메뉴 건너뛰기




Volumn 182, Issue , 2013, Pages 86-93

A micro-environmental study of the Zn+2-Aβ1-16 structural properties

Author keywords

Abeta peptide; Alzheimer; Metal; Molecular dynamics; QM MM

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-16]; COORDINATION COMPOUND; LIGAND; METAL DERIVATIVE; SOLVENT; UNCLASSIFIED DRUG; WATER; ZINC ION;

EID: 84885178116     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.07.002     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - Neurodegenerative diseases and prions
    • DOI 10.1056/NEJM200105173442006
    • S.B. Prusiner, Shattuck lecture: neurodegenerative diseases and prions, The New England Journal of Medicine 344 (2001) 1516-1526. (Pubitemid 32429212)
    • (2001) New England Journal of Medicine , vol.344 , Issue.20 , pp. 1516-1526
    • Prusiner, S.B.1
  • 3
    • 18244389436 scopus 로고    scopus 로고
    • The role of cerebral amyloid accumulation in common forms of Alzheimer disease
    • DOI 10.1172/JCI200525100
    • S. Gandy, The role of cerebral amyloid β accumulation in common forms of Alzheimer disease, Journal of Clinical Investigation 115 (2005) 1121-1129. (Pubitemid 40629026)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.5 , pp. 1121-1129
    • Gandy, S.1
  • 4
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • DOI 10.1016/S0166-2236(03)00067-5
    • A.I. Bush, The metallobiology of Alzheimer's disease, Trends in Neurosciences 26 (2003) 207-214. (Pubitemid 36412003)
    • (2003) Trends in Neurosciences , vol.26 , Issue.4 , pp. 207-214
    • Bush, A.I.1
  • 6
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of alzheimer disease: An alternative to the amyloid hypo thesis
    • R.D. Therry, The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis, Journal of Neuropathology and Experimental Neurology 55 (1996) 1023-1025.
    • (1996) Journal of Neuropathology and Experimental Neurology , vol.55 , pp. 1023-1025
    • Therry, R.D.1
  • 8
    • 0037355742 scopus 로고    scopus 로고
    • Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
    • DOI 10.1023/A:1020795422185
    • C. Opazo, M.I. Barria, F.H. Ruiz, N.C. Inestrosa, Copper reduction by copper binding proteins and its relation to neurodegenerative diseases, Biometals 16 (2003) 91-98. (Pubitemid 36140219)
    • (2003) BioMetals , vol.16 , Issue.1 , pp. 91-98
    • Opazo, C.1    Ines Barria, M.2    Ruiz, F.H.3    Inestrosa, N.C.4
  • 12
    • 58049206930 scopus 로고    scopus 로고
    • The role of metals in beta-amyloid peptide aggregation: X-ray spectroscopy and numerical simulations
    • S. Morante, The role of metals in beta-amyloid peptide aggregation: X-ray spectroscopy and numerical simulations, Current Alzheimer Research 5 (2008) 508-524.
    • (2008) Current Alzheimer Research , vol.5 , pp. 508-524
    • Morante, S.1
  • 14
    • 61749097242 scopus 로고    scopus 로고
    • Pleomorphic copper coordination by alzheimer's disease amyloid-β peptide
    • S.C. Drew, C.J. Noble, C.L. Masters, G.R. Hanson, K.J. Barnham, Pleomorphic copper coordination by Alzheimer's disease amyloid-β peptide, JACS 131 (2009) 1195-1207.
    • (2009) JACS , 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
  • 15
    • 66149161888 scopus 로고    scopus 로고
    • Copper(ii) binding to amyloid-beta fibrils of alzheimer's disease reveals a pico-molar affinity; Stoichiometry and coordination geometry is independent of a oligomeric form
    • C. Sarell, C.D. Syme, S. Rigby, J.H. Viles, Copper(II) binding to amyloid-beta fibrils of Alzheimer's disease reveals a pico-molar affinity; stoichiometry and coordination geometry is independent of a oligomeric form, Biochemistry 48 (2009) 4388-4402.
