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Volumn 2, Issue 6, 2011, Pages 281-287

Binding modes of thioflavin T molecules to prion peptide assemblies identified by using scanning tunneling microscopy

Author keywords

amyloid; binding mode; GNNQQNY; labeling molecule; scanning tunneling microscopy; thioflavin T

Indexed keywords

PRION PROTEIN; THIOFLAVINE;

EID: 79959249196     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn200006h     Document Type: Article
Times cited : (37)

References (39)
  • 3
    • 48849104834 scopus 로고    scopus 로고
    • Molecules that target beta-amyloid
    • Stains, C. I., Mondal, K., and Ghosh, I. (2007) Molecules that target beta-amyloid ChemMedChem 2 (12) 1674-1692
    • (2007) ChemMedChem , vol.2 , Issue.12 , pp. 1674-1692
    • Stains, C.I.1    Mondal, K.2    Ghosh, I.3
  • 4
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning, M. (2009) Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status J. Chem. Biol. 3, 1-18
    • (2009) J. Chem. Biol. , vol.3 , pp. 1-18
    • Groenning, M.1
  • 9
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • DOI 10.1111/j.1747-0285.2005.00318.x
    • Porat, Y., Abramowitz, A., and Gazit, E. (2006) Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism Chem. Biol. Drug Des. 67 (1) 27-37 (Pubitemid 43881385)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 10
    • 14844303913 scopus 로고    scopus 로고
    • Evidence for the presence of three distinct binding sites for the thioflavin T class of Alzheimer's disease PET imaging agents on β-amyloid peptide fibrils
    • DOI 10.1074/jbc.M412056200
    • Lockhart, A., Ye, L., Judd, D. B., Merritt, A. T., Lowe, P. N., Morgenstern, J. L., Hong, G., Gee, A. D., and Brown, J. (2005) Evidence for the presence of three distinct binding sites for the thioflavin T class of Alzheimer's disease PET imaging agents on beta-amyloid peptide fibrils J. Biol. Chem. 280 (9) 7677-7684 (Pubitemid 40349660)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7677-7684
    • Lockhart, A.1    Ye, L.2    Judd, D.B.3    Merrittu, A.T.4    Lowe, P.N.5    Morgenstern, J.L.6    Hong, G.7    Gee, A.D.8    Brown, J.9
  • 11
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • DOI 10.1016/j.jsb.2004.08.002, PII S1047847704001534
    • Krebs, M. R. H., Bromley, E. H. C., and Donald, A. M. (2005) The binding of thioflavin-T to amyloid fibrils: localisation and implications J. Struct. Biol. 149 (1) 30-37 (Pubitemid 40051399)
    • (2005) Journal of Structural Biology , vol.149 , Issue.1 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 12
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study
    • DOI 10.1016/j.febslet.2005.10.048, PII S0014579305013177
    • Dzwolak, W. and Pecul, M. (2005) Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study FEBS Lett. 579 (29) 6601-6603 (Pubitemid 41682446)
    • (2005) FEBS Letters , vol.579 , Issue.29 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 13
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • DOI 10.1074/jbc.C300049200
    • Ban, T., Hamada, D., Hasegawa, K., Naiki, H., and Goto, Y. (2003) Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence J. Biol. Chem. 278 (19) 16462-16465 (Pubitemid 36799502)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawall, K.3    Naiki, H.4    Goto, Y.5
  • 15
    • 0035902875 scopus 로고    scopus 로고
    • Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain
    • DOI 10.1016/S0024-3205(01)01232-2, PII S0024320501012322
