scopus 로고    scopus 로고
    • Expression and secretion of cathelicidin LL-37 in human epithelial cells after infection by Mycobacterium bovis Bacillus Calmette-Guerin
    • Mendez-Samperio, P.; Miranda, E.; Trejo, A. Expression and secretion of cathelicidin LL-37 in human epithelial cells after infection by Mycobacterium bovis Bacillus Calmette-Guerin. Clin. Vaccine Immunol., 2008, 15, 1450-5.
    • (2008) Clin. Vaccine Immunol. , vol.15 , pp. 1450-1455
    • Mendez-Samperio, P.1    Miranda, E.2    Trejo, A.3
  • 12
    • 48549100053 scopus 로고    scopus 로고
    • Human macrophage host defense against Mycobacterium tuberculosis
    • Liu, P. T.; Modlin, R. L. Human macrophage host defense against Mycobacterium tuberculosis. Curr. Opin. Immunol., 2008, 20, 371-6.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 371-376
    • Liu, P.T.1    Modlin, R.L.2
  • 14
    • 33845870644 scopus 로고    scopus 로고
    • Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1 mm to 9.4 mm I.D.)
    • DOI 10.1016/j.chroma.2006.11.052, PII S0021967306021960
    • Chen, Y.; Mant, C. T.; Hodges, R. S. Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1mm to 9.4mm I.D.). J. Chromatogr. A, 2007, 1140, 112-20. (Pubitemid 46026780)
    • (2007) Journal of Chromatography A , vol.1140 , Issue.1-2 , pp. 112-120
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 15
    • 0038265111 scopus 로고    scopus 로고
    • A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography
    • DOI 10.1074/jbc.M301777200
    • Lee, D. L.; Mant, C. T.; Hodges, R. S. A novel method to measure self-association of small amphipathic molecules: temperature profiling in reversed-phase chromatography. J. Biol. Chem., 2003, 278, 22918-27. (Pubitemid 36830356)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22918-22927
    • Lee, D.L.1    Mant, C.T.2    Hodges, R.S.3
  • 16
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • DOI 10.1038/299371a0
    • Eisenberg, D.; Weiss, R. M.; Terwilliger, T. C. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature, 1982, 299, 371-4. (Pubitemid 12012871)
    • (1982) Nature , vol.299 , Issue.5881 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 17
    • 0141617541 scopus 로고    scopus 로고
    • The design of Jemboss: A graphical user interface to EMBOSS
    • DOI 10.1093/bioinformatics/btg251
    • Carver, T.; Bleasby, A. The design of Jemboss: a graphical user interface to EMBOSS. Bioinformatics, 2003, 19, 1837-43. (Pubitemid 37220476)
    • (2003) Bioinformatics , vol.19 , Issue.14 , pp. 1837-1843
    • Carver, T.1    Bleasby, A.2
  • 18
    • 33646231485 scopus 로고    scopus 로고
    • Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects
    • Kovacs, J. M.; Mant, C. T.; Hodges, R. S. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects. Biopolymers (Peptide Science), 2006, 84, 283-97.
    • (2006) Biopolymers (Peptide Science) , vol.84 , pp. 283-297
    • Kovacs, J.M.1    Mant, C.T.2    Hodges, R.S.3
  • 19
    • 75649097134 scopus 로고    scopus 로고
    • Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales
    • Mant, C. T.; Kovacs, J. M.; Kim, H. M.; Pollock, D. D.; Hodges, R. S. Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales. Biopolymers (Peptide Science), 2009, 92, 573-95.