    • (2009) Biochemistry , vol.48 , pp. 4388-4402
    • Sarell, C.1    Syme, C.D.2    Rigby, S.3    Viles, J.H.4
  • 16
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid -peptide
    • DOI 10.1111/j.1742-4658.2006.05563.x
    • J. Danielsson, R. Pierattelli, L. Banci, A. Graeslund, High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide, FEBS Journal 274 (2007) 46-59. (Pubitemid 44952897)
    • (2007) FEBS Journal , vol.274 , Issue.1 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 18
    • 33644867988 scopus 로고    scopus 로고
    • Structural changes of region 1-16 of the Alzheimer disease amyloid -peptide upon zinc binding and in vitro aging
    • DOI 10.1074/jbc.M504454200
    • S. Zirah, S.A. Kozin, A.K.Mazur, A. Blond, M. Cheminant, I. Ségalas-Milazzo, P. Debey, S. Rebuffat, Structural changes of region 1-16 of the Alzheimer disease amyloid β-peptide upon zinc binding and in vitro aging, Journal of Biological Chemistry 281 (2006) 2151-2161. (Pubitemid 43845805)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 2151-2161
    • Zirah, S.1    Kozin, S.A.2    Mazur, A.K.3    Blond, A.4    Cheminant, M.5    Segalas-Milazzo, I.6    Debey, P.7    Rebuffat, S.8
  • 19
    • 33644530354 scopus 로고    scopus 로고
    • Solution 1h nmr investigation of zn2+ and cd2+ binding to amyloid-beta peptide (aβ) of alzheimer's disease
    • C.D. Syme, J.H. Viles, Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease, BBA 1764 (2006) 246-256.
    • (2006) BBA , vol.1764 , pp. 246-256
    • Syme, C.D.1    Viles, J.H.2
  • 20
    • 27944471348 scopus 로고    scopus 로고
    • Ab initio model studies of copper binding to peptides containing a His-His sequence: Relevance to the -amyloid peptide of Alzheimer's disease
    • DOI 10.1007/s00775-005-0038-9
    • D.F. Raffa, R. Gomez-Balderas, P. Brunelle, G.A. Rickard, A. Rauk, Ab initio model studies of copper binding to peptides containing a His-His sequence: relevance to the β-amyloid peptide of Alzheimer's disease, Journal of Biological Inorganic Chemistry 10 (2005) 887-902. (Pubitemid 41682552)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.8 , pp. 887-902
    • Raffa, D.F.1    Gomez-Balderas, R.2    Brunelle, P.3    Rickard, G.A.4    Rauk, A.5
  • 21
    • 33846669977 scopus 로고    scopus 로고
    • Ab initio modelling of the structure and redox behaviour of copper(I) bound to a His-His model peptide: Relevance to the -amyloid peptide of Alzheimer's disease
    • DOI 10.1007/s00775-006-0175-9
    • D.F. Raffa, G.A. Rickard, A. Rauk, Ab initiomodelling of the structure and redox behaviour of copper(I) bound to a His-Hismodel peptide: relevance to the β-amyloid peptide of Alzheimer's disease, Journal of Biological Inorganic Chemistry 12 (2007) 147-164. (Pubitemid 46197940)
    • (2007) Journal of Biological Inorganic Chemistry , vol.12 , Issue.2 , pp. 147-164
    • Raffa, D.F.1    Rickard, G.A.2    Rauk, A.3
  • 22
    • 39749196738 scopus 로고    scopus 로고
    • Why is the amyloid beta peptide of Alzheimer's disease neurotoxic?
    • DOI 10.1039/b718601k
    • A. Rauk,Why is the amyloid beta peptide of Alzheimer's disease neurotoxic? Dalton Transactions (2008) 1273-1282. (Pubitemid 351311808)
    • (2008) Dalton Transactions , Issue.10 , pp. 1273-1282
    • Rauk, A.1
  • 23
    • 34248194356 scopus 로고    scopus 로고
    • Molecular dynamics study of the beta amyloid peptide of alzheimer's disease and its divalent copper complexes
    • DOI 10.1021/jp0689621
    • D.F. Raffa, A. Rauk, Molecular dynamics study of the beta amyloid peptide of Alzheimer's disease and its divalent copper complexes, The Journal of Physical Chemistry. B 111 (2007) 3789-3799. (Pubitemid 46724009)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.14 , pp. 3789-3799
    • Raffa, D.F.1    Rauk, A.2
  • 24
    • 55949133729 scopus 로고    scopus 로고
    • Computational study of the binding of cuii to alzheimer's amyloid-β peptide: Do aβ42 and aβ40 bind copper in identical fashion?
