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Volumn 1808, Issue 11, 2011, Pages 2646-2655

Nanoscale structural and mechanical effects of beta-amyloid (1-42) on polymer cushioned membranes: A combined study by neutron reflectometry and AFM Force Spectroscopy

Author keywords

Beta amyloid; Force spectroscopy; Lipid bilayer; Neutron reflectivity; Polymer cushion

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; POLYMER;

EID: 80052273046     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.024     Document Type: Article
Times cited : (42)

References (46)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • D.J. Selkoe The molecular pathology of Alzheimer's disease Neuron 6 1991 487 498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • D.M. Walsh, and D.J. Selkoe A beta oligomers - a decade of discovery J. Neurochem. 101 2007 1172 1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 4
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DOI 10.1074/jbc.M500997200
    • A. Demuro, E. Mina, R. Kayed, S.C. Milton, I. Parker, and C.G. Glabe Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers J. Biol. Chem. 280 2005 17294 17300 (Pubitemid 41389198)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 5
    • 38349120748 scopus 로고    scopus 로고
    • Membrane fusogenic activity of the Alzheimer's peptide A beta(1-42) demonstrated by small-angle neutron scattering
    • S. Dante, T. Hauss, A. Brandt, and N.A. Dencher Membrane fusogenic activity of the Alzheimer's peptide A beta(1-42) demonstrated by small-angle neutron scattering J. Mol. Biol. 376 2008 393 404
    • (2008) J. Mol. Biol. , vol.376 , pp. 393-404
    • Dante, S.1    Hauss, T.2    Brandt, A.3    Dencher, N.A.4
  • 6
    • 0036019210 scopus 로고    scopus 로고
    • Abeta42-peptide assembly on lipid bilayers
    • C.M. Yip, A.A. Darabie, and J. McLaurin Abeta42-peptide assembly on lipid bilayers J. Mol. Biol. 318 2002 97 107
    • (2002) J. Mol. Biol. , vol.318 , pp. 97-107
    • Yip, C.M.1    Darabie, A.A.2    McLaurin, J.3
  • 7
    • 0036842021 scopus 로고    scopus 로고
    • β-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents
    • S. Dante, T. Hauss, and N.A. Dencher beta-Amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents Biophys. J. 83 2002 2610 2616 (Pubitemid 35265754)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2610-2616
    • Dante, S.1    Hauss, T.2    Dencher, N.A.3
  • 8
    • 0344823652 scopus 로고    scopus 로고
    • Insertion of Externally Administered Amyloid β Peptide 25-35 and Perturbation of Lipid Bilayers
    • DOI 10.1021/bi035056v
    • S. Dante, T. Hauss, and N.A. Dencher Insertion of externally administered amyloid beta peptide 25-35 and perturbation of lipid bilayers Biochemistry-Us 42 2003 13667 13672 (Pubitemid 37444917)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13667-13672
    • Dante, S.1    Hauss, T.2    Dencher, N.A.3
  • 10
    • 77955658694 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta peptide analogue alters the ps-dynamics of phospholipid membranes
    • A. Buchsteiner, T. Hauss, S. Dante, and N.A. Dencher Alzheimer's disease amyloid-beta peptide analogue alters the ps-dynamics of phospholipid membranes Biochim. Biophys. Acta-Biomembranes 1798 2010 1969 1976
    • (2010) Biochim. Biophys. Acta-Biomembranes , vol.1798 , pp. 1969-1976
    • Buchsteiner, A.1    Hauss, T.2    Dante, S.3    Dencher, N.A.4
  • 12
    • 0032816938 scopus 로고    scopus 로고
    • Polymer-cushioned bilayers. I. A structural study of various preparation methods using neutron reflectometry
    • J.Y. Wong, J. Majewski, M. Seitz, C.K. Park, J.N. Israelachvili, and G.S. Smith Polymer-cushioned bilayers. I. A structural study of various preparation methods using neutron reflectometry Biophys. J. 77 1999 1445 1457 (Pubitemid 29407317)
    • (1999) Biophysical Journal , vol.77 , Issue.3 , pp. 1445-1457
    • Wong, J.Y.1    Majewski, J.2    Seitz, M.3    Park, C.K.4    Israelachvili, J.N.5    Smith, G.S.6
  • 13
    • 0032817223 scopus 로고    scopus 로고
    • Polymer-cushioned bilayers. II. An investigation of interaction forces and fusion using the surface forces apparatus
