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Volumn 168, Issue 1, 2009, Pages 117-124

Conformation and topology of amyloid β-protein adsorbed on a tethered artificial membrane probed by surface plasmon field-enhanced fluorescence spectroscopy

Author keywords

Alzheimer's disease (AD); Amyloid peptide (A ); Immunoassay; Melatonin; SPFS; SPS

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN; MELATONIN; MONOCLONAL ANTIBODY; PEPTIDE;

EID: 69249213873     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.06.020     Document Type: Article
Times cited : (8)

References (35)
  • 3
    • 3442899664 scopus 로고    scopus 로고
    • Beta-sheet breakers for Alzheimer's disease therapy
    • Bieler S., and Soto C. Beta-sheet breakers for Alzheimer's disease therapy. Curr. Drug Targets 5 (2004) 553-558
    • (2004) Curr. Drug Targets , vol.5 , pp. 553-558
    • Bieler, S.1    Soto, C.2
  • 4
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J., Lorenzo A., and Yankner B.A. Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging Neurobiol. Aging 13 (1992) 609-612
    • (1992) Neurobiol. Aging Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 5
    • 0028986916 scopus 로고
    • β-Amyloid fibrils induce tau-phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., and Yankner B.A. β-Amyloid fibrils induce tau-phosphorylation and loss of microtubule binding. Neuron 14 (1995) 879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 8
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity
    • Geula C., Wu C.K., Saroff D., Lorenzo A., Yuan M.L., and Yankner B.A. Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity. Nat. Med. 4 (1998) 827-831
    • (1998) Nat. Med. , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.L.5    Yankner, B.A.6
  • 9
    • 0017532312 scopus 로고
    • The effect of thin organic films on the surface plasma resonance on gold
    • Gordon J.G., and Swalen J.D. The effect of thin organic films on the surface plasma resonance on gold. Optics Commun. 22 (1977) 374-376
    • (1977) Optics Commun. , vol.22 , pp. 374-376
    • Gordon, J.G.1    Swalen, J.D.2
  • 11
    • 84880187014 scopus 로고    scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis: an update and reappraisal
    • Hardy J. Alzheimer's disease: the amyloid cascade hypothesis: an update and reappraisal. J. Alzheimers Dis. 9 (2006) 151-153
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 151-153
    • Hardy, J.1
  • 12
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartly D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., Teplow D.B., and Selkoe D.J. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartly, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 13
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation
    • Ji S.R., Wu Y., and Sui S.F. Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277 (2002) 6273-6279
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 14
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276 (2001) 24985-24990
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 15
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 41 (2002) 7385-7390
    • (2002) Biochemistry , vol.41 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 16
    • 0037418703 scopus 로고    scopus 로고
    • Fullerene inhibits β-amyloid peptide aggregation
    • Kim J.E., and Lee M.Y. Fullerene inhibits β-amyloid peptide aggregation. Biochem. Biophys. Res. Commun. 303 (2003) 576-579
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 576-579
    • Kim, J.E.1    Lee, M.Y.2
  • 17
    • 5144219996 scopus 로고    scopus 로고
    • Supramolecular interfacial architectures for optical biosensing with surface plasmons
    • Knoll W., Park H., Sinner E.K., Yao D., and Yu F. Supramolecular interfacial architectures for optical biosensing with surface plasmons. Surf. Sci. 570 (2004) 30-42
    • (2004) Surf. Sci. , vol.570 , pp. 30-42
    • Knoll, W.1    Park, H.2    Sinner, E.K.3    Yao, D.4    Yu, F.5
  • 19
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, Prion, and HIV-1 Proteins
    • Mahfoud R., Garmy N., Maresca M., Yahi N., Puigserver A., and Fantini J. Identification of a common sphingolipid-binding domain in Alzheimer, Prion, and HIV-1 Proteins. J. Biol. Chem. 277 (2002) 11292-11296
