메뉴 건너뛰기




Volumn 110, Issue , 2014, Pages 97-105

Photophysical study of Thioflavin T as fluorescence marker of amyloid fibrils

Author keywords

Amyloid fibril; Fluorescent marker; Molecular rotor; Photophysical properties; Thioflavin T; TICT

Indexed keywords

BINDING ENERGY; CHEMICAL SENSORS; FLUORESCENCE; GLYCOPROTEINS; MAMMALS;

EID: 84905094067     PISSN: 01437208     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dyepig.2014.05.004     Document Type: Article
Times cited : (99)

References (47)
  • 1
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • R.N. Melanie Techniques to study amyloid fibril formation in vitro Methods 34 1 2004, Sep 151 160
    • (2004) Methods , vol.34 , Issue.1 , pp. 151-160
    • Melanie, R.N.1
  • 2
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils - Current status
    • M. Groenning Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils - current status J Chem Biol 3 1 2010 1 18
    • (2010) J Chem Biol , vol.3 , Issue.1 , pp. 1-18
    • Groenning, M.1
  • 3
    • 84866388266 scopus 로고    scopus 로고
    • Molecular rotors: What lies behind the high sensitivity of the Thioflavin-T fluorescent marker
    • N. Amdursky, Y. Erez, and D. Huppert Molecular rotors: what lies behind the high sensitivity of the Thioflavin-T fluorescent marker Acc Chem Res 45 9 2012 1548 1557
    • (2012) Acc Chem Res , vol.45 , Issue.9 , pp. 1548-1557
    • Amdursky, N.1    Erez, Y.2    Huppert, D.3
  • 4
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • DOI 10.1074/jbc.C300049200
    • T. Ban, D. Hamada, K. Hasegawa, H. Naiki, and Y. Goto Direct observation of amyloid fibril growth monitored by Thioflavin T fluorescence J Biol Chem 278 19 2003 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
  • 5
    • 34250890734 scopus 로고    scopus 로고
    • Thioflavin T fluorescence anisotropy: An alternative technique for the study of amyloid aggregation
    • DOI 10.1016/j.bbrc.2007.06.063, PII S0006291X0701234X
    • R. Sabaté, and S.J. Saupe Thioflavin T fluorescence anisotropy: an alternative technique for the study of amyloid aggregation Biochem Biophys Res Commun 360 1 2007 135 138 (Pubitemid 46990334)
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , Issue.1 , pp. 135-138
    • Sabate, R.1    Saupe, S.J.2
  • 7
    • 77956255164 scopus 로고    scopus 로고
    • Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method
    • A.A. Reinke, G.A. Abulwerdi, and J.E. Gestwicki Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method ChemBioChem 11 13 2010 1889 1895
    • (2010) ChemBioChem , vol.11 , Issue.13 , pp. 1889-1895
    • Reinke, A.A.1    Abulwerdi, G.A.2    Gestwicki, J.E.3
  • 8
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • D.J. Selkoe Folding proteins in fatal ways Nature 426 6968 2003 900 904 (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 10
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid [beta]-peptide Nat Rev Mol Cell Biol 8 2 2007 101 112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 11
    • 77955444936 scopus 로고    scopus 로고
    • Identifying the bond responsible for the fluorescence modulation in an amyloid fibril sensor
    • A. Srivastava, P.K. Singh, M. Kumbhakar, T. Mukherjee, S. Chattopadyay, and H. Pal et al. Identifying the bond responsible for the fluorescence modulation in an amyloid fibril sensor Chem Eur J 16 30 2010 9257 9263
    • (2010) Chem Eur J , vol.16 , Issue.30 , pp. 9257-9263
    • Srivastava, A.1    Singh, P.K.2    Kumbhakar, M.3    Mukherjee, T.4    Chattopadyay, S.5    Pal, H.6
  • 13
    • 58149175632 scopus 로고    scopus 로고
    • Thioflavin T as a molecular rotor: Fluorescent properties of Thioflavin T in solvents with different viscosity
