메뉴 건너뛰기




Volumn 344, Issue 1, 2005, Pages 43-52

Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin

Author keywords

Biacore; Equinatoxin; L1 chip; Liposomes; Pore forming toxin

Indexed keywords

CALCIUM CHLORIDE; FLUORESCENCE; FLUORESCENCE MICROSCOPY; SURFACE PLASMON RESONANCE; TOXIC MATERIALS;

EID: 27644593434     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.06.013     Document Type: Article
Times cited : (79)

References (40)
  • 1
    • 11244313892 scopus 로고    scopus 로고
    • Survey of the year 2003 commercial optical biosensor literature
    • R.L. Rich, D.G. Myszka, Survey of the year 2003 commercial optical biosensor literature, J. Mol. Recogn. 18 (2005) 1-39.
    • (2005) J. Mol. Recogn. , vol.18 , pp. 1-39
    • Rich, R.L.1    Myszka, D.G.2
  • 2
    • 0035884406 scopus 로고    scopus 로고
    • Membrane binding assays for peripheral proteins
    • W. Cho, L. Bittova, R.V. Stahelin, Membrane binding assays for peripheral proteins, Anal. Biochem. 296 (2001) 153-161.
    • (2001) Anal. Biochem. , vol.296 , pp. 153-161
    • Cho, W.1    Bittova, L.2    Stahelin, R.V.3
  • 3
    • 0029857123 scopus 로고    scopus 로고
    • Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer
    • O. Stachowiak, M. Dolder, T. Wallimann, Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer, Biochemistry 35 (1996) 15522-15528.
    • (1996) Biochemistry , vol.35 , pp. 15522-15528
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3
  • 4
    • 0028208688 scopus 로고
    • Stable immobilization of lipid vesicles for kinetic studies using surface plasmon resonance
    • L. Masson, A. Mazza, R. Brousseau, Stable immobilization of lipid vesicles for kinetic studies using surface plasmon resonance, Anal. Biochem. 218 (1994) 405-412.
    • (1994) Anal. Biochem. , vol.218 , pp. 405-412
    • Masson, L.1    Mazza, A.2    Brousseau, R.3
  • 5
    • 0031041314 scopus 로고    scopus 로고
    • Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance
    • C.R. MacKenzie, T. Hirama, K.K. Lee, E. Altman, N.M. Young, Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance, J. Biol. Chem. 272 (1997) 5533-5538.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5533-5538
    • MacKenzie, C.R.1    Hirama, T.2    Lee, K.K.3    Altman, E.4    Young, N.M.5
  • 6
    • 0034650303 scopus 로고    scopus 로고
    • A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors
    • M.A. Cooper, A. Hansson, S. Lofas, D.H. Williams, A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors, Anal. Biochem. 277 (2000) 196-205.
    • (2000) Anal. Biochem. , vol.277 , pp. 196-205
    • Cooper, M.A.1    Hansson, A.2    Lofas, S.3    Williams, D.H.4
  • 7
    • 0034630369 scopus 로고    scopus 로고
    • Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip
    • E.M. Erb, X. Chen, S. Allen, C.J. Roberts, S.J. Tendler, M.C. Davies, S. Forsen, Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip, Anal. Biochem. 280 (2000) 29-35.
    • (2000) Anal. Biochem. , vol.280 , pp. 29-35
    • Erb, E.M.1    Chen, X.2    Allen, S.3    Roberts, C.J.4    Tendler, S.J.5    Davies, M.C.6    Forsen, S.7
  • 8
    • 0027595323 scopus 로고
    • Protein binding to supported lipid membranes: Investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance
    • S. Terrettaz, T. Stora, C. Duschl, H. Vogel, Protein binding to supported lipid membranes: investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance, Langmuir 9 (1993) 1361-1369.
    • (1993) Langmuir , vol.9 , pp. 1361-1369
    • Terrettaz, S.1    Stora, T.2    Duschl, C.3    Vogel, H.4
  • 10
    • 0036853993 scopus 로고    scopus 로고
    • Surface plasmon resonance characterization of drug/liposome interactions
