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Volumn 18, Issue 4, 2009, Pages 792-800

9,10-Anthraquinone hinders β-aggregation: How does a small molecule interfere with Aβ-peptide amyloid fibrillation?

Author keywords

9,10 anthraquinone; Aggregation inhibition; Alzheimer's disease; Amyloid; Implicit solvent; Molecular dynamics

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; ANTHRACENE; ANTHRAQUINONE; OLIGOMER; THIOFLAVINE;

EID: 63449131863     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.87     Document Type: Article
Times cited : (106)

References (55)
  • 1
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443:774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 2
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid P-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid P-peptide. Nat Rev Mol Cell Biol 8:101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 3
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen FE, Kelly JW (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426:905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 4
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282:10311-10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 5
    • 33747484171 scopus 로고    scopus 로고
    • N-methylated peptide inhibitors of β-amyloid aggregation and toxicity, optimization of the inhibitor structure
    • Kokkoni N, Stott K. Amijee H, Mason JM, Doig AJ (2006) N-methylated peptide inhibitors of β-amyloid aggregation and toxicity, optimization of the inhibitor structure. Biochemistry 45:9906-9918.
    • (2006) Biochemistry , vol.45 , pp. 9906-9918
    • Kokkoni, N.1    Stott, K.2    Amijee, H.3    Mason, J.M.4    Doig, A.J.5
  • 6
    • 34247197575 scopus 로고    scopus 로고
    • IAPP mimic blocks Aβ cytotoxic self-assembly: Cross-suppression of amyloid toxicity of Aβ and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes
    • Yan L-M, Velkova A, Tatarek-Nossol M, Andreetto E, Kapurniotu A (2007) IAPP mimic blocks Aβ cytotoxic self-assembly: cross-suppression of amyloid toxicity of Aβ and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes. Angew Chem Int Ed Engl 46:1246-1252.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 1246-1252
    • Yan, L.-M.1    Velkova, A.2    Tatarek-Nossol, M.3    Andreetto, E.4    Kapurniotu, A.5
  • 8
    • 24044449002 scopus 로고    scopus 로고
    • Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β-amyloid
    • Kanapathipillai M, Lentzen G, Sierks M, Park CB (2005) Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β-amyloid. FEBS Lett 579: 4775-4780.
    • (2005) FEBS Lett , vol.579 , pp. 4775-4780
    • Kanapathipillai, M.1    Lentzen, G.2    Sierks, M.3    Park, C.B.4
  • 11
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: A potential role for heteroaromatic interactions
    • Porat Y, Mazor Y, Efrat S, Gazit E (2004) Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 43:14454-14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 12
    • 33645929400 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives
    • Cohen T, Frydman-Marom A, Rechter M, Gazit E (2006) Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives. Biochemistry 45:4727-4735.
    • (2006) Biochemistry , vol.45 , pp. 4727-4735
    • Cohen, T.1    Frydman-Marom, A.2    Rechter, M.3    Gazit, E.4
  • 13
    • 36749011905 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action
    • Morshedi D, Rezaei-Ghaleh N, Ebrahim-Habibi A, Ahmadian S Nemat-Gorgani M (2007) Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action. FEBS J 274:6415-6425.
    • (2007) FEBS J , vol.274 , pp. 6415-6425
    • Morshedi, D.1    Rezaei-Ghaleh, N.2    Ebrahim-Habibi, A.3    Ahmadian, S.4    Nemat-Gorgani, M.5
  • 14
    • 0030905125 scopus 로고    scopus 로고
    • Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction
    • Tomiyama T, Kaneko H, Kataoka K, Asano S, Endo N (1997) Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction. Biochem J 322 (Part 3): 859-865.