    • V.I. Stsiapura, A.A. Maskevich, V.A. Kuzmitsky, V.N. Uversky, I.M. Kuznetsova, and K.K. Turoverov Thioflavin T as a molecular rotor: fluorescent properties of Thioflavin T in solvents with different viscosity J Phys Chem B 112 49 2008 15893 15902
    • (2008) J Phys Chem B , vol.112 , Issue.49 , pp. 15893-15902
    • Stsiapura, V.I.1    Maskevich, A.A.2    Kuzmitsky, V.A.3    Uversky, V.N.4    Kuznetsova, I.M.5    Turoverov, K.K.6
  • 14
    • 77955616232 scopus 로고    scopus 로고
    • Charge transfer process determines ultrafast excited state deactivation of Thioflavin T in low-viscosity solvents
    • V.I. Stsiapura, A.A. Maskevich, S.A. Tikhomirov, and O.V. Buganov Charge transfer process determines ultrafast excited state deactivation of Thioflavin T in low-viscosity solvents J Phys Chem A 114 32 2010 900 904
    • (2010) J Phys Chem A , vol.114 , Issue.32 , pp. 900-904
    • Stsiapura, V.I.1    Maskevich, A.A.2    Tikhomirov, S.A.3    Buganov, O.V.4
  • 15
    • 67349108090 scopus 로고    scopus 로고
    • Steady-state and time-resolved emission studies of Thioflavin-T
    • L. Naik, A.B. Naik, and H. Pal Steady-state and time-resolved emission studies of Thioflavin-T J Photochem Photobiol A 204 2 2009 161 167
    • (2009) J Photochem Photobiol A , vol.204 , Issue.2 , pp. 161-167
    • Naik, L.1    Naik, A.B.2    Pal, H.3
  • 17
    • 78149417674 scopus 로고    scopus 로고
    • Fluorescence quantum yield of Thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils
    • A.I. Sulatskaya, A.A. Maskevich, I.M. Kuznetsova, V.N. Uversky, and K.K. Turoverov Fluorescence quantum yield of Thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils PLoS One 5 10 2010 e15385
    • (2010) PLoS One , vol.5 , Issue.10 , pp. 15385
    • Sulatskaya, A.I.1    Maskevich, A.A.2    Kuznetsova, I.M.3    Uversky, V.N.4    Turoverov, K.K.5
  • 18
    • 65249166593 scopus 로고    scopus 로고
    • Photophysical studies on the noncovalent interaction of Thioflavin T with cucurbit [n] uril macrocycles
    • S. Dutta Choudhury, J. Mohanty, H.P. Upadhyaya, A.C. Bhasikuttan, and H. Pal Photophysical studies on the noncovalent interaction of Thioflavin T with cucurbit [n] uril macrocycles J Phys Chem B 113 7 2009 1891 1898
    • (2009) J Phys Chem B , vol.113 , Issue.7 , pp. 1891-1898
    • Dutta Choudhury, S.1    Mohanty, J.2    Upadhyaya, H.P.3    Bhasikuttan, A.C.4    Pal, H.5
  • 19
    • 75749101746 scopus 로고    scopus 로고
    • Cooperative metal ion binding to a cucurbit [7] uril-Thioflavin T complex: Demonstration of a stimulus-responsive fluorescent supramolecular capsule
    • S.D. Choudhury, J. Mohanty, H. Pal, and A.C. Bhasikuttan Cooperative metal ion binding to a cucurbit [7] uril-Thioflavin T complex: demonstration of a stimulus-responsive fluorescent supramolecular capsule J Am Chem Soc 132 4 2010 1395 1401
    • (2010) J Am Chem Soc , vol.132 , Issue.4 , pp. 1395-1401
    • Choudhury, S.D.1    Mohanty, J.2    Pal, H.3    Bhasikuttan, A.C.4
  • 20
    • 77951780294 scopus 로고    scopus 로고
    • Viscosity effect on the ultrafast bond twisting dynamics in an amyloid fibril sensor: Thioflavin-T
    • P.K. Singh, M. Kumbhakar, H. Pal, and S. Nath Viscosity effect on the ultrafast bond twisting dynamics in an amyloid fibril sensor: Thioflavin-T J Phys Chem B 114 17 2010 5920 5927
    • (2010) J Phys Chem B , vol.114 , Issue.17 , pp. 5920-5927
    • Singh, P.K.1    Kumbhakar, M.2    Pal, H.3    Nath, S.4
  • 24
    • 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
    • M.R.H. Krebs, E.H.C. Bromley, and A.M. Donald The binding of Thioflavin-T to amyloid fibrils: localisation and implications J Struct Biol 149 1 2005 Jan 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
