메뉴 건너뛰기




Volumn 6, Issue 8, 2015, Pages 1436-1444

Fluorescent Filter-Trap Assay for Amyloid Fibril Formation Kinetics in Complex Solutions

Author keywords

aggregation; Alzheimers disease; Amyloid; filter trap; kinetics; site specific fluorophore labeling

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; FLUORESCENT DYE; HUMAN SERUM ALBUMIN; NANOPARTICLE; POLYSTYRENE; THIOFLAVINE; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; POLYSTYRENE DERIVATIVE; SERUM ALBUMIN; SOLUTION AND SOLUBILITY; THIAZOLE DERIVATIVE;

EID: 84939782105     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/acschemneuro.5b00104     Document Type: Article
Times cited : (21)

References (51)
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 333-366
    • (2006) Annu. Rev. Biochem. , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 78650462753 scopus 로고    scopus 로고
    • Alzheimers disease: A general introduction and pathomechanism
    • Finder, V. H. (2010) Alzheimers disease: A general introduction and pathomechanism J. Alzheimers Dis. 22, S5-S19
    • (2010) J. Alzheimers Dis. , vol.22 , pp. 5-S19
    • Finder, V.H.1
  • 6
    • 0026597063 scopus 로고
    • Alzheimers disease - The amyloid cascade hypothesis
    • Hardy, J. A. and Higgins, G. A. (1992) Alzheimers disease-the amyloid cascade hypothesis Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 7
    • 34249098080 scopus 로고    scopus 로고
    • Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding
    • Bateman, D. A., McLaurin, J., and Chakrabartty, A. (2007) Requirement of aggregation propensity of alzheimer amyloid peptides for neuronal cell surface binding, BMC Neurosci. 8.
    • (2007) BMC Neurosci. , vol.8
    • Bateman, D.A.1    McLaurin, J.2    Chakrabartty, A.3
  • 8
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • Cohen, S. I. A., Vendruscolo, M., Dobson, C. M., and Knowles, T. P. J. (2012) From macroscopic measurements to microscopic mechanisms of protein aggregation J. Mol. Biol. 421, 160-171
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 9
    • 84898954138 scopus 로고    scopus 로고
    • Charge dependent retardation of amyloid beta aggregation by hydrophilic proteins
    • Assarsson, A., Hellstrand, E., Cabaleiro-Lago, C., and Linse, S. (2014) Charge dependent retardation of amyloid beta aggregation by hydrophilic proteins ACS Chem. Neurosci. 5, 266-274
    • (2014) ACS Chem. Neurosci. , vol.5 , pp. 266-274
    • Assarsson, A.1    Hellstrand, E.2    Cabaleiro-Lago, C.3    Linse, S.4
  • 10
    • 84904966131 scopus 로고    scopus 로고
    • Effects of polyamino acids and polyelectrolytes on amyloid beta fibril formation
    • Assarsson, A., Linse, S., and Cabaleiro-Lago, C. (2014) Effects of polyamino acids and polyelectrolytes on amyloid beta fibril formation Langmuir 30, 8812-8818
    • (2014) Langmuir , vol.30 , pp. 8812-8818
    • Assarsson, A.1    Linse, S.2    Cabaleiro-Lago, C.3
  • 11
    • 77749320957 scopus 로고    scopus 로고
    • Inhibition of iapp and iapp((20-29)) fibrillation by polymeric nanoparticles
    • Cabaleiro-Lago, C., Lynch, I., Dawson, K. A., and Linse, S. (2010) Inhibition of iapp and iapp((20-29)) fibrillation by polymeric nanoparticles Langmuir 26, 3453-3461
    • (2010) Langmuir , vol.26 , pp. 3453-3461
    • Cabaleiro-Lago, C.1    Lynch, I.2    Dawson, K.A.3    Linse, S.4
  • 13
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • Hard, T. and Lendel, C. (2012) Inhibition of amyloid formation J. Mol. Biol. 421, 441-465
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Hard, T.1    Lendel, C.2
  • 14
    • 35648975464 scopus 로고    scopus 로고
    • The binding constant for amyloid a beta 40 peptide interaction with human serum albumin
