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Volumn 31, Issue 10, 2010, Pages 1811-1820

Interaction of cationic antimicrobial peptides with phospholipid vesicles and their antibacterial activity

Author keywords

Antimicrobial peptide; Calcein; Cationic; Liposomes; Phospholipid

Indexed keywords

CALCEIN; GLYCYLALANYLASPARAGINYLALANYLALANYLLYSYLLYSYLLEUCYLALANYLTHREONYLPHENYLALANYLALANYLLYSYLLYSYLISOLEUCYLPHENYLALANYLTHREONYLALANYLTYROSYLTRYPTOPHAN; GLYCYLALANYLASPARAGINYLALANYLALANYLLYSYLLYSYLPHENYLALANYLALANYLASPARAGINYLLEUCYLISOLEUCYLLYSYLLYSYLISOLEUCYLPHENYLALANYLASPARAGINYLTYROSYLISOLEUCYLTRYPTOPHAN; GLYCYLALANYLASPARAGINYLALANYLALANYLLYSYLLYSYLPHENYLALANYLALANYLTHREONYLISOLEUCYLALANYLLYSYLLYSYLPHENYLALANYLISOLEUCYLASPARAGINYLTYROSYLLEUCYLTRYPTOPHAN; GLYCYLALANYLASPARAGINYLALANYLLEUCYLLYSYLLYSYLTYROSYLPHENYLALANYLTHREONYLISOLEUCYLLEUCYLLYSYLLYSYLPHENYLALANYLPHENYLALANYLLYSYLLEUCYLALANYLTRYPTOPHAN; GLYCYLALANYLASPARAGINYLLEUCYLALANYLLYSYLLYSYLPHENYLALANYLTYROSYLTHREONYLTYROSYLISOLEUCYLASPARAGINYLLYSYLPHENYLALANYLISOLEUCYLASPARAGINYLTYROSYLALANYLTRYPTOPHAN; GLYCYLALANYLLYSYLALANYLLEUCYLTHREONYLLYSYLALANYLALANYLTHREONYLALANYLPHENYLALANYLTHREONYLLYSYLPHENYLALANYLTYROSYLLYSYLTHREONYLISOLEUCYLTRYPTOPHAN; GLYCYLALANYLLYSYLTYROSYLALANYLLYSYLISOLEUCYLISOLEUCYLTYROSYLASPARAGINYLTYROSYLLEUCYLLYSYLLYSYLISOLEUCYLALANYLASPARAGINYLALANYLLEUCYLTRYPTOPHAN; GLYCYLALANYLLYSYLTYROSYLALANYLLYSYLTYROSYLISOLEUCYLTYROSYLASPARAGINYLPHENYLALANYLTYROSYLLYSYLTYROSYLISOLEUCYLALANYLLYSYLTYROSYLISOLEUCYLTRYPTOPHAN; GLYCYLALANYLTHREONYLTYROSYLALANYLLYSYLLYSYLISOLEUCYLISOLEUCYLLYSYLTHREONYLISOLEUCYLTHREONYLLYSYLISOLEUCYLALANYLTHREONYLTHREONYLALANYLTRYPTOPHAN; GLYCYLISOLEUCYLGLYCYLLYSYLPHENYLALANYLLEUCYLHISTIDYLSERYLALANYLLYSYLLYSYLTRYPTOPHYLGLYCYLLYSYLALANYLPHENYLALANYLVALYLGLYCYLGLUTAMYLISOLEUCYLMETHIONYLASPARAGINYLSERINE; GLYCYLISOLEUCYLLYSYLISOLEUCYLALANYLLYSYLLYSYLALANYLISOLEUCYLTHREONYLISOLEUCYLALANYLLYSYLLYSYLISOLEUCYLALANYLLYSYLISOLEUCYLTYROSYLTRYPTOPHAN; GLYCYLLEUCYLTHREONYLPHENYLALANYLLEUCYLLYSYLLYSYLISOLEUCYLLEUCYLASPARAGINYLPHENYLALANYLALANYLLYSYLLYSYLISOLEUCYLTYROSYLTHREONYLALANYLISOLEUCYLTRYPTOPHAN; GLYCYLTRYPTOPHYLGLYCYLSERYLPHENYLALANYLPHENYLALANYLLYSYLLYSYLALANYLALANYLHISTIDYLVALYLGLYCYLLYSYLHISTIDYLVALYLGLYCYLLYSYLALANYLALANYLLEUCYLTHREONYLHISTIDYLTYROSYLLEUCINE; GLYCYLTYROSYLASPARAGINYLTYROSYLALANYLLYSYLLYSYLLEUCYLALANYLASPARAGINYLLEUCYLALANYLLYSYLLYSYLPHENYLALANYLALANYLASPARAGINYLALANYLLEUCYLTRYPTOPHAN; GLYCYLTYROSYLLYSYLTYROSYLISOLEUCYLASPARAGINYLASPARAGINYLISOLEUCYLISOLEUCYLLYSYLTYROSYLISOLEUCYLASPARAGINYLLYSYLPHENYLALANYLPHENYLALANYLLYSYLTYROSYLISOLEUCYLTRYPTOPHAN; GLYCYLTYROSYLLYSYLTYROSYLTYROSYLASPARAGINYLLYSYLISOLEUCYLTYROSYLASPARAGINYLTYROSYLLEUCYLASPARAGINYLLYSYLTYROSYLLEUCYLLYSYLTYROSYLALANYLTRYPTOPHAN; LIPOSOME; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 77956689158     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.06.021     Document Type: Article
Times cited : (57)