    • (2009) Biopolymers (Peptide Science) , vol.92 , pp. 573-595
    • Mant, C.T.1    Kovacs, J.M.2    Kim, H.M.3    Pollock, D.D.4    Hodges, R.S.5
  • 20
    • 0043135171 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography: I. Monitoring of dimerization and unfolding of amphipathic α-helical peptides
    • DOI 10.1016/S0021-9673(03)00621-6
    • Mant, C. T.; Chen, Y.; Hodges, R. S. Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization and unfolding of amphipathic alpha-helical peptides. J. Chromatogr. A, 2003, 1009, 29-43. (Pubitemid 36966669)
    • (2003) Journal of Chromatography A , vol.1009 , Issue.1-2 , pp. 29-43
    • Mant, C.T.1    Chen, Y.2    Hodges, R.S.3
  • 21
    • 0042634260 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography: II. Monitoring of folding and stability of two-stranded α-helical coiled-coils
    • DOI 10.1016/S0021-9673(03)00919-1
    • Mant, C. T.; Tripet, B.; Hodges, R. S. Temperature profiling of polypeptides in reversed-phase liquid chromatography. II. Monitoring of folding and stability of two-stranded alpha-helical coiledcoils. J. Chromatogr. A., 2003, 1009, 45-59. (Pubitemid 36966670)
    • (2003) Journal of Chromatography A , vol.1009 , Issue.1-2 , pp. 45-59
    • Mant, C.T.1    Tripet, B.2    Hodges, R.S.3
  • 22
    • 0024982236 scopus 로고
    • Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: Amphipathic alpha-helices
    • Zhou, N. E.; Mant, C. T.; Hodges, R. S. Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: amphipathic alpha-helices. Pept. Res., 1990, 3, 8-20.
    • (1990) Pept. Res. , vol.3 , pp. 8-20
    • Zhou, N.E.1    Mant, C.T.2    Hodges, R.S.3
  • 23
    • 0037008238 scopus 로고    scopus 로고
    • Temperature selectivity in reversed-phase high performance liquid chromatography
    • DOI 10.1016/S0021-9673(01)01321-8, PII S0021967301013218
    • Dolan, J. W. Temperature selectivity in reversed-phase high performance liquid chromatography. J. Chromatogr. A, 2002, 965, 195-205. (Pubitemid 34876318)
    • (2002) Journal of Chromatography A , vol.965 , Issue.1-2 , pp. 195-205
    • Dolan, J.W.1
  • 24
    • 0141568854 scopus 로고    scopus 로고
    • Factors determining the efficacy of alpha-helical antimicrobial peptides
    • DOI 10.2174/0929866033478663
    • Dennison, S. R.; Harris, F.; Phoenix, D. A. Factors determining the efficacy of alpha-helical antimicrobial peptides. Protein Pept. Lett., 2003, 10, 497-502. (Pubitemid 37143550)
    • (2003) Protein and Peptide Letters , vol.10 , Issue.5 , pp. 497-502
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 25
    • 11244333158 scopus 로고    scopus 로고
    • Amphiphilic α-helical antimicrobial peptides and their structure/function relationships
    • DOI 10.2174/0929866053406084
    • Dennison, S. R.; Wallace, J.; Harris, F.; Phoenix, D. A. Amphiphilic alpha-helical antimicrobial peptides and their structure/function relationships. Protein Pept. Lett., 2005, 12, 31-9. (Pubitemid 40068358)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.1 , pp. 31-39
    • Dennison, S.R.1    Wallace, J.2    Harris, F.3    Phoenix, D.A.4
  • 27
    • 0036185353 scopus 로고    scopus 로고
    • Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic α-helix
    • DOI 10.1046/j.1397-002x.2001.10994.x
    • Chen, Y.; Mant, C. T.; Hodges, R. S. Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix. J. Pept. Res., 2002, 59, 18-33. (Pubitemid 34185257)
    • (2002) Journal of Peptide Research , vol.59 , Issue.1 , pp. 18-33
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 28
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • Baumann, G.; Mueller, P. A molecular model of membrane excitability. J. Supramol. Struct., 1974, 2, 538-57.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 29
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G.; Lecar, H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys., 1977, 10, 1-34. (Pubitemid 8065109)
    • (1977) Quarterly Reviews of Biophysics , vol.10 , Issue.1 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 30
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • DOI 10.1021/bi0256983
    • Tachi, T.; Epand, R. F.; Epand, R. M.; Matsuzaki, K. Positiondependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry, 2002, 41, 10723-31. (Pubitemid 34913333)
    • (2002) Biochemistry , vol.41 , Issue.34 , pp. 10723-10731
    • Tachi, T.1    Epand, R.F.2    Epand, R.M.3    Matsuzaki, K.4
  • 31
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • DOI 10.1021/bi00164a017
    • Pouny, Y.; Rapaport, D.; Mor, A.; Nicolas, P.; Shai, Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry, 1992, 31,12416-23. (Pubitemid 23163118)
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5


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