메뉴 건너뛰기




Volumn 154, Issue 1-2, 2006, Pages 190-197

Kinetic analysis of β-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing

Author keywords

A ; Aggregation; Metal chelator; Metal ions; Surface plasmon resonance (SPR)

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; CALCIUM ION; CHELATING AGENT; COPPER ION; EDETIC ACID; FERROUS ION; IRON; METAL ION; ZINC ION;

EID: 33744510885     PISSN: 01650270     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jneumeth.2005.12.016     Document Type: Article
Times cited : (57)

References (43)
  • 1
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood C.S., Huang X., Moir R.D., Bacarra N.M., Romano D., Tanzi R.E., et al. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 273 (1998) 12817-12826
    • (1998) J Biol Chem , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Bacarra, N.M.4    Romano, D.5    Tanzi, R.E.6
  • 2
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid beta(1-42)
    • Atwood C.S., Scarpa R.C., Huang X., Moir R.D., Jones W.D., and Fairlie D.P. Characterization of copper interactions with Alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid beta(1-42). J Neurochem 75 (2000) 1219-1233
    • (2000) J Neurochem , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6
  • 3
    • 0027220686 scopus 로고
    • A novel zinc(II) binding site modulates the function of the beta Aβ amyloid protein precursor of Alzheimer's disease
    • Bush A.I., Multhauo G., Moir R.D., Willamson T.G., Small D.H., Rumble B., et al. A novel zinc(II) binding site modulates the function of the beta Aβ amyloid protein precursor of Alzheimer's disease. J Biol Chem 268 (1993) 16109-16112
    • (1993) J Biol Chem , vol.268 , pp. 16109-16112
    • Bush, A.I.1    Multhauo, G.2    Moir, R.D.3    Willamson, T.G.4    Small, D.H.5    Rumble, B.6
  • 6
    • 0033551782 scopus 로고    scopus 로고
    • Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion
    • Cherny R.A., Legg J.T., McLean C.A., Fairlie D.P., Huang X., Atwood C.S., et al. Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion. J Biol Chem 274 (1999) 23223-23228
    • (1999) J Biol Chem , vol.274 , pp. 23223-23228
    • Cherny, R.A.1    Legg, J.T.2    McLean, C.A.3    Fairlie, D.P.4    Huang, X.5    Atwood, C.S.6
  • 7
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny R.A., Atwood C.S., Xilinas M.E., Gray D.N., Jones W.D., McLean C.A., et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30 (2001) 665-676
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5    McLean, C.A.6
  • 8
    • 7444250743 scopus 로고    scopus 로고
    • A sensitivity comparison of optical biosensors based on four different surface plasmon resonance modes
    • Chien F.-C., and Chen S.-J. A sensitivity comparison of optical biosensors based on four different surface plasmon resonance modes. Biosens Bioelectron 20 (2004) 633-642
    • (2004) Biosens Bioelectron , vol.20 , pp. 633-642
    • Chien, F.-C.1    Chen, S.-J.2
  • 9
    • 7444244358 scopus 로고    scopus 로고
    • An investigation into the influence of secondary structures on DNA hybridization using surface plasmon resonance biosensing
    • Chien F.-C., Liu J.-S., Su H.-J., Kao L.-A., Chiou C.-F., Chen W.-Y., et al. An investigation into the influence of secondary structures on DNA hybridization using surface plasmon resonance biosensing. Chem Phys Lett 397 (2004) 429-434
    • (2004) Chem Phys Lett , vol.397 , pp. 429-434
    • Chien, F.-C.1    Liu, J.-S.2    Su, H.-J.3    Kao, L.-A.4    Chiou, C.-F.5    Chen, W.-Y.6
  • 10
    • 0023899417 scopus 로고
    • Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis
    • Coria F., Castano E., Prelli F., Larrondo-Lillo M., Van Duinen S., Shelanski M.L., et al. Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab Invest 58 (1988) 454-458
    • (1988) Lab Invest , vol.58 , pp. 454-458
    • Coria, F.1    Castano, E.2    Prelli, F.3    Larrondo-Lillo, M.4    Van Duinen, S.5    Shelanski, M.L.6
  • 11
    • 0028986858 scopus 로고
    • Alpha 1-antichymotrypsin regulates Alzheimer beta-amyloid peptide fibril formation
    • Eriksson S., Janciauskiene S., and Lannfelt L. Alpha 1-antichymotrypsin regulates Alzheimer beta-amyloid peptide fibril formation. Proc Natl Acad Sci USA 92 (1995) 2313-2317
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2313-2317
    • Eriksson, S.1    Janciauskiene, S.2    Lannfelt, L.3
  • 12
    • 0030024717 scopus 로고    scopus 로고
    • In vitro growth of Alzheimer's disease β-amyloid plaques displays first-order kinetics
