메뉴 건너뛰기




Volumn 44, Issue 11, 2011, Pages 1146-1155

The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APP PROTEIN, HUMAN; COPPER; ISOTOPE; NITROGEN; OXYGEN; REACTIVE OXYGEN METABOLITE;

EID: 81255197608     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar200014u     Document Type: Article
Times cited : (156)

References (39)
  • 1
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • DOI 10.1016/S0166-2236(03)00067-5
    • Bush, A. I. The metallobiology of Alzheimer's disease Trends Neurosci. 2003, 26, 207-214 (Pubitemid 36412003)
    • (2003) Trends in Neurosciences , vol.26 , Issue.4 , pp. 207-214
    • Bush, A.I.1
  • 3
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
    • Selkoe, D. J. Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior Behav. Brain Res. 2008, 192, 106-113
    • (2008) Behav. Brain Res. , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 4
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid β peptide
    • DOI 10.1016/j.bbamem.2007.02.002, PII S0005273607000387
    • Smith, D. G.; Cappai, R.; Barnham, K. J. The redox chemistry of the Alzheimer's disease amyloid beta peptide Biochim. Biophys. Acta 2007, 1768, 1976-1990 (Pubitemid 47125850)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 5
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's Diseases
    • Barnham, K. J.; Bush, A. I. Metals in Alzheimer's and Parkinson's Diseases Curr. Opin. Chem. Biol. 2008, 12, 222-228
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 6
    • 72949094439 scopus 로고    scopus 로고
    • Copper and zinc binding to amyloid-β: Coordination, dynamics, aggregation, reactivity and metal-ion transfer
    • Faller, P. Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer ChemBioChem 2009, 10, 2691-2703
    • (2009) ChemBioChem , vol.10 , pp. 2691-2703
    • Faller, P.1
  • 8
    • 46749100924 scopus 로고    scopus 로고
    • Therapeutics for Alzheimer's Disease Based on the Metal Hypothesis
    • DOI 10.1016/j.nurt.2008.05.001, PII S1933721308000901
    • Bush, A. I.; Tanzi, R. E. Therapeutics for Alzheimer's disease based on the metal hypothesis Neurotherapeutics 2008, 5, 421-432 (Pubitemid 351952485)
    • (2008) Neurotherapeutics , vol.5 , Issue.3 , pp. 421-432
    • Bush, A.I.1    Tanzi, R.E.2
  • 9
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain, C. C.; Ali, F.; Volitakis, I.; Cherny, R. A.; Norton, R. S.; Beyreuther, K.; Barrow, C. J.; Masters, C. L.; Bush, A. I.; Barnham, K. J. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits J. Biol. Chem. 2001, 276, 20466-20473
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 10
    • 0038802776 scopus 로고    scopus 로고
    • Coordination abilities of the 1-16 and 1-28 fragments of β-amyloid peptide towards copper(II) ions: A combined potentiometric and spectroscopic study
    • DOI 10.1016/S0162-0134(03)00128-4
    • Kowalik-Jankowska, T.; Ruta, M.; Wiśniewska, K.; Łankiewicz, L. Coordination abilities of the 1-16 and 1-28 fragments of β-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study J. Inorg. Biochem. 2003, 95, 270-282 (Pubitemid 36775348)
    • (2003) Journal of Inorganic Biochemistry , vol.95 , Issue.4 , pp. 270-282
    • Kowalik-Jankowska, T.1    Ruta, M.2    Wisniewska, K.3    Lankiewicz, L.4
  • 12
    • 2442461177 scopus 로고    scopus 로고
    • Copper binding to the amyloid-β peptide associated with Alzheimer's disease
    • Syme, C. D.; Nadal, R. C.; Rigby, S. E.; Viles, J. H. Copper binding to the amyloid-β peptide associated with Alzheimer's disease J. Biol. Chem. 2004, 279, 18169-18177
    • (2004) J. Biol. Chem. , vol.279 , pp. 18169-18177
    • Syme, C.D.1    Nadal, R.C.2    Rigby, S.E.3    Viles, J.H.4
  • 15
    • 34247177552 scopus 로고    scopus 로고
    • Role of aspartate-1 in Cu(II) binding to the amyloid-β peptide of Alzheimer's disease
    • DOI 10.1021/ja068952d
    • Karr, J. W.; Szalai, V. A. Role of aspartate-1 in Cu(II) binding to the amyloid-β peptide of Alzheimer's disease J. Am. Chem. Soc. 2007, 129, 3796-3797 (Pubitemid 46595480)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.13 , pp. 3796-3797