    • C.L. Baird, E.S. Courtenay, D.G. Myszka, Surface plasmon resonance characterization of drug/liposome interactions, Anal. Biochem. 310 (2002) 93-99.
    • (2002) Anal. Biochem. , vol.310 , pp. 93-99
    • Baird, C.L.1    Courtenay, E.S.2    Myszka, D.G.3
  • 11
    • 0036391231 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy: An emerging tool for the study of peptide-membrane interactions
    • H. Mozsolits, M.I. Aguilar, Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions, Biopolymers 66 (2002) 3-18.
    • (2002) Biopolymers , vol.66 , pp. 3-18
    • Mozsolits, H.1    Aguilar, M.I.2
  • 12
    • 0242380675 scopus 로고    scopus 로고
    • Peeking into a secret world of pore-forming toxins: Membrane binding processes studied by surface plasmon resonance
    • G. Anderluh, P. Macek, J.H. Lakey, Peeking into a secret world of pore-forming toxins: membrane binding processes studied by surface plasmon resonance, Toxicon 42 (2003) 225-228.
    • (2003) Toxicon , vol.42 , pp. 225-228
    • Anderluh, G.1    Macek, P.2    Lakey, J.H.3
  • 13
    • 0037326012 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy in the study of membrane-mediated cell signalling
    • H. Mozsolits, W.G. Thomas, M.I. Aguilar, Surface plasmon resonance spectroscopy in the study of membrane-mediated cell signalling, J. Pept. Sci. 9 (2003) 77-89.
    • (2003) J. Pept. Sci. , vol.9 , pp. 77-89
    • Mozsolits, H.1    Thomas, W.G.2    Aguilar, M.I.3
  • 14
    • 12244269069 scopus 로고    scopus 로고
    • Biosensor analysis of the interaction between drug compounds and liposomes of different properties: A two-dimensional characterization tool for estimation of membrane absorption
    • A. Frostell-Karlsson, H. Widegren, C.E. Green, M.D. Hamalainen, L. Westerlund, R. Karlsson, K. Fenner, W.H. van de Waterbeemd, Biosensor analysis of the interaction between drug compounds and liposomes of different properties: a two-dimensional characterization tool for estimation of membrane absorption, J. Pharm. Sci. 94 (2005) 25-37.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 25-37
    • Frostell-Karlsson, A.1    Widegren, H.2    Green, C.E.3    Hamalainen, M.D.4    Westerlund, L.5    Karlsson, R.6    Fenner, K.7    Van De Waterbeemd, W.H.8
  • 15
    • 2142767300 scopus 로고    scopus 로고
    • Probing the mechanism of drug/lipid membrane interactions using Biacore
    • Y.N. Abdiche, D.G. Myszka,c, Probing the mechanism of drug/lipid membrane interactions using Biacore, Anal. Biochem. 328 (2004) 233-243.
    • (2004) Anal. Biochem. , vol.328 , pp. 233-243
    • Abdiche, Y.N.1    Myszka, D.G.2
  • 16
    • 0034213343 scopus 로고    scopus 로고
    • SPR biosensor studies of the direct interaction between 27 drugs and a liposome surface: Correlation with fraction absorbed in humans
    • E. Danelian, A. Karlen, R. Karlsson, S. Winiwarter, A. Hansson, S. Lofas, H. Lennernas, M.D. Hamalainen, SPR biosensor studies of the direct interaction between 27 drugs and a liposome surface: correlation with fraction absorbed in humans, J. Med. Chem. 43 (2000) 2083-2086.
    • (2000) J. Med. Chem. , vol.43 , pp. 2083-2086
    • Danelian, E.1    Karlen, A.2    Karlsson, R.3    Winiwarter, S.4    Hansson, A.5    Lofas, S.6    Lennernas, H.7    Hamalainen, M.D.8
  • 17
    • 0023895943 scopus 로고
    • Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L
    • P. Maček, D. Lebez, Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L, Toxicon 26 (1988) 441-451.
    • (1988) Toxicon , vol.26 , pp. 441-451
    • Maček, P.1    Lebez, D.2
  • 18
    • 0038604282 scopus 로고    scopus 로고
    • A novel mechanism of pore formation: Membrane penetration by the N-terminal amphipathic region of equinatoxin