References (28)
  • 1
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • B. Bechinger, and K. Lohner Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochim Biophys Acta 1758 2006 1529 1539
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 2005 238 250
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • D.I. Chan, E.J. Prenner, and H.J. Vogel Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim Biophys Acta 1758 2006 1184 1202
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 4
    • 4143101331 scopus 로고    scopus 로고
    • Involvement of the N- and C-terminal fragments of bovine pancreatic deoxyribonuclease in active protein folding
    • W.J. Chen, P.T. Huang, J. Liu, and T.H. Liao Involvement of the N- and C-terminal fragments of bovine pancreatic deoxyribonuclease in active protein folding Biochemistry 43 2004 10653 10663
    • (2004) Biochemistry , vol.43 , pp. 10653-10663
    • Chen, W.J.1    Huang, P.T.2    Liu, J.3    Liao, T.H.4
  • 5
    • 1842507219 scopus 로고    scopus 로고
    • Biological functions of the disulfides in bovine pancreatic deoxyribonuclease
    • W.J. Chen, I.S. Lee, C.Y. Chen, and T.H. Liao Biological functions of the disulfides in bovine pancreatic deoxyribonuclease Protein Sci 13 2004 875 883
    • (2004) Protein Sci , vol.13 , pp. 875-883
    • Chen, W.J.1    Lee, I.S.2    Chen, C.Y.3    Liao, T.H.4
  • 6
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Y.H. Chen, J.T. Yang, and K.H. Chau Determination of the helix and beta form of proteins in aqueous solution by circular dichroism Biochemistry 13 1974 3350 3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 7
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • H.T. Chou, T.Y. Kuo, J.C. Chiang, M.J. Pei, W.T. Yang, and H.C. Yu Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp Int J Antimicrob Agents 32 2008 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
  • 8
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • M. Dathe, and T. Wieprecht Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells Biochim Biophys Acta 1462 1999 71 87
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 9
    • 0033960609 scopus 로고    scopus 로고
    • Miscibility of phosphatidylethanolamine - Phosphatidylglycerol mixtures as a function of pH and acyl chain length
    • P. Garidel, and A. Blume Miscibility of phosphatidylethanolamine - phosphatidylglycerol mixtures as a function of pH and acyl chain length Eur Biophys J 28 2000 629 638
    • (2000) Eur Biophys J , vol.28 , pp. 629-638
    • Garidel, P.1    Blume, A.2
  • 10
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • R.E. Hancock, and R. Lehrer Cationic peptides: a new source of antibiotics Trends Biotechnol 16 1998 82 88
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 11
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: From natural to novel antibiotics
    • R.E. Hancock, and A. Patrzykat Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics Curr Drug Targets Infect Disord 2 2002 79 83
    • (2002) Curr Drug Targets Infect Disord , vol.2 , pp. 79-83
    • Hancock, R.E.1    Patrzykat, A.2
  • 12
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • R.E. Hancock, and H.G. Sahl Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat Biotechnol 24 2006 1551 1557
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 13
  • 15
    • 0033055447 scopus 로고    scopus 로고
    • Addition and omission analogs of the 13-residue antibacterial and hemolytic peptide PKLLKTFLSKWIG: Structural preference, model membrane binding and biological activities
    • V. Krishnakumari, and R. Nagaraj Addition and omission analogs of the 13-residue antibacterial and hemolytic peptide PKLLKTFLSKWIG: structural preference, model membrane binding and biological activities J Peptide Res 53 1999 47 55
    • (1999) J Peptide Res , vol.53 , pp. 47-55
    • Krishnakumari, V.1    Nagaraj, R.2
  • 16
    • 51949114856 scopus 로고    scopus 로고
    • Structure-antimicrobial activity relationship between pleurocidin and its enantiomer
    • J. Lee, and D.G. Lee Structure-antimicrobial activity relationship between pleurocidin and its enantiomer Exp Mol Med 40 2008 370 376
    • (2008) Exp Mol Med , vol.40 , pp. 370-376
    • Lee, J.1    Lee, D.G.2
  • 17