    • J.Y. Wong, C.K. Park, M. Seitz, and J. Israelachvili Polymer-cushioned bilayers. II. An investigation of interaction forces and fusion using the surface forces apparatus Biophys. J. 77 1999 1458 1468
    • (1999) Biophys. J. , vol.77 , pp. 1458-1468
    • Wong, J.Y.1    Park, C.K.2    Seitz, M.3    Israelachvili, J.4
  • 14
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • K. Jacobson, E.D. Sheets, and R. Simson Revisiting the fluid mosaic model of membranes Science 268 1995 1441 1442
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 15
  • 16
    • 0030848621 scopus 로고    scopus 로고
    • Fuzzy nanoassemblies: Toward layered polymeric multicomposites
    • DOI 10.1126/science.277.5330.1232
    • G. Decher Fuzzy nanoassemblies: toward layered polymeric multicomposites Science 277 1997 1232 1237 (Pubitemid 27449063)
    • (1997) Science , vol.277 , Issue.5330 , pp. 1232-1237
    • Decher, G.1
  • 18
    • 0026512750 scopus 로고
    • Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers
    • E. Kalb, S. Frey, and L.K. Tamm Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers Biochim. Biophys. Acta 1103 1992 307 316
    • (1992) Biochim. Biophys. Acta , vol.1103 , pp. 307-316
    • Kalb, E.1    Frey, S.2    Tamm, L.K.3
  • 19
    • 0035962950 scopus 로고    scopus 로고
    • Neutron reflectivity at the solid/liquid interface: Examples of applications in biophysics
    • DOI 10.1088/0953-8984/13/21/322, PII S0953898401209084
    • G. Fragneto-Cusani Neutron reflectivity at the solid/liquid interface: examples of applications in biophysics J. Phys. Condens. Matter 13 2001 4973 4989 (Pubitemid 32527855)
    • (2001) Journal of Physics Condensed Matter , vol.13 , Issue.21 , pp. 4973-4989
    • Fragneto-Cusani, G.1
  • 20
    • 0035014204 scopus 로고    scopus 로고
    • Neutron reflection from interfaces with biological and biomimetic materials
    • DOI 10.1016/S1359-0294(01)00073-5, PII S1359029401000735
    • S. Krueger Neutron reflection from interfaces with biological and biomimetic materials Curr. Opin. Colloid Interface Sci. 6 2001 111 117 (Pubitemid 32447570)
    • (2001) Current Opinion in Colloid and Interface Science , vol.6 , Issue.2 , pp. 111-117
    • Krueger, S.1
  • 22
    • 33744797922 scopus 로고    scopus 로고
    • Reversible activation of diblock copolymer monolayers at the interface by pH modulation, 1: Lateral chain density and conformation
    • DOI 10.1021/jp054532j
    • F. Rehfeldt, R. Steitz, S.P. Armes, R. Von Klitzing, A.P. Gast, and M. Tanaka Reversible activation of diblock copolymer monolayers at the interface by pH modulation, 1: lateral chain density and conformation J. Phys. Chem. B 110 2006 9171 9176 (Pubitemid 43829011)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.18 , pp. 9171-9176
    • Rehfeldt, F.1    Steitz, R.2    Armes, S.P.3    Von Klitzing, R.4    Gast, A.P.5    Tanaka, M.6
  • 23
    • 33750395101 scopus 로고    scopus 로고
    • Semi-active suspension control using "fast" model-predictive techniques
    • DOI 10.1109/TCST.2006.880196
    • M. Canale, M. Milanese, and C. Novara Semi-active suspension control using "fast" model-predictive techniques IEEE Trans. Control Syst. Technol. 14 2006 1034 1046 (Pubitemid 44637619)
    • (2006) IEEE Transactions on Control Systems Technology , vol.14 , Issue.6 , pp. 1034-1046
    • Canale, M.1    Milanese, M.2    Novara, C.3
  • 24
    • 34547181885 scopus 로고    scopus 로고
    • Raft domain reorganization driven by short- and long-chain ceramide: A combined AFM and FCS study
    • DOI 10.1021/la7010919
    • S. Chiantia, N. Kahya, and P. Schwille Raft domain reorganization driven by short- and long-chain ceramide: a combined AFM and FCS study Langmuir 23 2007 7659 7665 (Pubitemid 47116430)
    • (2007) Langmuir , vol.23 , Issue.14 , pp. 7659-7665
    • Chiantia, S.1    Kahya, N.2    Schwille, P.3
  • 25
    • 0035118736 scopus 로고    scopus 로고
    • Amyloid-β peptide assembly: A critical step in fibrillogenesis and membrane disruption
    • C.M. Yip, and J. McLaurin Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption Biophys. J. 80 2001 1359 1371 (Pubitemid 32182160)