    • P. Malovrh, G. Viero, M. Dalla Serra, Z. Podlesek, J.H. Lakey, P. Maček, G. Menestrina, G. Anderluh, A novel mechanism of pore formation: membrane penetration by the N-terminal amphipathic region of equinatoxin, J. Biol. Chem. 278 (2003) 22678-22685.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22678-22685
    • Malovrh, P.1    Viero, G.2    Podlesek, Z.3    Lakey, J.H.4    Maček, P.5    Menestrina, G.6    Anderluh, G.7
  • 20
    • 12644291218 scopus 로고    scopus 로고
    • Mechanism of membrane permeabilisation by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus
    • M. Tejuca, M. Dalla Serra, M. Ferreras, M.E. Lanio, G. Menestrina, Mechanism of membrane permeabilisation by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus, Biochemistry 35 (1996) 14947-14957.
    • (1996) Biochemistry , vol.35 , pp. 14947-14957
    • Tejuca, M.1    Dalla Serra, M.2    Ferreras, M.3    Lanio, M.E.4    Menestrina, G.5
  • 21
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus
    • C.A. Valcarcel, M. Dalla Serra, C. Potrich, I. Bernhart, M. Tejuca, D. Martinez, F. Pazos, M.E. Lanio, G. Menestrina, Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus, Biophys. J. 80 (2001) 2761-2774.
    • (2001) Biophys. J. , vol.80 , pp. 2761-2774
    • Valcarcel, C.A.1    Dalla Serra, M.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martinez, D.6    Pazos, F.7    Lanio, M.E.8    Menestrina, G.9
  • 22
    • 0037663875 scopus 로고    scopus 로고
    • National Institutes of Health, Bethesda, MD
    • W.S. Rasband, Image J, National Institutes of Health, Bethesda, MD, 1997-2005.
    • (1997) Image J
    • Rasband, W.S.1
  • 23
    • 0242317915 scopus 로고    scopus 로고
    • Liposomes in the study of pore-forming toxins
    • M. Dalla Serra, G. Menestrina, Liposomes in the study of pore-forming toxins, Methods Enzymol. 372 (2003) 99-124.
    • (2003) Methods Enzymol. , vol.372 , pp. 99-124
    • Dalla Serra, M.1    Menestrina, G.2
  • 24
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • G. Anderluh, P. Maček, Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria), Toxicon 40 (2002) 111-124.
    • (2002) Toxicon , vol.40 , pp. 111-124
    • Anderluh, G.1    Maček, P.2
  • 25
    • 0027398335 scopus 로고
    • Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes
    • G. Belmonte, C. Pederzolli, P. Maček, G. Menestrina, Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes, J. Membrane Biol. 131 (1993) 11-22.
    • (1993) J. Membrane Biol. , vol.131 , pp. 11-22
    • Belmonte, G.1    Pederzolli, C.2    Maček, P.3    Menestrina, G.4
  • 26
    • 0028810511 scopus 로고
    • Intrinsic tryptophan fluorescence of equinatoxin II, a pore-forming polypeptide from the sea anemone Actinia equina L, monitors its interaction with lipid membranes
    • P. Maček, M. Zecchini, C. Pederzolli, M. Dalla Serra, G. Menestrina, Intrinsic tryptophan fluorescence of equinatoxin II, a pore-forming polypeptide from the sea anemone Actinia equina L, monitors its interaction with lipid membranes, Eur. J. Biochem. 234 (1995) 329-335.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 329-335
    • Maček, P.1    Zecchini, M.2    Pederzolli, C.3    Dalla Serra, M.4    Menestrina, G.5
  • 27
    • 0029818018 scopus 로고    scopus 로고
    • Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy
    • M.J. Citraand, P.H. Axelsen, Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy, Biophys. J. 71 (1996) 1796-1805.
    • (1996) Biophys. J. , vol.71 , pp. 1796-1805
    • Citraand, M.J.1    Axelsen, P.H.2
  • 28
    • 0023657247 scopus 로고
    • Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and delta-hemolysin with phosphatidylcholines