    • Karr, J.W.1    Szalai, V.A.2
  • 16
    • 33746335362 scopus 로고    scopus 로고
    • NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease
    • Hou, L.; Zagorski, M. G. NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease J. Am. Chem. Soc. 2006, 128, 9260-92615
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9260-92615
    • Hou, L.1    Zagorski, M.G.2
  • 17
    • 55249123932 scopus 로고    scopus 로고
    • The structure of the amyloid β-peptide high affinity Copper II binding site in Alzheimer's disease
    • Streltsov, V. A.; Titmuss, S. J.; Epa, V. C.; Barnham, K. J.; Masters, C. L.; Varghese, J. N. The structure of the amyloid β-peptide high affinity Copper II binding site in Alzheimer's disease Biophys. J. 2008, 95, 3447-3456
    • (2008) Biophys. J. , vol.95 , pp. 3447-3456
    • Streltsov, V.A.1    Titmuss, S.J.2    Epa, V.C.3    Barnham, K.J.4    Masters, C.L.5    Varghese, J.N.6
  • 18
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes
    • DOI 10.1021/bi0002479
    • Miura, T.; Suzuki, K.; Kohata, N.; Takeuchi, H. Metal binding modes of Alzheimer's amyloid β -peptide in insoluble aggregates and soluble complexes Biochemistry 2000, 39, 7024-7031 (Pubitemid 30390396)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 19
    • 50849126063 scopus 로고    scopus 로고
    • Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16
    • Shin, B.; Saxena, S. Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16 Biochemistry 2008, 47, 9117-9123
    • (2008) Biochemistry , vol.47 , pp. 9117-9123
    • Shin, B.1    Saxena, S.2
  • 20
    • 0016369980 scopus 로고
    • Structural implications derived from the analysis of EPR spectra of natural and artificial copper proteins
    • Peisach, J.; Blumberg, W. E. Structural implications derived from the analysis of EPR spectra of natural and artificial copper proteins Arch. Biochem. Biophys. 1974, 165, 691-698
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 691-698
    • Peisach, J.1    Blumberg, W.E.2
  • 22
    • 66149161888 scopus 로고    scopus 로고
    • Copper(II) binding to amyloid-beta fibrils of Alzheimers disease reveals a pico-molar affinity: Stoichiometry and coordination geometry is independent of Aβ Oligomeric Form
    • Sarell, C.; Syme, C.; Rigby, S.; Viles, J. Copper(II) binding to amyloid-beta fibrils of Alzheimers disease reveals a pico-molar affinity: stoichiometry and coordination geometry is independent of Aβ Oligomeric Form Biochemistry 2009, 48, 4388-4402
    • (2009) Biochemistry , vol.48 , pp. 4388-4402
    • Sarell, C.1    Syme, C.2    Rigby, S.3    Viles, J.4
  • 24
    • 84908778295 scopus 로고
    • In; Berliner, L. J. Reuben, J. Biological Magnetic Resonance 1; Plenum Press: New York
    • Boas, J. F.; Pilbrow, J. R.; Smith, T. D. In ESR of copper in biological systems; Berliner, L. J.; Reuben, J., Eds.; Biological Magnetic Resonance 1; Plenum Press: New York, 1978; pp 277-342.
    • (1978) ESR of Copper in Biological Systems , pp. 277-342
    • Boas, J.F.1    Pilbrow, J.R.2    Smith, T.D.3
  • 25
    • 0034350315 scopus 로고    scopus 로고
    • Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers
    • Deligiannakis, Y.; Louloudi, M.; Hadjiliadis, N. Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers Coord. Chem. Rev. 2000, 204, 1-112
    • (2000) Coord. Chem. Rev. , vol.204 , pp. 1-112
    • Deligiannakis, Y.1    Louloudi, M.2    Hadjiliadis, N.3
  • 26
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • DOI 10.1146/annurev.physchem.58.032806.104657
    • Millhauser, G. L. Copper and the Prion Protein: Methods, Structures, Function, and Disease Annu. Rev. Phys. Chem. 2007, 58, 299-320 (Pubitemid 46877592)
    • (2007) Annual Review of Physical Chemistry , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 27
    • 0003988115 scopus 로고    scopus 로고
    • Physical methods in bioinorganic chemistry: Spectroscopy and magnetism
    • In; Que, L. University Science Books: Sausalito CA