    • (1997) Biochem J , vol.322 , Issue.PART 3 , pp. 859-865
    • Tomiyama, T.1    Kaneko, H.2    Kataoka, K.3    Asano, S.4    Endo, N.5
  • 15
    • 34250373347 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone
    • Lieu VH, Wu JW, Wang SS-S, Wu C-H (2007) Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone. Biotechnol Prog 23: 698-706.
    • (2007) Biotechnol Prog , vol.23 , pp. 698-706
    • Lieu, V.H.1    Wu, J.W.2    Wang, S.S.-S.3    Wu, C.-H.4
  • 18
    • 0037195098 scopus 로고    scopus 로고
    • Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ 16-22, Aβ 16-35, and Aβ 10-35): Sequence effects
    • Ma B, Nussinov R (2002) Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ 16-22, Aβ 16-35, and Aβ 10-35): sequence effects. Proc Natl Acad Sci USA 99:14126-14131.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14126-14131
    • Ma, B.1    Nussinov, R.2
  • 19
    • 0037627715 scopus 로고    scopus 로고
    • The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35
    • Gsponer J, Haberthtir U, Caflisch A (2003) The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35. Proc Natl Acad Sci USA 100:5154-5159.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5154-5159
    • Gsponer, J.1    Haberthtir, U.2    Caflisch, A.3
  • 20
    • 0037337271 scopus 로고    scopus 로고
    • Dissecting the assembly of Aβ16-22 amyloid peptides into antiparallel β sheets
    • Klimov DK, Thirumalai D (2003) Dissecting the assembly of Aβ16-22 amyloid peptides into antiparallel β sheets. Structure 11:295-307.
    • (2003) Structure , vol.11 , pp. 295-307
    • Klimov, D.K.1    Thirumalai, D.2
  • 21
    • 4444346811 scopus 로고    scopus 로고
    • Kinetic control of dimer structure formation in amyloid fibrillogenesis
    • Hwang W, Zhang S, Kamm RD, Karplus M (2004) Kinetic control of dimer structure formation in amyloid fibrillogenesis. Proc Natl Acad Sci USA 101:12916-12921.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12916-12921
    • Hwang, W.1    Zhang, S.2    Kamm, R.D.3    Karplus, M.4
  • 22
    • 26844435756 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments
    • Buchete N-V, Tycko R, Hummer G (2005) Molecular dynamics simulations of Alzheimer's β-amyloid protofilaments. J Mol Biol 353:804-821.
    • (2005) J Mol Biol , vol.353 , pp. 804-821
    • Buchete, N.-V.1    Tycko, R.2    Hummer, G.3
  • 23
    • 19544375553 scopus 로고    scopus 로고
    • Sequence dependence of amyloid fibril formation: Insights from molecular dynamics simulations
    • de la Paz ML, de Mori GMS, Serrano L, Colombo G (2005) Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations. J Mol Biol 349:583-596.
    • (2005) J Mol Biol , vol.349 , pp. 583-596
    • de la Paz, M.L.1    de Mori, G.M.S.2    Serrano, L.3    Colombo, G.4
  • 24
    • 33748278029 scopus 로고    scopus 로고
    • Structures of soluble amyloid oligomers from computer simulations
    • Melquiond A, Mousseau N, Derreumaux P (2006) Structures of soluble amyloid oligomers from computer simulations. Proteins 65:180-191.
    • (2006) Proteins , vol.65 , pp. 180-191
    • Melquiond, A.1    Mousseau, N.2    Derreumaux, P.3
  • 25
    • 10844230140 scopus 로고    scopus 로고
    • Replica exchange molecular dynamics simulations of amyloid peptide aggregation
    • Cecchini M, Rao F, Seeber M, Caflisch A (2004) Replica exchange molecular dynamics simulations of amyloid peptide aggregation. J Chem Phys 121:10748-10756.
    • (2004) J Chem Phys , vol.121 , pp. 10748-10756
    • Cecchini, M.1    Rao, F.2    Seeber, M.3    Caflisch, A.4
  • 26
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, Vendruscolo M, Favrin G (2007) Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput Biol 3:1727-1738.
    • (2007) PLoS Comput Biol , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 27
    • 34047157022 scopus 로고    scopus 로고
    • Hydrophobic cooperativity as a mechanism for amyloid nucleation