  • 27
    • 84872858620 scopus 로고    scopus 로고
    • Thioflavine-T and Congo red reveal the polymorphism of insulin amyloid fibrils when probed by polarization-resolved fluorescence microscopy
    • J. Duboisset, P. Ferrand, W. He, X. Wang, H. Rigneault, and S. Brasselet Thioflavine-T and Congo red reveal the polymorphism of insulin amyloid fibrils when probed by polarization-resolved fluorescence microscopy J Phys Chem B 117 3 2013 784 788
    • (2013) J Phys Chem B , vol.117 , Issue.3 , pp. 784-788
    • Duboisset, J.1    Ferrand, P.2    He, W.3    Wang, X.4    Rigneault, H.5    Brasselet, S.6
  • 28
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-[beta] in Alzheimer's disease
    • F.M. LaFerla, K.N. Green, and S. Oddo Intracellular amyloid-[beta] in Alzheimer's disease Nat Rev Neurosci 8 7 2007 499 509
    • (2007) Nat Rev Neurosci , vol.8 , Issue.7 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 29
    • 33747652958 scopus 로고    scopus 로고
    • Distinct early folding and aggregation properties of Alzheimer amyloid-β peptides Aβ40 and Aβ42: Stable trimer or tetramer formation by Aβ42
    • DOI 10.1074/jbc.M602363200
    • Y. Chen, and C.G. Glabe Distinct early folding and aggregation properties of Alzheimer amyloid-β peptides Aβ40 and Aβ42: stable trimer or tetramer formation by Aβ42 J Biol Chem 281 34 2006 24414 24422 (Pubitemid 44274214)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24414-24422
    • Chen, Y.-R.1    Glabe, C.G.2
  • 30
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • D.M. Walsh, and D.J. Selkoe Aβ oligomers - a decade of discovery J Neurochem 101 5 2007 1172 1184
    • (2007) J Neurochem , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 31
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • DOI 10.1146/annurev.biochem.66.1.385
    • J.D. Harper, and P.T. Lansbury Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu Rev Biochem 66 1 1997 385 407 (Pubitemid 27274662)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 32
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1021/bi00069a001
    • J.T. Jarrett, E.P. Berger, and P.T. Lansbury The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 32 18 1993 4693 4697 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 33
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • DOI 10.1074/jbc.M210207200
    • W.B. Stine Jr., K.N. Dahlgren, G.A. Krafft, and M.J. LaDu In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis J Biol Chem 278 13 2003 11612 11622 (Pubitemid 36792723)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 35
    • 77951092364 scopus 로고    scopus 로고
    • Exchange-dynamics of a neutral hydrophobic dye in micellar solutions studied by fluorescence correlation spectroscopy
    • J. Bordello, M. Novo, and W. Al-Soufi Exchange-dynamics of a neutral hydrophobic dye in micellar solutions studied by fluorescence correlation spectroscopy J Colloid Interface Sci 345 2010 369 376
    • (2010) J Colloid Interface Sci , vol.345 , pp. 369-376
    • Bordello, J.1    Novo, M.2    Al-Soufi, W.3
  • 36
    • 0035331648 scopus 로고    scopus 로고
    • Principal component global analysis of fluorescence and absorption spectra of 2-(2′-hydroxyphenyl)benzimidazole
    • DOI 10.1366/0003702011952253
    • W. Al-Soufi, M. Novo, and M. Mosquera Principal component global analysis of fluorescence and absorption spectra of 2-(2'-hydroxyphenyl)benzimidazole Appl Spectrosc 55 5 2001 630 636 (Pubitemid 32546950)
    • (2001) Applied Spectroscopy , vol.55 , Issue.5 , pp. 630-636
    • Al-Soufi, W.1    Novo, M.2    Mosquera, M.3
  • 38
    • 44349108313 scopus 로고    scopus 로고
    • Formula for the viscosity of a glycerol-water mixture