    • Klunk, W. E., Wang, Y. M., Huang, G. F., Debnath, M. L., Holt, D. P., and Mathis, C. A. (2001) Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain Life Sci. 69 (13) 1471-1484 (Pubitemid 32786721)
    • (2001) Life Sciences , vol.69 , Issue.13 , pp. 1471-1484
    • Klunk, W.E.1    Wang, Y.2    Huang, G.-F.3    Debnath, M.L.4    Holt, D.P.5    Mathis, C.A.6
  • 17
    • 59449106971 scopus 로고    scopus 로고
    • Destruction of Amyloid Fibrils of a beta(2)-Microglobulin Fragment by Laser Beam Irradiation
    • Ozawa, D., Yagi, H., Ban, T., Kameda, A., Kawakami, T., Naiki, H., and Goto, Y. (2009) Destruction of Amyloid Fibrils of a beta(2)-Microglobulin Fragment by Laser Beam Irradiation J. Biol. Chem. 284 (2) 1009-1017
    • (2009) J. Biol. Chem. , vol.284 , Issue.2 , pp. 1009-1017
    • Ozawa, D.1    Yagi, H.2    Ban, T.3    Kameda, A.4    Kawakami, T.5    Naiki, H.6    Goto, Y.7
  • 19
    • 45749094206 scopus 로고    scopus 로고
    • Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site
    • DOI 10.1021/ja7109822
    • Harel, M., Sonoda, L. K., Silman, I., Sussman, J. L., and Rosenberry, T. L. (2008) Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site J. Am. Chem. Soc. 130 (25) 7856-7861 (Pubitemid 351875060)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 7856-7861
    • Harel, M.1    Sonoda, L.K.2    Silman, I.3    Sussman, J.L.4    Rosenberry, T.L.5
  • 20
    • 0026451628 scopus 로고
    • Binding of the Dye Congo Red to the Amyloid Protein Pig Insulin Reveals a Novel Homology Amongst Amyloid-Forming Peptide Sequences
    • Turnell, W. G. and Finch, J. T. (1992) Binding of the Dye Congo Red to the Amyloid Protein Pig Insulin Reveals a Novel Homology Amongst Amyloid-Forming Peptide Sequences J. Mol. Biol. 227 (4) 1205-1223
    • (1992) J. Mol. Biol. , vol.227 , Issue.4 , pp. 1205-1223
    • Turnell, W.G.1    Finch, J.T.2
  • 21
    • 58149326746 scopus 로고    scopus 로고
    • Molecular Mechanism of Thioflavin-T Binding to the Surface of beta-Rich Peptide Self-Assemblies
    • Biancalana, M., Makabe, K., Koide, A., and Koide, S. (2009) Molecular Mechanism of Thioflavin-T Binding to the Surface of beta-Rich Peptide Self-Assemblies J. Mol. Biol. 385 (4) 1052-1063
    • (2009) J. Mol. Biol. , vol.385 , Issue.4 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 22
    • 44549084117 scopus 로고    scopus 로고
    • On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2
    • Sabate, R., Lascu, I., and Saupe, S. J. (2008) On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2 J. Struct. Biol. 162 (3) 387-396
    • (2008) J. Struct. Biol. , vol.162 , Issue.3 , pp. 387-396
    • Sabate, R.1    Lascu, I.2    Saupe, S.J.3
  • 23
    • 34248670403 scopus 로고    scopus 로고
    • Study on the binding of Thioflavin T to β-sheet-rich and non-β-sheet cavities
    • DOI 10.1016/j.jsb.2006.12.010, PII S1047847706003923
    • Groenning, M., Olsen, L., van de Weert, M., Flink, J. M., Frokjaer, S., and Jorgensen, F. S. (2007) Study on the binding of Thioflavin T to beta-sheet-rich and non-beta-sheet cavities J. Struct. Biol. 158 (3) 358-369 (Pubitemid 46766672)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 358-369
    • Groenning, M.1    Olsen, L.2    Van De Weert, M.3    Flink, J.M.4    Frokjaer, S.5    Jorgensen, F.S.6
  • 24
    • 33846781516 scopus 로고    scopus 로고
    • Dual binding modes of Congo red to amyloid protofibril surface observed in molecular dynamics simulations
    • DOI 10.1021/ja0662772
    • Wu, C., Wang, Z. X., Lei, H. X., Zhang, W., and Duan, Y. (2007) Dual binding modes of Congo red to amyloid protofibril surface observed in molecular dynamics simulations J. Am. Chem. Soc. 129 (5) 1225-1232 (Pubitemid 46208593)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.5 , pp. 1225-1232