    • Rozga, M., Kloniecki, M., Jablonowska, A., Dandlez, M., and Bal, W. (2007) The binding constant for amyloid a beta 40 peptide interaction with human serum albumin Biochem. Biophys. Res. Commun. 364, 714-718
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 714-718
    • Rozga, M.1    Kloniecki, M.2    Jablonowska, A.3    Dandlez, M.4    Bal, W.5
  • 16
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using n-methylated derivatives - A general strategy to prevent amyloid formation
    • Hughes, E., Burke, R. M., and Doig, A. J. (2000) Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using n-methylated derivatives-a general strategy to prevent amyloid formation J. Biol. Chem. 275, 25109-25115
    • (2000) J. Biol. Chem. , vol.275 , pp. 25109-25115
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 17
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin t
    • LeVine, H. (1999) Quantification of beta-sheet amyloid fibril structures with thioflavin t Methods Enzymol. 309, 274-284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 19
    • 77951676986 scopus 로고    scopus 로고
    • Amyloid beta-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process
    • Hellstrand, E., Boland, B., Walsh, D. M., and Linse, S. (2010) Amyloid beta-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process ACS Chem. Neurosci. 1, 13-18
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 13-18
    • Hellstrand, E.1    Boland, B.2    Walsh, D.M.3    Linse, S.4
  • 20
    • 84355162816 scopus 로고    scopus 로고
    • Interference of low-molecular substances with the thioflavin-t fluorescence assay of amyloid fibrils
    • Noormai, A., Primar, K., Tougu, V., and Palumaa, P. (2012) Interference of low-molecular substances with the thioflavin-t fluorescence assay of amyloid fibrils J. Pept. Sci. 18, 59-64
    • (2012) J. Pept. Sci. , vol.18 , pp. 59-64
    • Noormai, A.1    Primar, K.2    Tougu, V.3    Palumaa, P.4
  • 21
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid beta 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
  • 22
    • 84869811189 scopus 로고    scopus 로고
    • Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (a beta) self-assembly
    • Jameson, L. P., Smith, N. W., and Dzyuba, S. V. (2012) Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (a beta) self-assembly ACS Chem. Neurosci. 3, 807-819
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 807-819
    • Jameson, L.P.1    Smith, N.W.2    Dzyuba, S.V.3
  • 23
    • 0035839080 scopus 로고    scopus 로고
    • A sensitive filter retention assay for the detection of prpsc and the screening of anti-prion compounds
    • Winklhofer, K. F., Hartl, F. U., and Tatzelt, J. (2001) A sensitive filter retention assay for the detection of prpsc and the screening of anti-prion compounds FEBS Lett. 503, 41-45
    • (2001) FEBS Lett. , vol.503 , pp. 41-45
    • Winklhofer, K.F.1    Hartl, F.U.2    Tatzelt, J.3
  • 24
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates
    • Wanker, E. E., Scherzinger, E., Heiser, V., Sittler, A., Eickhoff, H., and Lehrach, H. (1999) Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates Methods Enzymol. 309, 375-386
    • (1999) Methods Enzymol. , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 25
    • 37549071037 scopus 로고    scopus 로고
    • Detection and quantification of tau aggregation using a membrane filter assay
    • Chang, E. and Kuret, J. (2008) Detection and quantification of tau aggregation using a membrane filter assay Anal. Biochem. 373, 330-336
    • (2008) Anal. Biochem. , vol.373 , pp. 330-336
    • Chang, E.1    Kuret, J.2
  • 26
    • 33747056003 scopus 로고    scopus 로고
    • A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for het-s