    • Y. Mantri, M. Fioroni, M.H. Baik, Computational study of the binding of CuII to Alzheimer's amyloid-β peptide: Do Aβ42 and Aβ40 bind copper in identical fashion? Journal of Biological Inorganic Chemistry 13 (2008) 1197-1204.
    • (2008) Journal of Biological Inorganic Chemistry , vol.13 , pp. 1197-1204
    • Mantri, Y.1    Fioroni, M.2    Baik, M.H.3
  • 25
    • 68849100968 scopus 로고    scopus 로고
    • Modeling of the zn2+ binding in the 1-16 region of the amyloid β peptide involved in alzheimer's disease
    • S. Furlan, G. La Penna, Modeling of the Zn2+ binding in the 1-16 region of the amyloid β peptide involved in Alzheimer's disease, ChemPhysChem 11 (2009) 6468-6481.
    • (2009) ChemPhysChem , vol.11 , pp. 6468-6481
    • Furlan, S.1    La Penna, G.2
  • 26
    • 77956626762 scopus 로고    scopus 로고
    • On the metal ion (zn2+, cu2+) coordination with beta-amyloid peptide: Dft computational study
    • T. Marino, N. Russo, M. Toscano, M. Pavelka, On the metal ion (Zn2+, Cu2+) coordination with beta-amyloid peptide: DFT computational study, Interdiscipl Sci Comput Life Sci 2 (2010) 57-69.
    • (2010) Interdiscipl Sci Comput Life Sci , vol.2 , pp. 57-69
    • Marino, T.1    Russo, N.2    Toscano, M.3    Pavelka, M.4
  • 27
    • 84857355007 scopus 로고    scopus 로고
    • Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and xas measurements
    • P. Giannozzi, K. Jansen, G. La Penna, V.Minicozzi, S.Morante, G.C. Rossi, F. Stellato, Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements, Metallomics 4 (2012) 156-165.
    • (2012) Metallomics , vol.4 , pp. 156-165
    • Giannozzi, P.1    Jansen, K.2    La Penna, G.3    Minicozzi, V.4    Morante, S.5    Rossi, G.C.6    Stellato, F.7
  • 29
    • 38049136879 scopus 로고    scopus 로고
    • Effects of zinc binding on the conformational distribution of the amyloid-β peptide based on molecular dynamics simulations
    • W. Li, J. Zhang, Y. Su, J.Wang, M. Qin,W. Wangl, Effects of zinc binding on the conformational distribution of the amyloid-β peptide based on molecular dynamics simulations, The Journal of Physical Chemistry. B 111 (2007) 13814-13821.
    • (2007) The Journal of Physical Chemistry. B , vol.111 , pp. 13814-13821
    • Li, W.1    Zhang, J.2    Su, Y.3    Wang, J.4    Qin, M.5    Wangl, W.6
  • 32
    • 0000928098 scopus 로고    scopus 로고
    • A hybrid method for solutes in complex solvents: Density functional theory with empirical force fields
    • M. Eichinger, P. Tavan, J. Hutter, M. Parrinello, A hybrid method for solutes in complex solvents: density functional theory with empirical force fields, Journal of Chemical Physics 110 (1999) 10452-10467.
    • (1999) Journal of Chemical Physics , vol.110 , pp. 10452-10467
    • Eichinger, M.1    Tavan, P.2    Hutter, J.3    Parrinello, M.4
  • 35
    • 33646175469 scopus 로고    scopus 로고
    • Amber force field implementation, molecular modelling study, synthesis and mmp-1/mmp-2 inhibition profile of (r)-and (s)-n-hydroxy- 2-(n-isopropoxybiphenyl-4-ylsulfonamido)-3 methylbutanamides
    • T. Tuccinardi, A. Martinelli, E. Nuti, P. Carelli, F. Balzano, G. Uccello-Barretta, G. Murphy, A. Rossello, Amber force field implementation, molecular modelling study, synthesis and MMP-1/MMP-2 inhibition profile of (R)-and (S)-N-hydroxy- 2-(N-isopropoxybiphenyl-4-ylsulfonamido)-3 methylbutanamides, Bioorganic & Medicinal Chemistry 14 (2006) 4260-4276.