    • (2001) Biophysical Journal , vol.80 , Issue.3 , pp. 1359-1371
    • Yip, C.M.1    McLaurin, J.2
  • 26
    • 0031551394 scopus 로고    scopus 로고
    • Nanometer-scale surface properties of mixed phospholipid monolayers and bilayers
    • Y.F. Dufrene, W.R. Barger, J.B.D. Green, and G.U. Lee Nanometer-scale surface properties of mixed phospholipid monolayers and bilayers Langmuir 13 1997 4779 4784 (Pubitemid 127591876)
    • (1997) Langmuir , vol.13 , Issue.18 , pp. 4779-4784
    • Dufrene, Y.F.1    Barger, W.R.2    Green, J.-B.D.3    Lee, G.U.4
  • 27
    • 78649468166 scopus 로고    scopus 로고
    • Direct characterization of mixed phospholipid/glycolipid bilayers with chemically-functionalized AFM probes
    • Y.F. Dufrene, W.R. Barger, and G.U. Lee Direct characterization of mixed phospholipid/glycolipid bilayers with chemically-functionalized AFM probes Biophys. J. 74 1998 A330 A
    • (1998) Biophys. J. , vol.74
    • Dufrene, Y.F.1    Barger, W.R.2    Lee, G.U.3
  • 28
    • 0036132263 scopus 로고    scopus 로고
    • Tip penetration through lipid bilayers in atomic force microscopy
    • DOI 10.1016/S0927-7765(01)00254-5, PII S0927776501002545
    • V. Franz, S. Loi, H. Muller, E. Bamberg, and H.H. Butt Tip penetration through lipid bilayers in atomic force microscopy Colloids Surf. B Biointerfaces 23 2002 191 200 (Pubitemid 33115230)
    • (2002) Colloids and Surfaces B: Biointerfaces , vol.23 , Issue.2-3 , pp. 191-200
    • Franz, V.1    Loi, S.2    Muller, H.3    Bamberg, E.4    Butt, H.-J.5
  • 29
    • 78649490368 scopus 로고    scopus 로고
    • Force spectroscopy as a tool to investigate solid supported lipid membranes
    • C. Canale, M. Jacono, A. Diaspro, and S. Dante Force spectroscopy as a tool to investigate solid supported lipid membranes Microsc. Res. Tech. 73 2010 965 974
    • (2010) Microsc. Res. Tech. , vol.73 , pp. 965-974
    • Canale, C.1    Jacono, M.2    Diaspro, A.3    Dante, S.4
  • 32
    • 84986841299 scopus 로고
    • Buildup of Ultrathin multilayer films by a self-assembly process 1. Consecutive adsorption of anionic and cationic bipolar amphiphiles on charged surfaces
    • G. Decher, and J.D. Hong Buildup of Ultrathin multilayer films by a self-assembly process 1. Consecutive adsorption of anionic and cationic bipolar amphiphiles on charged surfaces Makromol. Chem. Macromol. Symp. 46 1991 321 327
    • (1991) Makromol. Chem. Macromol. Symp. , vol.46 , pp. 321-327
    • Decher, G.1    Hong, J.D.2
  • 33
    • 24944503493 scopus 로고    scopus 로고
    • Formation of polyelectrolyte multilayer architectures with embedded DMPC studied in situ by neutron reflectometry
    • DOI 10.1021/la050407n
    • C. Delajon, T. Gutberlet, R. Steitz, H. Mohwald, and R. Krastev Formation of poly, electrolyte multilayer architectures with embedded DMPC studied in situ by neutron reflectometry Langmuir 21 2005 8509 8514 (Pubitemid 41321832)
    • (2005) Langmuir , vol.21 , Issue.18 , pp. 8509-8514
    • Delajon, C.1    Gutberlet, T.2    Steitz, R.3    Mohwald, H.4    Krastev, R.5
  • 34
    • 0343340047 scopus 로고    scopus 로고
    • Influence of the ionic strength on the structure of polyelectrolyte films at the solid/liquid interface
    • DOI 10.1016/S0927-7757(99)00431-8, PII S0927775799004318
    • R. Steitz, V. Leiner, R. Siebrecht, and R. von Klitzing Influence of the ionic strength on the structure of polyelectrolyte films at the solid/liquid interface Colloids Surf. A-Physicochem. Eng. Aspects 163 2000 63 70 (Pubitemid 30017873)
    • (2000) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.163 , Issue.1 , pp. 63-70
    • Steitz, R.1    Leiner, V.2    Siebrecht, R.3    V. Klitzing, R.4
  • 35
    • 74049122589 scopus 로고    scopus 로고
    • Specific ion versus electrostatic effects on the construction of polyelectrolyte multilayers
    • J.E. Wong, H. Zastrow, W. Jaeger, and R. von Klitzing Specific ion versus electrostatic effects on the construction of polyelectrolyte multilayers Langmuir 25 2009 14061 14070
    • (2009) Langmuir , vol.25 , pp. 14061-14070
    • Wong, J.E.1    Zastrow, H.2    Jaeger, W.3    Von Klitzing, R.4
  • 36
    • 33646388001 scopus 로고    scopus 로고
