메뉴 건너뛰기




Volumn 1778, Issue 10, 2008, Pages 2430-2436

Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy

Author keywords

Antimicrobial peptides; Cationic peptides; Electrochemical impedance spectroscopy; Membrane electrochemical properties; Peptide membrane interaction; Planar supported bilayer

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 52049088052     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.06.016     Document Type: Article
Times cited : (46)

References (35)
  • 1
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 2
    • 3042620560 scopus 로고    scopus 로고
    • Structure and function of membrane-lytic peptides
    • Bechinger B. Structure and function of membrane-lytic peptides. Crit. Rev. Plant Sci. 23 (2004) 271-292
    • (2004) Crit. Rev. Plant Sci. , vol.23 , pp. 271-292
    • Bechinger, B.1
  • 3
    • 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. 3 (2005) 238-250
    • (2005) Nat. Rev., Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides
    • Sato H., and Feix J.B. Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006) 1245-1256
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 5
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin D.W., and Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim. Biophys. Acta 1778 (2008) 357-375
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 6
    • 7744229375 scopus 로고    scopus 로고
    • Structure and orientation of pardaxin determined by NMR experiments in model membranes
    • Porcelli F., Buck B., Lee D.-K., Hallock K.J., Ramamoorthy A., and Veglia G. Structure and orientation of pardaxin determined by NMR experiments in model membranes. J. Biol. Chem. 279 (2004) 45815-45823
    • (2004) J. Biol. Chem. , vol.279 , pp. 45815-45823
    • Porcelli, F.1    Buck, B.2    Lee, D.-K.3    Hallock, K.J.4    Ramamoorthy, A.5    Veglia, G.6
  • 7
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers - evidence for formation of multimeric pores
    • Wimley W.C., Selsted M.E., and White S.H. Interactions between human defensins and lipid bilayers - evidence for formation of multimeric pores. Protein Sci. 3 (1994) 1362-1373
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 8
    • 0031008251 scopus 로고    scopus 로고
    • Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching
    • Ladokhin A.S., Wimley W.C., Hristova K., and White S.H. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching. Methods Enzymol. 278 (1997) 474-486
    • (1997) Methods Enzymol. , vol.278 , pp. 474-486
    • Ladokhin, A.S.1    Wimley, W.C.2    Hristova, K.3    White, S.H.4
  • 9
    • 0034818715 scopus 로고    scopus 로고
    • Kinetics of membrane lysis by custom lytic peptides and peptide orientations in membrane
    • Chen H.M., Clayton A.H.A., Wang W., and Sawyer W.H. Kinetics of membrane lysis by custom lytic peptides and peptide orientations in membrane. Eur. J. Biochem. 268 (2001) 1659-1669
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1659-1669
    • Chen, H.M.1    Clayton, A.H.A.2    Wang, W.3    Sawyer, W.H.4
  • 10
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin-2, in phospholipid-bilayers
    • Matsuzaki K., Murase O., and Miyajima K. Kinetics of pore formation by an antimicrobial peptide, magainin-2, in phospholipid-bilayers. Biochemistry 34 (1995) 12553-12559
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 11
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin-2, across lipid bilayers by forming a pore
    • Matsuzaki K., Murase O., Fujii N., and Miyajima K. Translocation of a channel-forming antimicrobial peptide, magainin-2, across lipid bilayers by forming a pore. Biochemistry 34 (1995) 6521-6526
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 12
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides
    • Pokorny A., and Almeida P.F.F. Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides. Biochemistry 43 (2004) 8846-8857
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 13
    • 0035941062 scopus 로고    scopus 로고
    • The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
    • Haukland H.H., Ulvatne H., Sandvik K., and Vorland L.H. The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett. 508 (2001) 389-393
    • (2001) FEBS Lett. , vol.508 , pp. 389-393
    • Haukland, H.H.1    Ulvatne, H.2    Sandvik, K.3    Vorland, L.H.4
  • 14
    • 0032849898 scopus 로고    scopus 로고
    • The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers-The effects of charges and pH
    • Vogt T.C.B., and Bechinger B. The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers-The effects of charges and pH. J. Biol. Chem. 274 (1999) 29115-29121
    • (1999) J. Biol. Chem. , vol.274 , pp. 29115-29121
    • Vogt, T.C.B.1    Bechinger, B.2
  • 15
    • 0032200757 scopus 로고    scopus 로고
    • Microscopic observations of the different morphological changes caused by anti-bacterial peptides on Klebsiella pneumoniae and HL-60 leukemia cells
    • Chan S.C., Yau W.L., Wang W., Smith D.K., Sheu F.S., and Chen H.M. Microscopic observations of the different morphological changes caused by anti-bacterial peptides on Klebsiella pneumoniae and HL-60 leukemia cells. J. Peptide Sci. 4 (1998) 413-425
    • (1998) J. Peptide Sci. , vol.4 , pp. 413-425
    • Chan, S.C.1    Yau, W.L.2    Wang, W.3    Smith, D.K.4    Sheu, F.S.5    Chen, H.M.6
  • 16
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki K., Sugishita K., Harada M., Fujii N., and Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327 (1997) 119-130
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 17
    • 0034705132 scopus 로고    scopus 로고
    • Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function
    • Oren Z., and Shai Y. Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function. Biochemistry 39 (2000) 6103-6114
    • (2000) Biochemistry , vol.39 , pp. 6103-6114
    • Oren, Z.1    Shai, Y.2
  • 18