    • 47049098589 scopus 로고    scopus 로고
    • Liposome-based biomembrane mimetic systems: Implications for lipid-peptide interactions
    • K. Lohner, E. Sevcsik, G. Pabst, and A.L. Liu Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions Adv Planar Lipid Bilayers Liposomes 6 2008 103 137
    • (2008) Adv Planar Lipid Bilayers Liposomes , vol.6 , pp. 103-137
    • Lohner, K.1    Sevcsik, E.2    Pabst, G.3    Liu, A.L.4
  • 18
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • L.D. Mayer, M.J. Hope, and P.R. Cullis Vesicles of variable sizes produced by a rapid extrusion procedure Biochim Biophys Acta 858 1986 161 168
    • (1986) Biochim Biophys Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 19
    • 25444445004 scopus 로고    scopus 로고
    • Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system
    • B. Pozo Navas, K. Lohner, G. Deutsch, E. Sevcsik, K.A. Riske, and R. Dimova Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system Biochim Biophys Acta 1716 2005 40 48
    • (2005) Biochim Biophys Acta , vol.1716 , pp. 40-48
    • Pozo Navas, B.1    Lohner, K.2    Deutsch, G.3    Sevcsik, E.4    Riske, K.A.5    Dimova, R.6
  • 20
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane perturbing abilities
    • G. Saberwal, and R. Nagaraj Cell-lytic and antibacterial peptides that act perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane perturbing abilities Biochim Biophys Acta 1197 1994 109 131
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 21
    • 12844268168 scopus 로고    scopus 로고
    • Peptide-lipid interactions: Insights and perspectives
    • J.M. Sanderson Peptide-lipid interactions: insights and perspectives Org Biomol Chem 3 2005 201 212
    • (2005) Org Biomol Chem , vol.3 , pp. 201-212
    • Sanderson, J.M.1
  • 22
    • 77949415172 scopus 로고    scopus 로고
    • Proteomic identification of membrane proteins regulating antimicrobial peptide resistance in Vibrio parahaemolyticus
    • C.J. Shen, T.Y. Kuo, C.C. Lin, L.P. Chow, and W.J. Chen Proteomic identification of membrane proteins regulating antimicrobial peptide resistance in Vibrio parahaemolyticus J Appl Microbiol 108 2010 1398 1407
    • (2010) J Appl Microbiol , vol.108 , pp. 1398-1407
    • Shen, C.J.1    Kuo, T.Y.2    Lin, C.C.3    Chow, L.P.4    Chen, W.J.5
  • 23
    • 25144472273 scopus 로고    scopus 로고
    • The threat of antibiotic resistance in Gram-negative pathogenic bacteria: Beta-lactams in peril
    • J.M. Thomson, and R.A. Bonomo The threat of antibiotic resistance in Gram-negative pathogenic bacteria: beta-lactams in peril Curr Opin Microbiol 8 2005 518 524
    • (2005) Curr Opin Microbiol , vol.8 , pp. 518-524
    • Thomson, J.M.1    Bonomo, R.A.2
  • 24
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic alpha-helical antimicrobial peptides
    • A. Tossi, L. Sandri, A. Giangaspero, and Amphipathic alpha-helical antimicrobial peptides Biopolymers 55 2000 4 30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 26
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positive charged helix face on the membrane activity of amphipatic, antibacterial peptides
    • T. Wieprecht, M. Dathe, R.M. Epand, M. Beyerman, E. Krause, and W.L. Maloy Influence of the angle subtended by the positive charged helix face on the membrane activity of amphipatic, antibacterial peptides Biochemistry 36 1997 12869 12880
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyerman, M.4    Krause, E.5    Maloy, W.L.6
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • M.R. Yeaman, and N.Y. Yount Mechanisms of antimicrobial peptide action and resistance Pharmacol Rev 55 2003 27 55
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
    • 0035134035 scopus 로고    scopus 로고
    • Interaction of pleurocidin and its analogs with phospholipids membrane and their antibacterial activity
    • K. Yoshida, Y. Mukai, T. Niidome, C. Takashi, Y. Tokunaga, and T. Hatakeyama Interaction of pleurocidin and its analogs with phospholipids membrane and their antibacterial activity J Pept Res 57 2001 119 126
    • (2001) J Pept Res , vol.57 , pp. 119-126
    • Yoshida, K.1    Mukai, Y.2    Niidome, T.3    Takashi, C.4    Tokunaga, Y.5    Hatakeyama, T.6


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