    • Wu, C.1    Wang, Z.2    Lei, H.3    Zhang, W.4    Duan, Y.5
  • 25
    • 84954358136 scopus 로고    scopus 로고
    • The Binding of Thioflavin T and Its Neutral Analog BTA-1 to Protofibrils of the Alzheimer's Disease A beta(16-22) Peptide Probed by Molecular Dynamics Simulations
    • Wu, C., Wang, Z. X., Lei, H. X., Duan, Y., Bowers, M. T., and Shea, J. E. (2008) The Binding of Thioflavin T and Its Neutral Analog BTA-1 to Protofibrils of the Alzheimer's Disease A beta(16-22) Peptide Probed by Molecular Dynamics Simulations J. Mol. Biol. 384 (3) 718-729
    • (2008) J. Mol. Biol. , vol.384 , Issue.3 , pp. 718-729
    • Wu, C.1    Wang, Z.X.2    Lei, H.X.3    Duan, Y.4    Bowers, M.T.5    Shea, J.E.6
  • 26
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils
    • DOI 10.1016/S0197-4580(97)00164-4, PII S0197458097001644
    • Carter, D. B. and Chou, K. C. (1998) A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils Neurobiol. Aging 19 (1) 37-40 (Pubitemid 28167793)
    • (1998) Neurobiology of Aging , vol.19 , Issue.1 , pp. 37-40
    • Carter, D.B.1    Chou, K.-C.2
  • 27
    • 67349128044 scopus 로고    scopus 로고
    • Amyloid-beta (1-42) Folding Multiplicity and Single Molecule Binding Behavior Studied by STM
    • Ma, X. J., Liu, L., Mao, X. B., Niu, L., Deng, K., Wu, W. H., Li, Y. M., Yang, Y. L., and Wang, C. (2009) Amyloid-beta (1-42) Folding Multiplicity and Single Molecule Binding Behavior Studied by STM J. Mol. Biol. 388, 894-901
    • (2009) J. Mol. Biol. , vol.388 , pp. 894-901
    • Ma, X.J.1    Liu, L.2    Mao, X.B.3    Niu, L.4    Deng, K.5    Wu, W.H.6    Li, Y.M.7    Yang, Y.L.8    Wang, C.9
  • 29
    • 67650756419 scopus 로고    scopus 로고
    • Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy
    • Mao, X. B., Ma, X. J., Liu, L., Niu, L., Yang, Y. L., and Wang, C. (2009) Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy J. Struct. Biol. 167 (3) 209-215
    • (2009) J. Struct. Biol. , vol.167 , Issue.3 , pp. 209-215
    • Mao, X.B.1    Ma, X.J.2    Liu, L.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 30
    • 68649092815 scopus 로고    scopus 로고
    • Molecular-Level Evidence of the Surface-Induced Transformation of Peptide Structures Revealed by Scanning Tunneling Microscopy
    • Mao, X. B., Wang, Y. B., Liu, L., Niu, L., Yang, Y. L., and Wang, C. (2009) Molecular-Level Evidence of the Surface-Induced Transformation of Peptide Structures Revealed by Scanning Tunneling Microscopy Langmuir 25 (16) 8849-8853
    • (2009) Langmuir , vol.25 , Issue.16 , pp. 8849-8853
    • Mao, X.B.1    Wang, Y.B.2    Liu, L.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 31
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • DOI 10.1038/nature03680
    • Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O., Riekel, C., Grothe, R., and Eisenberg, D. (2005) Structure of the cross-beta spine of amyloid-like fibrils Nature 435 (7043) 773-778 (Pubitemid 40839722)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5    Grothe, R.6    Eisenberg, D.7
  • 33
    • 71949110860 scopus 로고    scopus 로고
    • Chaperon-Mediated Single Molecular Approach Toward Modulating Aβ Peptide Aggregation
    • Liu, L., Zhang, L., Mao, X., Niu, L., Yang, Y., and Wang, C. (2009) Chaperon-Mediated Single Molecular Approach Toward Modulating Aβ Peptide Aggregation Nano Lett. 9 (12) 4066-4072
    • (2009) Nano Lett. , vol.9 , Issue.12 , pp. 4066-4072