    • DOI 10.1021/ie071349z
    • N. Cheng Formula for the viscosity of a glycerol-water mixture Ind Eng Chem Res 47 9 2008 3285 3288 (Pubitemid 351747446)
    • (2008) Industrial and Engineering Chemistry Research , vol.47 , Issue.9 , pp. 3285-3288
    • Cheng, N.-S.1
  • 39
    • 84905111224 scopus 로고    scopus 로고
    • The Dow Chemical Company [accessed 15.03.14]
    • The Dow Chemical Company. Refractive index of glycerine-water solutions. Available at: http://www.dow.com/optim/optim-advantage/physical-properties/ refractive.htm [accessed 15.03.14].
    • Refractive Index of Glycerine-water Solutions
  • 42
    • 0000899341 scopus 로고
    • Solvatochromism and prototropism in 2-(aminophenyl) benzothiazoles
    • J.K. Dey, and S.K. Dogra Solvatochromism and prototropism in 2-(aminophenyl) benzothiazoles Bull Chem Soc Jpn 64 10 1991 3142 3152
    • (1991) Bull Chem Soc Jpn , vol.64 , Issue.10 , pp. 3142-3152
    • Dey, J.K.1    Dogra, S.K.2
  • 43
    • 34047236476 scopus 로고    scopus 로고
    • Excited-state intramolecular proton transfer in 2-(3′-Hydroxy- 2′-pyridyl)benzoxazole. Evidence of coupled proton and charge transfer in the excited state of some o-hydroxyarylbenzazoles
    • DOI 10.1021/jp0653813
    • S. Rios Vazquez, M.C. Rios Rodriguez, M. Mosquera, and F. Rodriguez-Prieto Excited-state intramolecular proton transfer in 2-(3'-hydroxy-2'-pyridyl)benzoxazole. Evidence of coupled proton and charge transfer in the excited state of some o-hydroxyarylbenzazoles J Phys Chem B 111 10 2007 1814 1826 (Pubitemid 46543236)
    • (2007) Journal of Physical Chemistry A , vol.111 , Issue.10 , pp. 1814-1826
    • Vazquez, S.R.1    Rios Rodriguez, M.C.2    Mosquera, M.3    Rodriguez-Prieto, F.4
  • 44
    • 84872696585 scopus 로고    scopus 로고
    • Excited-state proton coupled charge transfer modulated by molecular structure and media polarization
    • A.P. Demchenko, K. Tang, and P. Chou Excited-state proton coupled charge transfer modulated by molecular structure and media polarization Chem Soc Rev 42 3 2013 1379 1408
    • (2013) Chem Soc Rev , vol.42 , Issue.3 , pp. 1379-1408
    • Demchenko, A.P.1    Tang, K.2    Chou, P.3
  • 45
    • 33646349196 scopus 로고    scopus 로고
    • Methods for enhancing the accuracy and reproducibility of Congo red and thioflavin T assays
    • DOI 10.1016/j.ab.2006.03.015, PII S0003269706001801
    • R. Eisert, L. Felau, and L.R. Brown Methods for enhancing the accuracy and reproducibility of Congo red and Thioflavin T assays Anal Biochem 353 2006 144 146 (Pubitemid 43668937)
    • (2006) Analytical Biochemistry , vol.353 , Issue.1 , pp. 144-146
    • Eisert, R.1    Felau, L.2    Brown, L.R.3
  • 46
    • 80053401483 scopus 로고    scopus 로고
    • Interaction of Thioflavin T with amyloid fibrils: Stoichiometry and affinity of dye binding, absorption spectra of bound dye
    • A.I. Sulatskaya, I.M. Kuznetsova, and K.K. Turoverov Interaction of Thioflavin T with amyloid fibrils: stoichiometry and affinity of dye binding, absorption spectra of bound dye J Phys Chem B 115 39 2011 11519 11524
    • (2011) J Phys Chem B , vol.115 , Issue.39 , pp. 11519-11524
    • Sulatskaya, A.I.1    Kuznetsova, I.M.2    Turoverov, K.K.3
  • 47
    • 84857510553 scopus 로고    scopus 로고
    • Analyzing Thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique
    • I.M. Kuznetsova, A.I. Sulatskaya, V.N. Uversky, and K.K. Turoverov Analyzing Thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique PLoS One 7 2 2012 e30724
    • (2012) PLoS One , vol.7 , Issue.2 , pp. 30724
    • Kuznetsova, I.M.1    Sulatskaya, A.I.2    Uversky, V.N.3    Turoverov, K.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.