    • Chasteen, N. D.; Snetsinger, P. A. Physical methods in bioinorganic chemistry: spectroscopy and magnetism. In Electron paramagnetic resonance of metalloproteins; Que, L., Ed.; University Science Books: Sausalito CA, 2000; p 213.
    • (2000) Electron Paramagnetic Resonance of Metalloproteins , pp. 213
    • Chasteen, N.D.1    Snetsinger, P.A.2
  • 28
    • 61749097242 scopus 로고    scopus 로고
    • Pleomorphic Copper Coordination by Alzheimer's Disease Amyloid-β Peptide
    • Drew, S. C.; Noble, C. J.; Masters, C. L.; Hanson, G. R.; Barnham, K. J. Pleomorphic Copper Coordination by Alzheimer's Disease Amyloid-β Peptide J. Am. Chem. Soc. 2009, 131, 1195-1207
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1195-1207
    • Drew, S.C.1    Noble, C.J.2    Masters, C.L.3    Hanson, G.R.4    Barnham, K.J.5
  • 29
    • 25144485008 scopus 로고    scopus 로고
    • Peak suppression in ESEEM spectra of multinuclear spin systems
    • DOI 10.1016/j.jmr.2005.07.012, PII S1090780705002260
    • Stoll, S.; Calle, C.; Mitrikas, G.; Schweiger, A. Peak suppression in ESEEM spectra of multinuclear spin systems J. Magn. Reson. 2005, 177, 93-101 (Pubitemid 41336668)
    • (2005) Journal of Magnetic Resonance , vol.177 , Issue.1 , pp. 93-101
    • Stoll, S.1    Calle, C.2    Mitrikas, G.3    Schweiger, A.4
  • 30
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
    • Faller, P.; Hureau, C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide Dalton Trans. 2009, 1080-1094
    • (2009) Dalton Trans. , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 31
    • 67649600828 scopus 로고    scopus 로고
    • 2+ coordination of Alzheimer's disease amyloid-β peptide - Relevance to N-terminally truncated forms
    • 2+ coordination of Alzheimer's disease amyloid-β peptide - relevance to N-terminally truncated forms J. Am. Chem. Soc. 2009, 131, 8760-8761
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8760-8761
    • Drew, S.C.1    Masters, C.L.2    Barnham, K.J.3
  • 33
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid-β(1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques
    • Iwatsubo, T; Saido, T. C.; Mann, D. M.; Lee, V. M.; Trojanowski, J. Q. Full-length amyloid-β(1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques Am. J. Pathol. 1996, 149, 1823-1830 (Pubitemid 26415203)
    • (1996) American Journal of Pathology , vol.149 , Issue.6 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.A.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 34
    • 73249137909 scopus 로고    scopus 로고
    • Deprotonation of the Asp1-Ala2 peptide bond induces modification of the dynamic copper(II) environment in the amyloid-β peptide near physiological pH
    • Hureau, C.; Coppel, Y.; Dorlet, P.; Solari, P. L.; Sayen, S.; Guillon, E.; Sabater, L.; Faller, P. Deprotonation of the Asp1-Ala2 peptide bond induces modification of the dynamic copper(II) environment in the amyloid-β peptide near physiological pH Angew. Chem., Int. Ed. 2009, 48, 9522-9525
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 9522-9525
    • Hureau, C.1    Coppel, Y.2    Dorlet, P.3    Solari, P.L.4    Sayen, S.5    Guillon, E.6    Sabater, L.7    Faller, P.8
  • 36
    • 72949092936 scopus 로고    scopus 로고
    • Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-β peptide: A key role of the first two N-terminus residues
    • Dorlet, P.; Gambarelli, S.; Faller, P.; Hureau, C. Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-β peptide: A key role of the first two N-terminus residues Angew. Chem., Int. Ed. 2009, 48, 9273-9276
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 9273-9276
    • Dorlet, P.1    Gambarelli, S.2    Faller, P.3    Hureau, C.4
  • 38
    • 80052210889 scopus 로고    scopus 로고
    • Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance
    • H14} mode contributes to component I at physiological pH (; doi: 10.1021/jp200379m).
    • H14} mode contributes to component I at physiological pH (Shin, B.; Saxena, S. Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance. J. Phys. Chem. A 2011, doi: 10.1021/jp200379m).
    • (2011) J. Phys. Chem. A
    • Shin, B.1    Saxena, S.2
  • 39


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.