    • Liu, L.1    Zhang, L.2    Mao, X.3    Niu, L.4    Yang, Y.5    Wang, C.6
  • 34
    • 79953734661 scopus 로고    scopus 로고
    • Molecular level studies on binding modes of labeling molecules with polyalanine peptides
    • DOI: 10.1039/c0nr00782j.
    • Mao, X. B., Wang, C. X., Ma, X. J., Zhang, M., Liu, L., Zhang, L., Niu, L., Zeng, Q. D., Yang, Y. L., and Wang, C. Molecular level studies on binding modes of labeling molecules with polyalanine peptides. Nanoscale 2011, DOI: 10.1039/c0nr00782j.
    • (2011) Nanoscale
    • Mao, X.B.1    Wang, C.X.2    Ma, X.J.3    Zhang, M.4    Liu, L.5    Zhang, L.6    Niu, L.7    Zeng, Q.D.8    Yang, Y.L.9    Wang, C.10
  • 35
    • 0035420570 scopus 로고    scopus 로고
    • Identification of hydrogen bond characterizations of isomeric 4Bpy and 2Bpy by STM
    • DOI 10.1002/sia.1046
    • Xu, B., Yin, S. X., Wang, C., Zeng, Q. D., Qiu, X. H., and Bai, C. L. (2001) Identification of hydrogen bond characterizations of isomeric 4Bpy and 2Bpy by STM Surf. Interface Anal. 32, 245-247 (Pubitemid 32805617)
    • (2001) Surface and Interface Analysis , vol.32 , Issue.1 , pp. 245-247
    • Chen, A.1    Cao, E.-H.2    Sun, X.-G.3    Qin, J.-F.4    Liu, D.5    Wang, C.6    Bai, C.-L.7
  • 36
    • 36148995807 scopus 로고    scopus 로고
    • Matrix-molecule induced chiral enhancement effect of binary supramolecular liquid crystals
    • DOI 10.1039/b710701c
    • Ma, X. J., Shen, Y. T., Deng, K., Tang, H., Lei, S. B., Wang, C., Yang, Y. L., and Feng, X. Z. (2007) Matrix-molecule induced chiral enhancement effect of binary supramolecular liquid crystals J. Mater. Chem. 17 (44) 4699-4704 (Pubitemid 350114560)
    • (2007) Journal of Materials Chemistry , vol.17 , Issue.44 , pp. 4699-4704
    • Ma, X.-J.1    Shen, Y.-T.2    Deng, K.3    Tang, H.4    Lei, S.-B.5    Wang, C.6    Yang, Y.-L.7    Feng, X.-Z.8
  • 37
    • 0031176371 scopus 로고    scopus 로고
    • Source of image contrast in STM images of functionalized alkanes on graphite: A systematic functional group approach
    • Claypool, C. L., Faglioni, F., Goddard, W. A., Gray, H. B., Lewis, N. S., and Marcus, R. A. (1997) Source of image contrast in STM images of functionalized alkanes on graphite: A systematic functional group approach J. Phys. Chem. B 101 (31) 5978-5995 (Pubitemid 127611934)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.31 , pp. 5978-5995
    • Claypool, C.L.1    Faglioni, F.2    Goddard III, W.A.3    Gray, H.B.4    Lewis, N.S.5    Marcus, R.A.6
  • 38
    • 33749275052 scopus 로고    scopus 로고
    • Functional group identification in scanning tunneling microscopy of molecular adsorbates
    • Cyr, D. M., Venkataraman, B., Flynn, G. W., Black, A., and Whitesides, G. M. (1996) Functional group identification in scanning tunneling microscopy of molecular adsorbates J. Phys. Chem. 100 (32) 13747-13759 (Pubitemid 126814707)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.32 , pp. 13747-13759
    • Cyr, D.M.1    Venkataraman, B.2    Flynn, G.W.3    Black, A.4    Whitesides, G.M.5
  • 39
    • 48149107920 scopus 로고    scopus 로고
    • Thioflavin derivatives as markers for amyloid-beta fibrils: Insights into structural features important for high-affinity binding
    • Yona, R. L., Mazeres, S., Faller, P., and Gras, E. (2008) Thioflavin derivatives as markers for amyloid-beta fibrils: Insights into structural features important for high-affinity binding ChemMedChem 3 (1) 63-66
    • (2008) ChemMedChem , vol.3 , Issue.1 , pp. 63-66
    • Yona, R.L.1    Mazeres, S.2    Faller, P.3    Gras, E.4


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