메뉴 건너뛰기




Volumn 30, Issue 16, 2014, Pages 4767-4774

Permeabilization assay for antimicrobial peptides based on pore-spanning lipid membranes on nanoporous alumina

Author keywords

[No Author keywords available]

Indexed keywords

ALUMINA; ANODIC OXIDATION; FLUORESCENCE; LIPID BILAYERS;

EID: 84899653213     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la500358h     Document Type: Article
Times cited : (6)

References (44)
  • 1
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley, H.; Cremer, P. S. Stochastic sensors inspired by biology Nature 2001, 413, 226-230
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 4
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • Joliot, A.; Prochiantz, A. Transduction peptides: From technology to physiology Nat. Cell Biol. 2004, 6, 189-196
    • (2004) Nat. Cell Biol. , vol.6 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 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
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • Henriques, S. T.; Melo, M. N.; Castanho, M. A. R. B. Cell-penetrating peptides and antimicrobial peptides: How different are they? Biochem. J. 2006, 399, 1-7
    • (2006) Biochem. J. , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.R.B.3
  • 7
    • 79960936612 scopus 로고    scopus 로고
    • Multifunctional cationic host defence peptides and their clinical applications
    • Yeung, A. T. Y.; Gellatly, S. L.; Hancock, R. E. W. Multifunctional cationic host defence peptides and their clinical applications Cell. Mol. Life Sci. 2011, 68, 2161-2176
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2161-2176
    • Yeung, A.T.Y.1    Gellatly, S.L.2    Hancock, R.E.W.3
  • 8
    • 33644517894 scopus 로고    scopus 로고
    • Unmet medical needs in antibacterial therapy
    • Rice, L. B. Unmet medical needs in antibacterial therapy Biochem. Pharmacol. 2006, 71, 991-995
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 991-995
    • Rice, L.B.1
  • 10
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms Nature 2002, 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 11
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E.; Scott, M. G. The role of antimicrobial peptides in animal defenses Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 8856-8861
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 12
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • Hristova, K.; Selsted, M. E.; White, S. H. Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins J. Biol. Chem. 1997, 272, 24224-24233
    • (1997) J. Biol. Chem. , vol.272 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 14
    • 34447252557 scopus 로고    scopus 로고
    • The lipid dependence of melittin action investigated by dual-color fluorescence burst analysis
    • van den Bogaart, G.; Mika, J. T.; Krasnikov, V.; Poolman, B. The lipid dependence of melittin action investigated by dual-color fluorescence burst analysis Biophys. J. 2007, 93, 154-163
    • (2007) Biophys. J. , vol.93 , pp. 154-163
    • Van Den Bogaart, G.1    Mika, J.T.2    Krasnikov, V.3    Poolman, B.4
  • 16
    • 84860276903 scopus 로고    scopus 로고
    • The dynamics of melittin-induced membrane permeability
    • Kokot, G.; Mally, M.; Svetina, S. The dynamics of melittin-induced membrane permeability Eur. Biophys. J. 2012, 41, 461-474
    • (2012) Eur. Biophys. J. , vol.41 , pp. 461-474
    • Kokot, G.1    Mally, M.2    Svetina, S.3
  • 17
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K.; Yoneyama, S.; Miyajima, K. Pore formation and translocation of melittin Biophys. J. 1997, 73, 831-838
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 18
    • 33750302132 scopus 로고    scopus 로고
    • Solid supported lipid bilayers: From biophysical studies to sensor design