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee M.T., Chen F.Y., and Huang H.W. Energetics of pore formation induced by membrane active peptides. Biochemistry 43 (2004) 3590-3599
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.T.1    Chen, F.Y.2    Huang, H.W.3
  • 19
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model?. A case study on melittin pores
    • Yang L., Harroun T.A., Weiss T.M., Ding L., and Huang H.W. Barrel-stave model or toroidal model?. A case study on melittin pores. Biophys. J. 81 (2001) 1475-1485
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 20
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler-Wildman K.A., Lee D.K., and Ramamoorthy A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 42 (2003) 6545-6558
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler-Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 22
    • 33244472850 scopus 로고    scopus 로고
    • Directed assembly of surface-supported bilayers with transmembrane helices
    • Merzlyakov M., Li E., and Hristova K. Directed assembly of surface-supported bilayers with transmembrane helices. Langmuir 22 (2006) 1247-1253
    • (2006) Langmuir , vol.22 , pp. 1247-1253
    • Merzlyakov, M.1    Li, E.2    Hristova, K.3
  • 23
    • 38049138241 scopus 로고    scopus 로고
    • Electrical measurements of bilayer membranes formed by Langmuir-Blodgett deposition on single-crystal silicon
    • Nikolov V., Lin J., Merzlyakov M., Hristova K., and Searson P.C. Electrical measurements of bilayer membranes formed by Langmuir-Blodgett deposition on single-crystal silicon. Langmuir 23 (2007) 13040-13045
    • (2007) Langmuir , vol.23 , pp. 13040-13045
    • Nikolov, V.1    Lin, J.2    Merzlyakov, M.3    Hristova, K.4    Searson, P.C.5
  • 24
    • 23044512120 scopus 로고    scopus 로고
    • Rational combinatorial design of pore-forming beta-sheet peptides
    • Rausch J.M., Marks J.R., and Wimley W.C. Rational combinatorial design of pore-forming beta-sheet peptides. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 10511-10515
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 10511-10515
    • Rausch, J.M.1    Marks, J.R.2    Wimley, W.C.3
  • 25
    • 35649005895 scopus 로고    scopus 로고
    • beta-Sheet pore-forming peptides selected from a rational combinatorial library: mechanism of pore formation in lipid vesicles and activity in biological membranes
    • Rausch J.M., Marks J.R., Rathinakumar R., and Wimley W.C. beta-Sheet pore-forming peptides selected from a rational combinatorial library: mechanism of pore formation in lipid vesicles and activity in biological membranes. Biochemistry 46 (2007) 12124-12139
    • (2007) Biochemistry , vol.46 , pp. 12124-12139
    • Rausch, J.M.1    Marks, J.R.2    Rathinakumar, R.3    Wimley, W.C.4
  • 27
    • 29444456640 scopus 로고    scopus 로고
    • Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule. 1. Incorporation of channel peptides
    • He L.H., Robertson J.W.F., Li J., Kärcher I., Schiller S.M., Knoll W., and Naumann R. Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule. 1. Incorporation of channel peptides. Langmuir 21 (2005) 11666-11672
    • (2005) Langmuir , vol.21 , pp. 11666-11672
    • He, L.H.1    Robertson, J.W.F.2    Li, J.3    Kärcher, I.4    Schiller, S.M.5    Knoll, W.6    Naumann, R.7
  • 28
    • 33846169065 scopus 로고    scopus 로고
    • Surface-supported bilayers with transmembrane proteins: role of the polymer cushion revisited
    • Merzlyakov M., Li E., Gitsov I., and Hristova K. Surface-supported bilayers with transmembrane proteins: role of the polymer cushion revisited. Langmuir 22 (2006) 10145-10151
    • (2006) Langmuir , vol.22 , pp. 10145-10151
    • Merzlyakov, M.1    Li, E.2    Gitsov, I.3    Hristova, K.4
  • 29
    • 7044224839 scopus 로고    scopus 로고
    • The protein-lipid interface: perspectives from magnetic resonance and crystal structures
    • Marsh D., and Pali T. The protein-lipid interface: perspectives from magnetic resonance and crystal structures. Biochim. Biophys. Acta 1666 (2004) 118-141
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 118-141
    • Marsh, D.1    Pali, T.2
  • 30
    • 0035803077 scopus 로고    scopus 로고
    • Deposition of highly resistive lipid bilayer on silicon-silicon dioxide electrode and incorporation of gramicidin studied by ac impedance spectroscopy
    • Purrucker O., Hillebrandt H., Adlkofer K., and Tanaka M. Deposition of highly resistive lipid bilayer on silicon-silicon dioxide electrode and incorporation of gramicidin studied by ac impedance spectroscopy. Electrochim. Acta 47 (2001) 791-798
    • (2001) Electrochim. Acta , vol.47 , pp. 791-798
    • Purrucker, O.1    Hillebrandt, H.2    Adlkofer, K.3    Tanaka, M.4
  • 32
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin p1 with phospholipid-vesicles
    • Gazit E., Boman A., Boman H.G., and Shai Y. Interaction of the mammalian antibacterial peptide cecropin p1 with phospholipid-vesicles. Biochemistry 34 (1995) 11479-11488
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 33
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro L., Gupta K., Weiser J.N., and Axelsen P.H. The concentration-dependent membrane activity of cecropin A. Biochemistry 36 (1997) 11452-11460
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 34
    • 0023887975 scopus 로고
    • Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: salt and cholesterol effects
    • Stankowski S., Schwarz U.D., and Schwarz G. Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: salt and cholesterol effects. Biochim. Biophys. Acta 941 (1988) 11-18
    • (1988) Biochim. Biophys. Acta , vol.941 , pp. 11-18
    • Stankowski, S.1    Schwarz, U.D.2    Schwarz, G.3
  • 35
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols - model ion channels
    • Sansom M.S. Alamethicin and related peptaibols - model ion channels. Eur. Biophys. J. 22 (1993) 105-124
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.