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Volumn 118, Issue 35, 2014, Pages 10355-10361

Zn2+ effect on structure and residual hydrophobicity of amyloid β-peptide monomers

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; HYDROPHOBICITY; MOLECULAR DYNAMICS; MONOMERS; NEURODEGENERATIVE DISEASES; PEPTIDES;

EID: 84926430036     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp504779m     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert, M.; Spillantini, M. G. A century of Alzheimer's disease. Science 2006, 314, 777-781.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 2
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. Folding proteins in fatal ways. Nature 2003, 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 5
    • 70349923038 scopus 로고    scopus 로고
    • Alzheimer's disease: From pathology to therapeutic approaches
    • Jakob-Roetne, R.; Jacobsen, H. Alzheimer's disease: From pathology to therapeutic approaches. Angew. Chem., Int. Ed. 2009, 48, 3030-3059.
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 3030-3059
    • Jakob-Roetne, R.1    Jacobsen, H.2
  • 6
    • 84867477898 scopus 로고    scopus 로고
    • The amyloid beta peptide: A chemist's perspective. Role in Alzheimer's and fibrillization
    • Hamley, I. W. The amyloid beta peptide: A chemist's perspective. Role in Alzheimer's and fibrillization. Chem. Rev. 2012, 112, 5147-5192.
    • (2012) Chem. Rev. , vol.112 , pp. 5147-5192
    • Hamley, I.W.1
  • 7
    • 84867460758 scopus 로고    scopus 로고
    • Bioinorganic chemistry of Alzheimer's disease
    • Kepp, K. P. Bioinorganic chemistry of Alzheimer's disease. Chem. Rev. 2012, 112, 5193-5239.
    • (2012) Chem. Rev. , vol.112 , pp. 5193-5239
    • Kepp, K.P.1
  • 8
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 9
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 1997, 20, 154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 10
    • 0027379395 scopus 로고
    • Characterization of beta-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey, C.; Lee, D.; Keim, P.; Lieberburg, I.; Schenk, D. B. Characterization of beta-amyloid peptide from human cerebrospinal fluid. J. Neurochem. 1993, 61, 1965-1968.
    • (1993) J. Neurochem. , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 11
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of Alzheimer's disease
    • Rauk, A. The chemistry of Alzheimer's disease. Chem. Soc. Rev. 2009, 38, 2698-2715.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2698-2715
    • Rauk, A.1
  • 12
    • 80155209561 scopus 로고    scopus 로고
    • Misfolded proteins in Alzheimer's disease and type II diabetes
    • De Toma, A. S.; Salamekh, S.; Ramamoorthy, A.; Lim, M. H. Misfolded proteins in Alzheimer's disease and type II diabetes. Chem. Soc. Rev. 2012, 41, 608-621.
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 608-621
    • De Toma, A.S.1    Salamekh, S.2    Ramamoorthy, A.3    Lim, M.H.4
  • 13
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4
    • Wood, S. J.; Wetzel, R.; Martin, J. D.; Hurle, M. R. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4. Biochemistry 1995, 34, 724-730.
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 14
    • 0029854533 scopus 로고    scopus 로고
    • Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence
    • Esler, W. P.; Stimson, E. R.; Ghilardi, J. R.; Lu, Y. A.; Felix, A. M.; Vinters, H. V.; Mantyh, P. W.; Lee, J. P.; Maggio, J. E. Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry 1996, 35, 13914-13921.
    • (1996) Biochemistry , vol.35 , pp. 13914-13921
    • Esler, W.P.1    Stimson, E.R.2    Ghilardi, J.R.3    Lu, Y.A.4    Felix, A.M.5    Vinters, H.V.6    Mantyh, P.W.7    Lee, J.P.8    Maggio, J.E.9
  • 15
    • 0035133048 scopus 로고    scopus 로고
    • Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution
    • Massi, F.; Peng, J. W.; Lee, J. P.; Straub, J. E. Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. Biophys. J. 2001, 80, 31-44.