    • Boye-Harnasch, M. and Cullin, C. (2006) A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for het-s J. Biotechnol. 125, 222-230
    • (2006) J. Biotechnol. , vol.125 , pp. 222-230
    • Boye-Harnasch, M.1    Cullin, C.2
  • 27
    • 68949163262 scopus 로고    scopus 로고
    • Preparation of fluorescently-labeled amyloid-beta peptide assemblies: The effect of fluorophore conjugation on structure and function
    • Jungbauer, L. M., Yu, C., Laxton, K. J., and LaDu, M. J. (2009) Preparation of fluorescently-labeled amyloid-beta peptide assemblies: The effect of fluorophore conjugation on structure and function J. Mol. Recognit. 22, 403-413
    • (2009) J. Mol. Recognit. , vol.22 , pp. 403-413
    • Jungbauer, L.M.1    Yu, C.2    Laxton, K.J.3    LaDu, M.J.4
  • 30
    • 83655191659 scopus 로고    scopus 로고
    • Transmission electron microscopy characterization of fluorescently labelled amyloid beta 1-40 and alpha-synuclein aggregates
    • Anderson, V. L. and Webb, W. W. (2011) Transmission electron microscopy characterization of fluorescently labelled amyloid beta 1-40 and alpha-synuclein aggregates, BMC Biotechnol. 11.
    • (2011) BMC Biotechnol. , vol.11
    • Anderson, V.L.1    Webb, W.W.2
  • 32
    • 0026664548 scopus 로고
    • Atomic-structure and chemistry of human serum-albumin
    • He, X. M. and Carter, D. C. (1992) Atomic-structure and chemistry of human serum-albumin Nature 358, 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 35
    • 68849102984 scopus 로고    scopus 로고
    • Interactions of thioflavin t with serum albumins: Spectroscopic analyses
    • Sen, P., Fatima, S., Ahmad, B., and Khan, R. H. (2009) Interactions of thioflavin t with serum albumins: Spectroscopic analyses Spectrochim. Acta, Part A 74, 94-99
    • (2009) Spectrochim. Acta, Part A , vol.74 , pp. 94-99
    • Sen, P.1    Fatima, S.2    Ahmad, B.3    Khan, R.H.4
  • 36
    • 33751285404 scopus 로고    scopus 로고
    • Amyloid fibril formation and other aggregate species formed by human serum albumin association
    • Taboada, P., Barbosa, S., Castro, E., and Mosquera, V. (2006) Amyloid fibril formation and other aggregate species formed by human serum albumin association J. Phys. Chem. B 110, 20733-20736
    • (2006) J. Phys. Chem. B , vol.110 , pp. 20733-20736
    • Taboada, P.1    Barbosa, S.2    Castro, E.3    Mosquera, V.4
  • 37
    • 72249108028 scopus 로고    scopus 로고
    • Human serum albumin inhibits a beta fibrillization through a "monomer-competitor" mechanism
    • Milojevic, J., Raditsis, A., and Melacini, G. (2009) Human serum albumin inhibits a beta fibrillization through a "monomer-competitor" mechanism Biophys. J. 97, 2585-2594
    • (2009) Biophys. J. , vol.97 , pp. 2585-2594
    • Milojevic, J.1    Raditsis, A.2    Melacini, G.3
  • 38
    • 78651245383 scopus 로고    scopus 로고
    • Stoichiometry and affinity of the human serum albumin-alzheimers a beta peptide interactions
    • Milojevic, J. and Melacini, G. (2011) Stoichiometry and affinity of the human serum albumin-alzheimers a beta peptide interactions Biophys. J. 100, 183-192
    • (2011) Biophys. J. , vol.100 , pp. 183-192
    • Milojevic, J.1    Melacini, G.2
  • 39
    • 34247204257 scopus 로고    scopus 로고
    • Understanding the molecular basis for the inhibition of the alzheimers a beta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation nmr spectroscopy
    • Milojevic, J., Esposito, V., Das, R., and Melacini, G. (2007) Understanding the molecular basis for the inhibition of the alzheimers a beta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation nmr spectroscopy J. Am. Chem. Soc. 129, 4282-4290
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4282-4290
    • Milojevic, J.1    Esposito, V.2    Das, R.3    Melacini, G.4