    • Hills RD, Brooks CL (2007) Hydrophobic cooperativity as a mechanism for amyloid nucleation. J Mol Biol 368: 894-901.
    • (2007) J Mol Biol , vol.368 , pp. 894-901
    • Hills, R.D.1    Brooks, C.L.2
  • 28
    • 50349099883 scopus 로고    scopus 로고
    • Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses
    • Simone AD, Esposito L, Pedone C, Vitagliano L (2008) Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses. Biophys J 95:1965-1973.
    • (2008) Biophys J , vol.95 , pp. 1965-1973
    • Simone, A.D.1    Esposito, L.2    Pedone, C.3    Vitagliano, L.4
  • 29
    • 33644821609 scopus 로고    scopus 로고
    • A molecular dynamics approach to the structural characterization of amyloid aggregation
    • Cecchini M, Curcio R. Pappalardo M, Melki R. Caflisch A (2006) A molecular dynamics approach to the structural characterization of amyloid aggregation. J Mol Biol 357: 1306-1321.
    • (2006) J Mol Biol , vol.357 , pp. 1306-1321
    • Cecchini, M.1    Curcio, R.2    Pappalardo, M.3    Melki, R.4    Caflisch, A.5
  • 30
    • 36049022567 scopus 로고    scopus 로고
    • New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides
    • Soto P, Griffin MA, Shea J-E (2007) New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides. Biophys J 93: 3015-3025.
    • (2007) Biophys J , vol.93 , pp. 3015-3025
    • Soto, P.1    Griffin, M.A.2    Shea, J.-E.3
  • 31
    • 61849111130 scopus 로고    scopus 로고
    • Cognitive performance recovery of Alzheimer's disease model mice by modulating early soluble amyloidal assemblies
    • Frydman-Marom A, Rechter M, Bram V. Shalev DE, Gazit E (2009) Cognitive performance recovery of Alzheimer's disease model mice by modulating early soluble amyloidal assemblies. Angew Chem Int Ed Engl 48:1981-1986.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 1981-1986
    • Frydman-Marom, A.1    Rechter, M.2    Bram, V.3    Shalev, D.E.4    Gazit, E.5
  • 34
    • 33748525884 scopus 로고    scopus 로고
    • Computational models for the prediction of polypeptide aggregation propensity
    • Caflisch A (2006) Computational models for the prediction of polypeptide aggregation propensity. Curr Opin Chem Biol 10:437-444.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 437-444
    • Caflisch, A.1
  • 35
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia GG, Cavalli A, Pellarin R. Caflisch A (2005) Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci 14:2723-2734.
    • (2005) Protein Sci , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 36
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic affects for Alzheimer's β-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M (2004) Curcumin has potent anti-amyloidogenic affects for Alzheimer's β-amyloid fibrils in vitro. J Neurosci Res 75:742-750.
    • (2004) J Neurosci Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 37
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of Amyloid B (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
    • Bartolini M. Bertucci C, Bolognesi ML, Cavalli A, Melchiorre C, Andrisano V (2007) Insight into the kinetic of Amyloid B (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action. Chem Biol Chem 8: 2152-2161.
    • (2007) Chem Biol Chem , vol.8 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 38
    • 44449160026 scopus 로고    scopus 로고
    • Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril Thioflavin-T interactions: Implications for mechanistic studies of β-cell death
    • Meng F, Marek P, Potter KJ, Verchere CB, Raleigh DP (2008) Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril Thioflavin-T interactions: implications for mechanistic studies of β-cell death. Biochemistry 47:6016-6024.
    • (2008) Biochemistry , vol.47 , pp. 6016-6024
    • Meng, F.1    Marek, P.2    Potter, K.J.3    Verchere, C.B.4    Raleigh, D.P.5
  • 39
    • 84986512474 scopus 로고    scopus 로고