    • (2006) Bioorganic & Medicinal Chemistry , vol.14 , pp. 4260-4276
    • Tuccinardi, T.1    Martinelli, A.2    Nuti, E.3    Carelli, P.4    Balzano, F.5    Uccello-Barretta, G.6    Murphy, G.7    Rossello, A.8
  • 36
    • 0026675574 scopus 로고
    • Molecular dynamics studies on superoxide dismutase and its mutants: The structural and functional role of arg 143
    • L. Banci, P. Carloni, G. La Penna, P.L. Orioli, Molecular dynamics studies on superoxide dismutase and its mutants: the structural and functional role of Arg 143, JACS 114 (1992) 6994-7001.
    • (1992) JACS , vol.114 , pp. 6994-7001
    • Banci, L.1    Carloni, P.2    La Penna, G.3    Orioli, P.L.4
  • 37
    • 84943502952 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • S. Nosé, A unified formulation of the constant temperature molecular dynamics methods, Molecular Physics 52 (1984) 255-268.
    • (1984) Molecular Physics , vol.52 , pp. 255-268
    • Nosé, S.1
  • 38
    • 33846823909 scopus 로고
    • Particle mesh ewald-an n. Log(n) method for ewald sums in large systems
    • T. Darden, D. York, L. Pedersen, Particle Mesh Ewald-an N. Log(N) method for Ewald sums in large systems, Journal of Chemical Physics 98 (1993) 10089-10092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 39
    • 31144441067 scopus 로고    scopus 로고
    • 2 oxidative addition
    • M. Svensson, S. Humbel, R.D.J. Froese, T.Matsubara, S. Sieber, K. Morokuma, ONIOM: amultilayered integratedMO + MMmethod for geometry optimizations and single point energy predictions. A test for Diels-Alder reactions and Pt(P(t-Bu)3)2 + H2 oxidative addition, Journal of Physical Chemistry 100 (1996) 19357-19363. (Pubitemid 126786970)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.50 , pp. 19357-19363
    • Svensson, M.1    Humbel, S.2    Froese, R.D.J.3    Matsubara, T.4    Sieber, S.5    Morokuma, K.6
  • 40
    • 0001519072 scopus 로고    scopus 로고
    • -
    • S. Humbel, S. Sieber, K. Morokuma, The IMOMO method: integration of different levels of molecular orbital approximations for geometry optimization of large systems. Test for n-butane conformation and SN2 reaction: RCl + Cl-, Journal of Chemical Physics 105 (1996) 1959-1967. (Pubitemid 126612904)
    • (1996) Journal of Chemical Physics , vol.105 , Issue.5 , pp. 1959-1967
    • Humbel, S.1    Sieber, S.2    Morokuma, K.3
  • 43
    • 0042041206 scopus 로고
    • UFF, a full periodic table force field for molecular mechanics and molecular dynamics simulations
    • A.K. Rappe, C.J. Casewit, K.S. Colwell, W.A. Goddard, W.M. Skiff, UFF, a full periodic table force field for molecular mechanics and molecular dynamics simulations, JACS 114 (1992) 10024-10035.
    • (1992) JACS , vol.114 , pp. 10024-10035
    • Rappe, A.K.1    Casewit, C.J.2    Colwell, K.S.3    Goddard, W.A.4    Skiff, W.M.5
  • 44
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • DOI 10.1016/0263-7855(96)00018-5
    • W. Humphrey, A. Dalke, K. Schulten, VMD: visual molecular dynamics, Journal of Molecular Graphics 14 (1996) 33-38. (Pubitemid 26152973)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 45
    • 0037448474 scopus 로고    scopus 로고
    • On the transferability of force field parameters with an ab initio force field developed for sulfonamides
    • F. Sato, S. Hojo, H. Sun, On the transferability of force field parameters with an ab initio force field developed for sulfonamides, Journal of Physical Chemistry A 107 (2003) 248-257.
    • (2003) Journal of Physical Chemistry A , vol.107 , pp. 248-257
    • Sato, F.1    Hojo, S.2    Sun, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.