    • Surface interactions during polyelectrolyte multilayer build-up. 2. The effect of ionic strength on the structure of preformed multilayers
    • E. Blomberg, E. Poptoshev, and F. Caruso Surface interactions during polyelectrolyte multilayer build-up. 2. The effect of ionic strength on the structure of preformed multilayers Langmuir 22 2006 4153 4157
    • (2006) Langmuir , vol.22 , pp. 4153-4157
    • Blomberg, E.1    Poptoshev, E.2    Caruso, F.3
  • 37
    • 63449122484 scopus 로고    scopus 로고
    • Lipid layers on polyelectrolyte multilayer supports
    • M. Fischlechner Lipid layers on polyelectrolyte multilayer supports Soft Matter 4 2008 2245 2258
    • (2008) Soft Matter , vol.4 , pp. 2245-2258
    • Fischlechner, M.1
  • 39
    • 79957527414 scopus 로고    scopus 로고
    • Polymorphism of amyloid beta peptide in different environments: Implications for membrane insertion and pore formation
    • R. Nussinov, F.T. Arce, H.B. Jang, S. Ramachandran, P.B. Landon, and R. Lal Polymorphism of amyloid beta peptide in different environments: implications for membrane insertion and pore formation Soft Matter 7 2011 5267 5273
    • (2011) Soft Matter , vol.7 , pp. 5267-5273
    • Nussinov, R.1    Arce, F.T.2    Jang, H.B.3    Ramachandran, S.4    Landon, P.B.5    Lal, R.6
  • 41
    • 34547156274 scopus 로고    scopus 로고
    • Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
    • DOI 10.1016/j.bbamem.2006.12.014, PII S0005273606004913
    • R.M. Murphy Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins Biochim. Biophys. Acta 1768 2007 1923 1934 (Pubitemid 47125847)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1923-1934
    • Murphy, R.M.1
  • 42
    • 33845406090 scopus 로고    scopus 로고
    • Preferential accumulation of Aβ(1-42) on gel phase domains of lipid bilayers: An AFM and fluorescence study
    • DOI 10.1016/j.bbamem.2006.09.005, PII S0005273606003336
    • A. Choucair, M. Chakrapani, B. Chakravarthy, J. Katsaras, and L.J. Johnston Preferential accumulation of A beta(1-42) on gel phase domains of lipid bilayers: an AFM and fluorescence study Biochim. Biophys. Acta-Biomembranes 1768 2007 146 154 (Pubitemid 44909080)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.1 , pp. 146-154
    • Choucair, A.1    Chakrapani, M.2    Chakravarthy, B.3    Katsaras, J.4    Johnston, L.J.5
  • 43
    • 58149277415 scopus 로고    scopus 로고
    • Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: Implications for cell toxicity
    • G. Valincius, F. Heinrich, R. Budvytyte, D.J. Vanderah, D.J. McGillivray, Y. Sokolov, J.E. Hall, and M. Losche Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity Biophys. J. 95 2008 4845 4861
    • (2008) Biophys. J. , vol.95 , pp. 4845-4861
    • Valincius, G.1    Heinrich, F.2    Budvytyte, R.3    Vanderah, D.J.4    McGillivray, D.J.5    Sokolov, Y.6    Hall, J.E.7    Losche, M.8
  • 44
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • B. Jacrot The study of biological structures by neutron scattering from solution Rep. Prog. Phys. 39 1976 911 953
    • (1976) Rep. Prog. Phys. , vol.39 , pp. 911-953
    • Jacrot, B.1
  • 45
    • 77957905232 scopus 로고    scopus 로고
    • Aggregation structure of Alzheimer amyloid-beta(1-40) peptide with sodium dodecyl sulfate as revealed by small-angle X-ray and neutron scattering
    • T.L. Lin, J.M. Lin, U.S. Jeng, Z.H. Huang, and Y.S. Huang Aggregation structure of Alzheimer amyloid-beta(1-40) peptide with sodium dodecyl sulfate as revealed by small-angle X-ray and neutron scattering Soft Matter 5 2009 3913 3919
    • (2009) Soft Matter , vol.5 , pp. 3913-3919
    • Lin, T.L.1    Lin, J.M.2    Jeng, U.S.3    Huang, Z.H.4    Huang, Y.S.5
  • 46
    • 0033061633 scopus 로고    scopus 로고
    • Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex
    • S.W. Chiu, S. Subramaniam, and E. Jakobsson Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex Biophys. J. 76 1999 1929 1938 (Pubitemid 29266350)
    • (1999) Biophysical Journal , vol.76 , Issue.4 , pp. 1929-1938
    • Chiu, S.-W.1    Subramaniam, S.2    Jakobsson, E.3


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