    • (2001) Biophys. J. , vol.80 , pp. 31-44
    • Massi, F.1    Peng, J.W.2    Lee, J.P.3    Straub, J.E.4
  • 16
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430, 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 17
    • 65349162724 scopus 로고    scopus 로고
    • Hyperhomocysteinemia increases beta-amyloid by enhancing expression of gamma-secretase and phosphor-ylation of amyloid precursor protein in rat brain
    • Zhang, C. E.; Wei, W.; Liu, Y. H.; Peng, J. H.; Tian, Q.; Liu, G. P.; Zhang, Y.; Wang, J. Z. Hyperhomocysteinemia increases beta-amyloid by enhancing expression of gamma-secretase and phosphor-ylation of amyloid precursor protein in rat brain. Am. J. Pathol. 2009, 174, 1481-1491.
    • (2009) Am. J. Pathol. , vol.174 , pp. 1481-1491
    • Zhang, C.E.1    Wei, W.2    Liu, Y.H.3    Peng, J.H.4    Tian, Q.5    Liu, G.P.6    Zhang, Y.7    Wang, J.Z.8
  • 19
    • 36749100841 scopus 로고    scopus 로고
    • Investigations of the molecular mechanism of metal-induced Abeta (1-40) amyloido-genesis
    • Lim, K. H.; Kim, Y. K.; Chang, Y. T. Investigations of the molecular mechanism of metal-induced Abeta (1-40) amyloido-genesis. Biochemistry 2007, 46, 13523-13532.
    • (2007) Biochemistry , vol.46 , pp. 13523-13532
    • Lim, K.H.1    Kim, Y.K.2    Chang, Y.T.3
  • 20
    • 84859651929 scopus 로고    scopus 로고
    • Metal-associated amyloid-beta species in Alzheimer's disease
    • Pithadia, A. S.; Lim, M. H. Metal-associated amyloid-beta species in Alzheimer's disease. Curr. Opin. Chem. Biol. 2012, 16, 67-73.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 67-73
    • Pithadia, A.S.1    Lim, M.H.2
  • 21
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide
    • Faller, P.; Hureau, C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide. Dalton Trans. 2009, 1080-1094.
    • (2009) Dalton Trans. , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 22
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide
    • Danielsson, J.; Pierattelli, R.; Banci, L.; Graslund, A. High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide. FEBS J. 2007, 274, 46-59.
    • (2007) FEBS J. , vol.274 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 23
    • 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
  • 27
    • 84888354585 scopus 로고    scopus 로고
    • Effects of Zn (2+) binding on the structural and dynamic properties of amyloid beta peptide associated with Alzheimer's disease: Asp (1) or Glu (11) ?
    • Xu, L.; Wang, X.; Wang, X. Effects of Zn (2+) binding on the structural and dynamic properties of amyloid beta peptide associated with Alzheimer's disease: Asp (1) or Glu (11) ? ACS Chem. Neurosci. 2013, 4, 1458-1468.
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 1458-1468
    • Xu, L.1    Wang, X.2    Wang, X.3
  • 28
    • 33644867988 scopus 로고    scopus 로고
    • Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging
    • Zirah, S.; Kozin, S. A.; Mazur, A. K.; Blond, A.; Cheminant, M.; Segalas-Milazzo, I.; Debey, P.; Rebuffat, S. Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging. J. Biol. Chem. 2006, 281, 2151-2161.