    • Castellana, C. P. S.; Edward, T. Solid supported lipid bilayers: From biophysical studies to sensor design Surf. Sci. Rep. 2006, 61, 429-444
    • (2006) Surf. Sci. Rep. , vol.61 , pp. 429-444
    • Castellana, C.P.S.1    Edward, T.2
  • 19
    • 38549083648 scopus 로고    scopus 로고
    • Membrane biosensor platforms using nano- and microporous supports
    • Reimhult, E.; Kumar, K. Membrane biosensor platforms using nano- and microporous supports Trends Biotechnol. 2008, 26, 82-89
    • (2008) Trends Biotechnol. , vol.26 , pp. 82-89
    • Reimhult, E.1    Kumar, K.2
  • 20
    • 74149091001 scopus 로고    scopus 로고
    • Real-time monitoring of melittin-induced pore and tubule formation from supported lipid bilayers and its physiological relevance
    • Machán, R.; Miszta, A.; Hermens, W.; Hof, M. Real-time monitoring of melittin-induced pore and tubule formation from supported lipid bilayers and its physiological relevance Chem. Phys. Lipids 2010, 163, 200-206
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 200-206
    • Machán, R.1    Miszta, A.2    Hermens, W.3    Hof, M.4
  • 21
    • 41649105098 scopus 로고    scopus 로고
    • Cationic peptide-induced remodelling of model membranes: Direct visualization by in situ atomic force microscopy
    • Shaw, J. E.; Epand, R. F.; Hsu, J. C. Y.; Mo, G. C. H.; Epand, R. M.; Yip, C. M. Cationic peptide-induced remodelling of model membranes: Direct visualization by in situ atomic force microscopy J. Struct. Biol. 2008, 162, 121-138
    • (2008) J. Struct. Biol. , vol.162 , pp. 121-138
    • Shaw, J.E.1    Epand, R.F.2    Hsu, J.C.Y.3    Mo, G.C.H.4    Epand, R.M.5    Yip, C.M.6
  • 22
    • 0034667493 scopus 로고    scopus 로고
    • Interaction of melittin with solid supported membranes
    • Steinem, C.; Galla, H.-J.; Janshoff, A. Interaction of melittin with solid supported membranes Phys. Chem. Chem. Phys. 2000, 2, 4580-4585
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4580-4585
    • Steinem, C.1    Galla, H.-J.2    Janshoff, A.3
  • 23
    • 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.; Huang, H. W. Barrel-stave model or toroidal model? A case study on melittin pores Biophys. J. 2001, 81, 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
  • 24
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • Raghuraman, H.; Chattopadhyay, A. Melittin: A membrane-active peptide with diverse functions Biosci. Rep. 2007, 27, 189-223
    • (2007) Biosci. Rep. , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 25
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor Proc. Natl. Acad. Sci. U. S. A. 1987, 84, 5449-5453
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 27
    • 79960360793 scopus 로고    scopus 로고
    • Benefits and limitations of porous substrates as biosensors for protein adsorption
    • Lazzara, T. D.; Mey, I.; Steinem, C.; Janshoff, A. Benefits and limitations of porous substrates as biosensors for protein adsorption Anal. Chem. 2011, 83, 5624-5630
    • (2011) Anal. Chem. , vol.83 , pp. 5624-5630
    • Lazzara, T.D.1    Mey, I.2    Steinem, C.3    Janshoff, A.4
  • 28
    • 79959220297 scopus 로고    scopus 로고
    • Orthogonal functionalization of nanoporous substrates: Control of 3D surface functionality
    • Lazzara, T. D.; Kliesch, T.-T.; Janshoff, A.; Steinem, C. Orthogonal functionalization of nanoporous substrates: Control of 3D surface functionality ACS Appl. Mater. Interface 2011, 3, 1068-1076
    • (2011) ACS Appl. Mater. Interface , vol.3 , pp. 1068-1076
    • Lazzara, T.D.1    Kliesch, T.-T.2    Janshoff, A.3    Steinem, C.4
  • 29
    • 80053309394 scopus 로고    scopus 로고
    • Separating attoliter-sized compartments using fluid pore-spanning lipid bilayers
    • Lazzara, T. D.; Carnarius, C.; Kocun, M.; Janshoff, A.; Steinem, C. Separating attoliter-sized compartments using fluid pore-spanning lipid bilayers ACS Nano 2011, 5, 6935-6944