    • J.W. Brauner, R. Mendelsohn, F.G. Prendergast, Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and delta-hemolysin with phosphatidylcholines, Biochemistry 26 (1987) 8151-8158.
    • (1987) Biochemistry , vol.26 , pp. 8151-8158
    • Brauner, J.W.1    Mendelsohn, R.2    Prendergast, F.G.3
  • 29
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers: A polarized attenuated total reflection infrared study
    • S. Frey, L.K. Tamm, Orientation of melittin in phospholipid bilayers: a polarized attenuated total reflection infrared study, Biophys. J. 60 (1991) 922-930.
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 30
    • 0032906668 scopus 로고    scopus 로고
    • Quantitative orientation measurements in thin lipid films by attenuated total reflection infrared spectroscopy
    • F. Picard, T. Buffeteau, B. Desbat, M. Auger, M. Pezolet, Quantitative orientation measurements in thin lipid films by attenuated total reflection infrared spectroscopy, Biophys. J. 76 (1999) 539-551.
    • (1999) Biophys. J. , vol.76 , pp. 539-551
    • Picard, F.1    Buffeteau, T.2    Desbat, B.3    Auger, M.4    Pezolet, M.5
  • 31
    • 2542516405 scopus 로고    scopus 로고
    • The density and refractive index of adsorbing protein layers
    • J. Voros, The density and refractive index of adsorbing protein layers, Biophys. J. 87 (2004) 553-561.
    • (2004) Biophys. J. , vol.87 , pp. 553-561
    • Voros, J.1
  • 34
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • S.C. Hinnah, K. Hill, R. Wagner, T. Schlicher, J. Soll, Reconstitution of a chloroplast protein import channel, EMBO J. 16 (1997) 7351-7360.
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 35
    • 0035901553 scopus 로고    scopus 로고
    • Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: A surface plasmon resonance study on phospholipases A2
    • R.V. Stahelin, W. Cho, Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2, Biochemistry 40 (2001) 4672-4678.
    • (2001) Biochemistry , vol.40 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 36
    • 11844280405 scopus 로고    scopus 로고
    • Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance
    • H. Kamimoria, K. Halla, D.J. Craick, M.-I. Aguilar, Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance, Anal. Biochem. 337 (2005) 149-153.
    • (2005) Anal. Biochem. , vol.337 , pp. 149-153
    • Kamimoria, H.1    Halla, K.2    Craick, D.J.3    Aguilar, M.-I.4
  • 37
    • 23644439970 scopus 로고    scopus 로고
    • Membrane binding of β2-glycoprotein I can be described by a two-state reaction model: An atomic force microscopy and surface plasmon resonance study
    • doi:10.1042/BJ20050156
    • R. Gamsjaeger, A. Johs, A. Gries, H.J. Gruber, C. Romanin, R. Prassl, P. Hinterdorfer, Membrane binding of β2-glycoprotein I can be described by a two-state reaction model: an atomic force microscopy and surface plasmon resonance study, Biochem. J. (2005), doi:10.1042/BJ20050156.
    • (2005) Biochem. J.
    • Gamsjaeger, R.1    Johs, A.2    Gries, A.3    Gruber, H.J.4    Romanin, C.5    Prassl, R.6    Hinterdorfer, P.7
  • 38
    • 0004273681 scopus 로고
    • Oxford University Press, Oxford, UK
    • R.R.C. New (Ed.), Liposomes: A Practical Approach, Oxford University Press, Oxford, UK, 1990.
    • (1990) Liposomes: A Practical Approach
  • 39
    • 5644251808 scopus 로고    scopus 로고
    • Real time analysis of intact organelles using surface plasmon resonance
    • G. Ferracci, M. Seagar, C. Joel, R. Miquelis, C. Leveque, Real time analysis of intact organelles using surface plasmon resonance, Anal. Biochem. 334 (2004) 367-375.
    • (2004) Anal. Biochem. , vol.334 , pp. 367-375
    • Ferracci, G.1    Seagar, M.2    Joel, C.3    Miquelis, R.4    Leveque, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.