    • Esler W.P., Stimson E.R., Ghilardi J.R., Vinters H.V., Lee J.P., Mantyh P.W., et al. In vitro growth of Alzheimer's disease β-amyloid plaques displays first-order kinetics. Biochemistry 35 (1996) 749-757
    • (1996) Biochemistry , vol.35 , pp. 749-757
    • Esler, W.P.1    Stimson, E.R.2    Ghilardi, J.R.3    Vinters, H.V.4    Lee, J.P.5    Mantyh, P.W.6
  • 14
    • 0021207461 scopus 로고
    • Alzheimer disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G.G., and Wong C.W. Alzheimer disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 122 (1984) 1131-1135
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 15
    • 3042706248 scopus 로고    scopus 로고
    • A localized surface plasmon resonance biosensor: first steps toward an assay for Alzheimer's disease
    • Haes A.J., Hall W.P., Chang L., Klein W.L., and Van Duyne R.P. A localized surface plasmon resonance biosensor: first steps toward an assay for Alzheimer's disease. Nano Lett 4 (2004) 1029-1034
    • (2004) Nano Lett , vol.4 , pp. 1029-1034
    • Haes, A.J.1    Hall, W.P.2    Chang, L.3    Klein, W.L.4    Van Duyne, R.P.5
  • 16
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance
    • Hasegawa K., Ono K., Yamada M., and Naiki H. Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance. Biochemistry 41 (2002) 13489-13498
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 17
    • 0032626631 scopus 로고    scopus 로고
    • Surface plasmon resonancesensors: review
    • Homola J., Yee S.S., and Gauglitz G. Surface plasmon resonancesensors: review. Sens Actuators B 54 (1999) 3-15
    • (1999) Sens Actuators B , vol.54 , pp. 3-15
    • Homola, J.1    Yee, S.S.2    Gauglitz, G.3
  • 18
    • 1842790740 scopus 로고    scopus 로고
    • A novel ultrahigh-resolution surface plasmon resonance biosensor with an Au nanocluster-embedded dielectric film
    • Hu W.-P., Chen S.-J., Huang K.-T., Hsu J.H., Chen W.-Y., Chang G.L., et al. A novel ultrahigh-resolution surface plasmon resonance biosensor with an Au nanocluster-embedded dielectric film. Biosens Bioelectron 19 (2004) 1465-1471
    • (2004) Biosens Bioelectron , vol.19 , pp. 1465-1471
    • Hu, W.-P.1    Chen, S.-J.2    Huang, K.-T.3    Hsu, J.H.4    Chen, W.-Y.5    Chang, G.L.6
  • 19
    • 0030704680 scopus 로고    scopus 로고
    • Zinc-induced Alzheimer's Aβ1-40 aggregation is mediated by conformational factors
    • Huang X., Atwood C.S., Moir R.D., Hartshorn M.A., Vonsattel J.P., Tanzi R.E., et al. Zinc-induced Alzheimer's Aβ1-40 aggregation is mediated by conformational factors. J Biol Chem 272 (1997) 26464-26470
    • (1997) J Biol Chem , vol.272 , pp. 26464-26470
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Vonsattel, J.P.5    Tanzi, R.E.6
  • 20
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides
    • Huang X., Atwood C.S., Moir R.D., Hartshorn M.A., Tanzi R.E., and Bush A.I. Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides. J Biol Inorg Chem 9 (2004) 954-960
    • (2004) J Biol Inorg Chem , vol.9 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 21
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., and Lansbury P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 23
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • Kremer J.J., Pallitto M.M., Sklansky D.J., and Murphy R.M. Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry 39 (2000) 10309-10318
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 24
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, chemical characterization and quantitation of Aβ 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits
    • Kuo Y.M., Emmerling M.R., Woods A.S., Cotter R.J., and Roher A.E. Isolation, chemical characterization and quantitation of Aβ 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits. Biochem Biophysical Res Commun 237 (1997) 188-191
    • (1997) Biochem Biophysical Res Commun , vol.237 , pp. 188-191
    • Kuo, Y.M.1    Emmerling, M.R.2    Woods, A.S.3    Cotter, R.J.4    Roher, A.E.5
  • 26
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J., Yee A., Brewer Jr. H.B., Das S., and Potter H. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372 (1994) 92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer Jr., H.B.3    Das, S.4    Potter, H.5
  • 27
    • 0035254995 scopus 로고    scopus 로고
    • Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation
    • Massi F., and Straub J.E. Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation. Proteins Struct Funct Genet 42 (2001) 217-229
    • (2001) Proteins Struct Funct Genet , vol.42 , pp. 217-229
    • Massi, F.1    Straub, J.E.2
  • 29
    • 0033528666 scopus 로고    scopus 로고