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M (1983) CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217.
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M (1983) CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217.
  • 40
  • 41
    • 0346951125 scopus 로고
    • Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 1. Application to neutral molecules as models for polypeptides
    • No K, Grant J, Scheraga H (1990) Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 1. Application to neutral molecules as models for polypeptides. J Phys Chem 94: 4732-4739.
    • (1990) J Phys Chem , vol.94 , pp. 4732-4739
    • No, K.1    Grant, J.2    Scheraga, H.3
  • 42
    • 33751553791 scopus 로고
    • Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 2. Application to ionic and aromatic molecules as models for polypeptides
    • No K. Grant J, Jhon M. Scheraga H (1990) Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 2. Application to ionic and aromatic molecules as models for polypeptides. J Phys Chem 94:4740-4746.
    • (1990) J Phys Chem , vol.94 , pp. 4740-4746
    • No, K.1    Grant, J.2    Jhon, M.3    Scheraga, H.4
  • 43
    • 0041831011 scopus 로고    scopus 로고
    • Electrostatic interaction of π-acidic amides with hydrogen-bond acceptors
    • Li Y, Snyder L, Langley DR (2003) Electrostatic interaction of π-acidic amides with hydrogen-bond acceptors. Bioorganic & Medicinal Chemistry Letters 13:3261-3266.
    • (2003) Bioorganic & Medicinal Chemistry Letters , vol.13 , pp. 3261-3266
    • Li, Y.1    Snyder, L.2    Langley, D.R.3
  • 44
    • 0001204389 scopus 로고    scopus 로고
    • Temperature dependence of the rigid-body motion of Anthraquinone
    • Fu Y, Brock CP (1998) Temperature dependence of the rigid-body motion of Anthraquinone. Acta Cryst B 54: 308-315.
    • (1998) Acta Cryst B , vol.54 , pp. 308-315
    • Fu, Y.1    Brock, C.P.2
  • 45
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H, III. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein 2:404-410.
    • (1993) Protein , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 46
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • Meyer EA, Castellano RK. Diederieh F (2003) Interactions with aromatic rings in chemical and biological recognition. Angew Chem Int Ed Engl 42:1210-1250.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederieh, F.3
  • 49
    • 2942701830 scopus 로고    scopus 로고
    • Cation-π versus anion-π interactions: A comparative ab initio study based on energetic, electron charge density and aromatic features
    • Garau C, Frontera A, Quinonero D, Ballester P, Costa A, Deya PM. (2004) Cation-π versus anion-π interactions: a comparative ab initio study based on energetic, electron charge density and aromatic features. Chem Phys Lett 392:85-89.
    • (2004) Chem Phys Lett , vol.392 , pp. 85-89
    • Garau, C.1    Frontera, A.2    Quinonero, D.3    Ballester, P.4    Costa, A.5    Deya, P.M.6
  • 50
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • Pellarin R, Caflisch A (2006) Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 360:882-892.
    • (2006) J Mol Biol , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 51
    • 35748943830 scopus 로고    scopus 로고
    • Pathways and intermediates of amyloid fibril formation
    • Pellarin R, Guarnera E, Caflisch A (2007) Pathways and intermediates of amyloid fibril formation. J Mol Biol 374: 917-924.
    • (2007) J Mol Biol , vol.374 , pp. 917-924
    • Pellarin, R.1    Guarnera, E.2    Caflisch, A.3
  • 54
    • 0030801497 scopus 로고    scopus 로고
    • Inhibitors of Aβ peptide aggregation as potential anti-Alzheimer agents
    • Bandiera T, Lansen J, Post C, Varasi M (1997) Inhibitors of Aβ peptide aggregation as potential anti-Alzheimer agents. Curr Med Chem 4:159-170.
    • (1997) Curr Med Chem , vol.4 , pp. 159-170
    • Bandiera, T.1    Lansen, J.2    Post, C.3    Varasi, M.4


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