    • (2006) J. Biol. Chem. , vol.281 , 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
  • 29
    • 38049136879 scopus 로고    scopus 로고
    • Effects of zinc binding on the conformational distribution of the amyloid-beta peptide based on molecular dynamics simulations
    • Li, W.; Zhang, J.; Su, Y.; Wang, J.; Qin, M.; Wang, W. Effects of zinc binding on the conformational distribution of the amyloid-beta peptide based on molecular dynamics simulations. J. Phys. Chem. B 2007, 111, 13814-13821.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 13814-13821
    • Li, W.1    Zhang, J.2    Su, Y.3    Wang, J.4    Qin, M.5    Wang, W.6
  • 30
    • 84865652373 scopus 로고    scopus 로고
    • Structures and free energy landscapes of aqueous zinc (II)-bound amyloid-beta (1-40) and zinc (II)-bound amyloid-beta (1-42) with dynamics
    • Wise-Scira, O.; Xu, L.; Perry, G.; Coskuner, O. Structures and free energy landscapes of aqueous zinc (II)-bound amyloid-beta (1-40) and zinc (II)-bound amyloid-beta (1-42) with dynamics. J. Biol. Inorg. Chem. 2012, 17, 927-938.
    • (2012) J. Biol. Inorg. Chem. , vol.17 , pp. 927-938
    • Wise-Scira, O.1    Xu, L.2    Perry, G.3    Coskuner, O.4
  • 31
    • 77956608400 scopus 로고    scopus 로고
    • Structural survey of zinc containing proteins and the development of the zinc AMBER force field (ZAFF)
    • Peters, M. B.; Yang, Y.; Wang, B.; Fusti-Molnar, L.; Weaver, M. N.; Merz, K. M., Jr. Structural Survey of Zinc Containing Proteins and the Development of the Zinc AMBER Force Field (ZAFF). J. Chem. Theory. Comput. 2010, 6, 2935-2947.
    • (2010) J. Chem. Theory. Comput. , vol.6 , pp. 2935-2947
    • Peters, M.B.1    Yang, Y.2    Wang, B.3    Fusti-Molnar, L.4    Weaver, M.N.5    Merz, K.M.6
  • 32
    • 43049141516 scopus 로고    scopus 로고
    • The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: Two new functionals and systematic testing of four M06-class functionals and 12 other functionals
    • Zhao, Y.; Truhlar, D. The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: Two new functionals and systematic testing of four M06-class functionals and 12 other functionals. Theor. Chem. Acc. 2008, 120, 215-241.
    • (2008) Theor. Chem. Acc. , vol.120 , pp. 215-241
    • Zhao, Y.1    Truhlar, D.2
  • 34
    • 0036438914 scopus 로고    scopus 로고
    • Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain
    • Crescenzi, O.; Tomaselli, S.; Guerrini, R.; Salvadori, S.; D'Ursi, A. M.; Temussi, P. A.; Picone, D. Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. Eur. J. Biochem. 2002, 269, 5642-5648.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5642-5648
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvadori, S.4    D'Ursi, A.M.5    Temussi, P.A.6    Picone, D.7
  • 35
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 1996, 14(33-38), 27-28.
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 39
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto, S.; Kollman, P. A. Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comput. Chem. 1992, 13, 952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 40
    • 84867460758 scopus 로고    scopus 로고
    • Bioinorganic chemistry of Alzheimer's disease
    • Kepp, K. P. Bioinorganic chemistry of Alzheimer's disease. Chem. Rev. 2012, 112, 5193-5239.
    • (2012) Chem. Rev. , vol.112 , pp. 5193-5239
    • Kepp, K.P.1
  • 41
    • 0037126693 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide
    • Blasie, C. A.; Berg, J. M. Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide. Biochemistry 2002, 41, 15068-15073.
    • (2002) Biochemistry , vol.41 , pp. 15068-15073
    • Blasie, C.A.1    Berg, J.M.2
  • 42
    • 38349181087 scopus 로고    scopus 로고
    • Metal-coupled folding of Cys2His2 zinc-finger
    • Li, W.; Zhang, J.; Wang, J.; Wang, W. Metal-coupled folding of Cys2His2 zinc-finger. J. Am. Chem. Soc. 2008, 130, 892-900.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 892-900
    • Li, W.1    Zhang, J.2    Wang, J.3    Wang, W.4
  • 43
    • 82555173714 scopus 로고    scopus 로고
    • Amyloid-beta peptide structure in aqueous solution varies with fragment size
    • Wise-Scira, O.; Xu, L.; Kitahara, T.; Perry, G.; Coskuner, O. Amyloid-beta peptide structure in aqueous solution varies with fragment size. J. Chem. Phys. 2011, 135, 205101-205113.