    • (2011) ACS Nano , vol.5 , pp. 6935-6944
    • Lazzara, T.D.1    Carnarius, C.2    Kocun, M.3    Janshoff, A.4    Steinem, C.5
  • 30
    • 57349141830 scopus 로고    scopus 로고
    • Nanopore-spanning lipid bilayers for controlled chemical release
    • Mager, M. D.; Melosh, N. A. Nanopore-spanning lipid bilayers for controlled chemical release Adv. Mater. 2008, 20, 4423-4427
    • (2008) Adv. Mater. , vol.20 , pp. 4423-4427
    • Mager, M.D.1    Melosh, N.A.2
  • 33
    • 34548526628 scopus 로고    scopus 로고
    • Micro-BLMs on highly ordered porous silicon substrates: Rupture process and lateral mobility
    • Weiskopf, D.; Schmitt, E. K.; Klühr, M. H.; Dertinger, S. K.; Steinem, C. Micro-BLMs on highly ordered porous silicon substrates: Rupture process and lateral mobility Langmuir 2007, 23, 9134-9139
    • (2007) Langmuir , vol.23 , pp. 9134-9139
    • Weiskopf, D.1    Schmitt, E.K.2    Klühr, M.H.3    Dertinger, S.K.4    Steinem, C.5
  • 35
    • 0026788013 scopus 로고
    • Mechanism of magainin 2a induced permeabilization of phospholipid vesicles
    • Grant, E.; Beeler, T. J.; Taylor, K. M. P.; Gable, K.; Roseman, M. A. Mechanism of magainin 2a induced permeabilization of phospholipid vesicles Biochemistry 1992, 31, 9912-9918
    • (1992) Biochemistry , vol.31 , pp. 9912-9918
    • Grant, E.1    Beeler, T.J.2    Taylor, K.M.P.3    Gable, K.4    Roseman, M.A.5
  • 36
    • 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. 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.3
  • 37
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • Almeida, P. 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.1    Pokorny, A.2
  • 38
    • 58149341606 scopus 로고    scopus 로고
    • Macromolecular crowding and size effects on probe microviscosity
    • Goins, A. B.; Sanabria, H.; Waxham, M. N. Macromolecular crowding and size effects on probe microviscosity Biophys. J. 2008, 95, 5362-5373
    • (2008) Biophys. J. , vol.95 , pp. 5362-5373
    • Goins, A.B.1    Sanabria, H.2    Waxham, M.N.3
  • 40
    • 34047270717 scopus 로고    scopus 로고
    • The response of giant phospholipid vesicles to pore-forming peptide melittin
    • Mally, M.; Majhenc, J.; Svetina, S.; Zeks, B. The response of giant phospholipid vesicles to pore-forming peptide melittin Biochim. Biophys. Acta 2007, 1768, 1179-1189
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1179-1189
    • Mally, M.1    Majhenc, J.2    Svetina, S.3    Zeks, B.4
  • 41
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee, M.-T.; Chen, F.-Y.; Huang, H. W. Energetics of pore formation induced by membrane active peptides Biochemistry 2004, 43, 3590-3599
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.-T.1    Chen, F.-Y.2    Huang, H.W.3
  • 42
    • 78649773506 scopus 로고    scopus 로고
    • Comparative study of the membrane-permeabilizing activities of mastoparans and related histamine-releasing agents in bacteria, erythrocytes, and mast cells
    • Nakao, S.; Komagoe, K.; Inoue, T.; Katsu, T. Comparative study of the membrane-permeabilizing activities of mastoparans and related histamine-releasing agents in bacteria, erythrocytes, and mast cells Biochim. Biophys. Acta 2011, 1808, 490-497
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 490-497
    • Nakao, S.1    Komagoe, K.2    Inoue, T.3    Katsu, T.4
  • 43
    • 77955542886 scopus 로고    scopus 로고
    • Mounted nanoporous anodic alumina thin films as planar optical waveguides
    • Lazzara, T. D.; Aaron Lau, K. H.; Knoll, W. Mounted nanoporous anodic alumina thin films as planar optical waveguides J. Nanosci. Nanotechnol. 2010, 10, 4293-4299
    • (2010) J. Nanosci. Nanotechnol. , vol.10 , pp. 4293-4299
    • Lazzara, T.D.1    Aaron Lau, K.H.2    Knoll, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.