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 20
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes
    • McLaurin J., and Chakrabartty A. Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes. European Journal of Biochemistry/FEBS 245 2 (1997) 355-363
    • (1997) European Journal of Biochemistry/FEBS , vol.245 , Issue.2 , pp. 355-363
    • McLaurin, J.1    Chakrabartty, A.2
  • 21
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., and Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosc. 6 1 (2005) 11-22
    • (2005) Nat. Rev. Neurosc. , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 22
    • 34547473731 scopus 로고    scopus 로고
    • Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice
    • Muhs A., Hickman D.T., Pihlgren M., Chuard N., et al. Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice. PNAS 104 (2007) 9810-9815
    • (2007) PNAS , vol.104 , pp. 9810-9815
    • Muhs, A.1    Hickman, D.T.2    Pihlgren, M.3    Chuard, N.4
  • 24
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., and Cotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13 (1993) 1676-1687
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 26
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe D.J. The cell biology of amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8 (1998) 447-453
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 28
    • 69249228490 scopus 로고
    • Interaction of the aromatic hormone melatonin with lipid-membranes
    • Shida C.S., Costa E.X., Ito A.S., and Lamyfreund M.T. Interaction of the aromatic hormone melatonin with lipid-membranes. Biophys. J. 66 (1994) A57
    • (1994) Biophys. J. , vol.66
    • Shida, C.S.1    Costa, E.X.2    Ito, A.S.3    Lamyfreund, M.T.4
  • 29
    • 0025063656 scopus 로고
    • Daily variation in the concentration of melatonin and 5-methoxytryptophol in the human pineal gland: effect of age and Alzheimer's disease
    • Skene D.J., Vivien-Roels B., Sparks D.L., Hunsaker J.C., Pévet P., Ravid D., and Swaab D.F. Daily variation in the concentration of melatonin and 5-methoxytryptophol in the human pineal gland: effect of age and Alzheimer's disease. Brain Res. 528 (1990) 170-174
    • (1990) Brain Res. , vol.528 , pp. 170-174
    • Skene, D.J.1    Vivien-Roels, B.2    Sparks, D.L.3    Hunsaker, J.C.4    Pévet, P.5    Ravid, D.6    Swaab, D.F.7
  • 30
    • 0035200670 scopus 로고    scopus 로고
    • Interaction between synthetic amyloid-β-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry
    • Skribanek Z., Baláspiri L., and Mák M. Interaction between synthetic amyloid-β-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry. J. Mass Spectrom. 36 (2001) 1226-1229
    • (2001) J. Mass Spectrom. , vol.36 , pp. 1226-1229
    • Skribanek, Z.1    Baláspiri, L.2    Mák, M.3
  • 31
    • 85159087573 scopus 로고    scopus 로고
    • Peptide-tethered bilayer lipid membranes and their interaction with amyloid beta-peptide
    • Song H., Sinner E.K., and Knoll W. Peptide-tethered bilayer lipid membranes and their interaction with amyloid beta-peptide. Biointerphases 2 (2007) 151-158
    • (2007) Biointerphases , vol.2 , pp. 151-158
    • Song, H.1    Sinner, E.K.2    Knoll, W.3
  • 34
    • 0038616312 scopus 로고    scopus 로고
    • Surface plasmon field-enhanced fluorescence spectroscopy studies of the interaction between an antibody and its surface-coupled antigen
    • Yu F., Yao D., and Knoll W. Surface plasmon field-enhanced fluorescence spectroscopy studies of the interaction between an antibody and its surface-coupled antigen. Anal. Chem. 75 (2003) 2610-2617
    • (2003) Anal. Chem. , vol.75 , pp. 2610-2617
    • Yu, F.1    Yao, D.2    Knoll, W.3
  • 35
    • 17744371694 scopus 로고    scopus 로고
    • Oligomerization of amyloid β-protein occurs during the isolation of lipid rafts
    • Yu W., Zou K., Gong J.S., Ko M., Yanagisawa K., and Michikawa M. Oligomerization of amyloid β-protein occurs during the isolation of lipid rafts. J. Neurosci. Res. 80 (2005) 114-119
    • (2005) J. Neurosci. Res. , vol.80 , pp. 114-119
    • Yu, W.1    Zou, K.2    Gong, J.S.3    Ko, M.4    Yanagisawa, K.5    Michikawa, M.6


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