    • (2011) J. Chem. Phys. , vol.135 , pp. 205101-205113
    • Wise-Scira, O.1    Xu, L.2    Kitahara, T.3    Perry, G.4    Coskuner, O.5
  • 44
    • 84880795190 scopus 로고    scopus 로고
    • Molecular dynamics simulation and computational two-dimensional infrared spectroscopic study of model amyloid β-peptide oligomers
    • Xu, J.; Zhang, J. Z. H.; Xiang, Y. Molecular dynamics simulation and computational two-dimensional infrared spectroscopic study of model amyloid β-peptide oligomers. J. Phys. Chem. A 2013, 117, 6373-6379.
    • (2013) J. Phys. Chem. A , vol.117 , pp. 6373-6379
    • Xu, J.1    Zhang, J.Z.H.2    Xiang, Y.3
  • 45
    • 84878034899 scopus 로고    scopus 로고
    • Untangling amyloid-beta, tau, and metals in Alzheimer's disease
    • Savelieff, M. G.; Lee, S.; Liu, Y.; Lim, M. H. Untangling amyloid-beta, tau, and metals in Alzheimer's disease. ACS Chem. Biol. 2013, 8, 856-865.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 856-865
    • Savelieff, M.G.1    Lee, S.2    Liu, Y.3    Lim, M.H.4
  • 46
    • 77956508413 scopus 로고    scopus 로고
    • Can peptide folding simulations provide predictive information for aggregation propensity?
    • Lin, E. I.; Shell, M. S. Can peptide folding simulations provide predictive information for aggregation propensity? J. Phys. Chem. B 2010, 114, 11899-11908.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11899-11908
    • Lin, E.I.1    Shell, M.S.2
  • 47
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • Hou, T.; Wang, J.; Li, Y.; Wang, W. Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations. J. Chem. Inf. Model. 2011, 51, 69-82.
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 69-82
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 48
    • 0031728016 scopus 로고    scopus 로고
    • Residual structure in the Alzheimer's disease peptide: Probing the origin of a central hydrophobic cluster
    • Zhang, S.; Casey, N.; Lee, J. P. Residual structure in the Alzheimer's disease peptide: Probing the origin of a central hydrophobic cluster. Folding Des. 1998, 3, 413-422.
    • (1998) Folding Des. , vol.3 , pp. 413-422
    • Zhang, S.1    Casey, N.2    Lee, J.P.3
  • 50
    • 28544452382 scopus 로고    scopus 로고
    • Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils
    • Chen, Z.; Krause, G.; Reif, B. Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils. J. Mol. Biol. 2005, 354, 760-776.
    • (2005) J. Mol. Biol. , vol.354 , pp. 760-776
    • Chen, Z.1    Krause, G.2    Reif, B.3
  • 51
    • 34548291359 scopus 로고    scopus 로고
    • Surface structure of amyloid-beta fibrils contributes to cytotoxicity
    • Yoshiike, Y.; Akagi, T.; Takashima, A. Surface structure of amyloid-beta fibrils contributes to cytotoxicity. Biochemistry 2007, 46, 9805-9812.
    • (2007) Biochemistry , vol.46 , pp. 9805-9812
    • Yoshiike, Y.1    Akagi, T.2    Takashima, A.3
  • 52
    • 33645521792 scopus 로고    scopus 로고
    • Protein aggregation and its consequences for human disease
    • Dobson, C. M. Protein aggregation and its consequences for human disease. Protein Pept. Lett. 2006, 13, 219-227.
    • (2006) Protein Pept. Lett. , vol.13 , pp. 219-227
    • Dobson, C.M.1


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