  • 40
    • 84865007775 scopus 로고    scopus 로고
    • Human serum albumin can regulate amyloid-beta peptide fiber growth in the brain interstitium implications for Alzheimer disease
    • Stanyon, H. F. and Viles, J. H. (2012) Human serum albumin can regulate amyloid-beta peptide fiber growth in the brain interstitium implications for alzheimer disease J. Biol. Chem. 287, 28163-28168
    • (2012) J. Biol. Chem. , vol.287 , pp. 28163-28168
    • Stanyon, H.F.1    Viles, J.H.2
  • 42
    • 48849114891 scopus 로고    scopus 로고
    • Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide
    • Rocha, S., Thueneman, A. F., Pereira, M. d. C., Coelho, M., Moehwald, H., and Brezesinski, G. (2008) Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide Biophys. Chem. 137, 35-42
    • (2008) Biophys. Chem. , vol.137 , pp. 35-42
    • Rocha, S.1    Thueneman, A.F.2    Pereira D. M, C.3    Coelho, M.4    Moehwald, H.5    Brezesinski, G.6
  • 45
    • 84870614632 scopus 로고    scopus 로고
    • Negatively charged gold nanoparticles inhibit alzheimers amyloid-beta fibrillization, induce fibril dissociation, and mitigate neurotoxicity
    • Liao, Y.-H., Chang, Y.-J., Yoshiike, Y., Chang, Y.-C., and Chen, Y.-R. (2012) Negatively charged gold nanoparticles inhibit alzheimers amyloid-beta fibrillization, induce fibril dissociation, and mitigate neurotoxicity Small 8, 3631-3639
    • (2012) Small , vol.8 , pp. 3631-3639
    • Liao, Y.-H.1    Chang, Y.-J.2    Yoshiike, Y.3    Chang, Y.-C.4    Chen, Y.-R.5
  • 46
    • 84906330021 scopus 로고    scopus 로고
    • Surface effects on aggregation kinetics of amyloidogenic peptides
    • Vacha, R., Linse, S., and Lund, M. (2014) Surface effects on aggregation kinetics of amyloidogenic peptides J. Am. Chem. Soc. 136, 11776-11782
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 11776-11782
    • Vacha, R.1    Linse, S.2    Lund, M.3
  • 47
    • 77951681963 scopus 로고    scopus 로고
    • Dual effect of amino modified polystyrene nanoparticles on amyloid beta protein fibrillation
    • Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Dawson, K. A., and Linse, S. (2010) Dual effect of amino modified polystyrene nanoparticles on amyloid beta protein fibrillation ACS Chem. Neurosci. 1, 279-287
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 279-287
    • Cabaleiro-Lago, C.1    Quinlan-Pluck, F.2    Lynch, I.3    Dawson, K.A.4    Linse, S.5
  • 49
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption-coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption-coefficient of a protein Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 50
    • 60349100306 scopus 로고    scopus 로고
    • A facile method for expression and purification of the alzheimers disease-associated amyloid beta-peptide
    • Walsh, D. M., Thulin, E., Minogue, A. M., Gustavsson, N., Pang, E., Teplow, D. B., and Linse, S. (2009) A facile method for expression and purification of the alzheimers disease-associated amyloid beta-peptide FEBS J. 276, 1266-1281
    • (2009) FEBS J. , vol.276 , pp. 1266-1281
    • Walsh, D.M.1    Thulin, E.2    Minogue, A.M.3    Gustavsson, N.4    Pang, E.5    Teplow, D.B.6    Linse, S.7
  • 51
    • 0036751701 scopus 로고    scopus 로고
    • Alexa and Oregon green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions
    • Rusinova, E., Tretyachenko-Ladokhina, V., Vele, O. E., Senear, D. F., and Ross, J. B. A. (2002) Alexa and oregon green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions Anal. Biochem. 308, 18-25
    • (2002) Anal. Biochem. , vol.308 , pp. 18-25
    • Rusinova, E.1    Tretyachenko-Ladokhina, V.2    Vele, O.E.3    Senear, D.F.4    Ross, J.B.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.