    • Differential effects of apolipoprotein E isoforms on metal-induced aggregation of Aβ using physiological concentrations
    • Moir R.D., Atwood C.S., Romano D.M., Laurans M.H., Huang X., Bush A.I., et al. Differential effects of apolipoprotein E isoforms on metal-induced aggregation of Aβ using physiological concentrations. Biochemistry 38 (1999) 4595-4603
    • (1999) Biochemistry , vol.38 , pp. 4595-4603
    • Moir, R.D.1    Atwood, C.S.2    Romano, D.M.3    Laurans, M.H.4    Huang, X.5    Bush, A.I.6
  • 30
    • 0025784267 scopus 로고
    • Differential expression of β amyloid protein precursor (APP) and tau in the aged human brain: individual variability and correlation between APP-751 and four-repeat tau
    • Oyama F., Shimada H., Oyama R., Titani K., and Ihara Y. Differential expression of β amyloid protein precursor (APP) and tau in the aged human brain: individual variability and correlation between APP-751 and four-repeat tau. J Neuropathol Exp Neurol 50 (1991) 560-578
    • (1991) J Neuropathol Exp Neurol , vol.50 , pp. 560-578
    • Oyama, F.1    Shimada, H.2    Oyama, R.3    Titani, K.4    Ihara, Y.5
  • 31
    • 0027322817 scopus 로고
    • β-Amyloid protein precursor and T mRNA levels versus β-amyloid plaque and neurofibrillary tangles in the aged human brain
    • Oyama F., Shimada H., Oyama R., Titani K., and Ihara Y. β-Amyloid protein precursor and T mRNA levels versus β-amyloid plaque and neurofibrillary tangles in the aged human brain. J Neurochem 60 (1993) 1658-1664
    • (1993) J Neurochem , vol.60 , pp. 1658-1664
    • Oyama, F.1    Shimada, H.2    Oyama, R.3    Titani, K.4    Ihara, Y.5
  • 32
    • 0035997230 scopus 로고    scopus 로고
    • Imaging real-time aggregation of amyloid beta protein(1-42) by atomic force microscopy
    • Parbhu A., Lin H., Thimm J., and Lal R. Imaging real-time aggregation of amyloid beta protein(1-42) by atomic force microscopy. Peptides 23 (2002) 1265-1270
    • (2002) Peptides , vol.23 , pp. 1265-1270
    • Parbhu, A.1    Lin, H.2    Thimm, J.3    Lal, R.4
  • 37
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins and therapy. Physiol Rev 81 (2001) 741-766
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 38
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain
    • Snow A.D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mizutani A., et al. An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain. Neuron 12 (1994) 219-234
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6
  • 39
    • 0141702360 scopus 로고    scopus 로고
    • Trace amounts of copper in water induce beta-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease
    • Sparks D.L., and Schreurs B.G. Trace amounts of copper in water induce beta-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease. Proc Natl Acad Sci USA 100 (2003) 11065-11069
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11065-11069
    • Sparks, D.L.1    Schreurs, B.G.2
  • 40
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • Stenberg E., Persson B., Roos H., and Urbaniczky C. Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J Colloid Interf Sci 143 (1991) 513-526
    • (1991) J Colloid Interf Sci , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 41
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • Suh S.W., Jensen K.B., Jensen M.S., Silva D.S., Kesslak P.J., Danscher G., et al. Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res 852 (2000) 274-278
    • (2000) Brain Res , vol.852 , pp. 274-278
    • Suh, S.W.1    Jensen, K.B.2    Jensen, M.S.3    Silva, D.S.4    Kesslak, P.J.5    Danscher, G.6
  • 42
    • 9644302450 scopus 로고    scopus 로고
    • Hemoglobin promotes Aβ oligomer formation and localizes in neurons and amyloid deposits
    • Wu C.W., Liao P.C., Yu L., Wang S.T., Chen S.T., Wu C.M., et al. Hemoglobin promotes Aβ oligomer formation and localizes in neurons and amyloid deposits. Neurobiol Dis 17 (2004) 367-377
    • (2004) Neurobiol Dis , vol.17 , pp. 367-377
    • Wu, C.W.1    Liao, P.C.2    Yu, L.3    Wang, S.T.4    Chen, S.T.5    Wu, C.M.6
  • 43
    • 0029920929 scopus 로고    scopus 로고
    • Glycoprotein 330/megalin: probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers
    • Zlokovic B.V., Martel C.L., Matsubara E., McComb J.G., Zheng G., McCluskey R.T., et al. Glycoprotein 330/megalin: probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers. Proc Natl Acad Sci USA 93 (1996) 4229-4234
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4229-4234
    • Zlokovic, B.V.1    Martel, C.L.2    Matsubara, E.3    McComb, J.G.4    Zheng, G.5    McCluskey, R.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.