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Volumn 408, Issue 1, 2011, Pages 115-119

Interactions between a luminescent conjugated polyelectrolyte and amyloid fibrils investigated with flow linear dichroism spectroscopy

Author keywords

Amyloid fibrils; Conjugated polyelectrolytes; Flow LD; Fluorescent probes

Indexed keywords

AMYLOID; BIOPOLYMER; LUMINESCENT AGENT; POLYELECTROLYTE; THIOFLAVINE;

EID: 79955455539     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.132     Document Type: Article
Times cited : (17)

References (27)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 31144460030 scopus 로고    scopus 로고
    • Functional amyloid formation within mammalian tissue
    • Fowler D.M., Koulov A.V., Alory-Jost C., et al. Functional amyloid formation within mammalian tissue. PLoS Biol. 2006, 4:e6.
    • (2006) PLoS Biol. , vol.4
    • Fowler, D.M.1    Koulov, A.V.2    Alory-Jost, C.3
  • 4
    • 77949380640 scopus 로고    scopus 로고
    • Biomolecular nanowires decorated by organic electronic polymers
    • Björk P., Herland A., Hamedi M., Inganäs O. Biomolecular nanowires decorated by organic electronic polymers. J. Mater. Chem. 2010, 20:2269.
    • (2010) J. Mater. Chem. , vol.20 , pp. 2269
    • Björk, P.1    Herland, A.2    Hamedi, M.3    Inganäs, O.4
  • 5
    • 77949261467 scopus 로고    scopus 로고
    • Nanostructured films from hierarchical self-assembly of amyloidogenic proteins
    • Knowles T.P.J., Oppenheim T.W., Buell A.K., et al. Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. Nat. Nanotechnol. 2010, 5:204-207.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 204-207
    • Knowles, T.P.J.1    Oppenheim, T.W.2    Buell, A.K.3
  • 6
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: localisation and implications
    • Krebs M.R.H., Bromley E.H.C., Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 2005, 149:30-37.
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 7
    • 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., Finch J.T. Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J Mol Biol. 1992, 227:1205-1223.
    • (1992) J Mol Biol. , vol.227 , pp. 1205-1223
    • Turnell, W.G.1    Finch, J.T.2
  • 8
    • 34548639390 scopus 로고    scopus 로고
    • Conjugated polymers as optical probes for protein interactions and protein conformations
    • Herland A., Inganäs O. Conjugated polymers as optical probes for protein interactions and protein conformations. Macromol. Rapid Commun. 2007, 28:1703-1713.
    • (2007) Macromol. Rapid Commun. , vol.28 , pp. 1703-1713
    • Herland, A.1    Inganäs, O.2
  • 9
    • 69249100953 scopus 로고    scopus 로고
    • Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses
    • Åslund A., Sigurdson C.J., Klingstedt T., et al. Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. ACS Chem. Biol. 2009, 4:673-684.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 673-684
    • Åslund, A.1    Sigurdson, C.J.2    Klingstedt, T.3
  • 10
    • 34248332079 scopus 로고    scopus 로고
    • Chemical sensors based on amplifying fluorescent conjugated polymers
    • Thomas S.W., Joly G.D., Swager T.M. Chemical sensors based on amplifying fluorescent conjugated polymers. Chem. Rev. 2007, 107:1339-1386.
    • (2007) Chem. Rev. , vol.107 , pp. 1339-1386
    • Thomas, S.W.1    Joly, G.D.2    Swager, T.M.3
  • 11
    • 77956498665 scopus 로고    scopus 로고
    • Supramolecular assembly of designed alpha-helical polypeptide-based nanostructures and luminescent conjugated polyelectrolytes
    • Wigenius J., Björk P., Hamedi M., Aili D. Supramolecular assembly of designed alpha-helical polypeptide-based nanostructures and luminescent conjugated polyelectrolytes. Macromol. Biosci. 2010, 836-841.
    • (2010) Macromol. Biosci. , pp. 836-841
    • Wigenius, J.1    Björk, P.2    Hamedi, M.3    Aili, D.4
  • 12
    • 0042754735 scopus 로고    scopus 로고
    • Functionalized regioregular polythiophenes: towards the development of biochromic sensors
    • Faid K., Leclerc M. Functionalized regioregular polythiophenes: towards the development of biochromic sensors. Chem. Commun. 1996, 4:2761-2762.
    • (1996) Chem. Commun. , vol.4 , pp. 2761-2762
    • Faid, K.1    Leclerc, M.2
  • 13
    • 14844356353 scopus 로고    scopus 로고
    • Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation
    • Nilsson K.P.R., Herland A., Hammarström P., Inganäs O. Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation. Biochemistry 2005, 44:3718-3724.
    • (2005) Biochemistry , vol.44 , pp. 3718-3724
    • Nilsson, K.P.R.1    Herland, A.2    Hammarström, P.3    Inganäs, O.4
  • 14
    • 35348907339 scopus 로고    scopus 로고
    • Imaging distinct conformational states of amyloid fibrils in alzheimer's disease using novel luminescent probes
    • Nilsson K.P.R., Åslund A., Berg I., et al. Imaging distinct conformational states of amyloid fibrils in alzheimer's disease using novel luminescent probes. ACS Chem. Biol. 2007, 2:553-560.
    • (2007) ACS Chem. Biol. , vol.2 , pp. 553-560
    • Nilsson, K.P.R.1    Åslund, A.2    Berg, I.3
  • 15
    • 76149083590 scopus 로고    scopus 로고
    • Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy
    • Nilsson K.P.R., Ikenberg K., Aslund A. Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy. Am J Pathol. 2010, 176:563-574.
    • (2010) Am J Pathol. , vol.176 , pp. 563-574
    • Nilsson, K.P.R.1    Ikenberg, K.2    Aslund, A.3
  • 18
    • 70349467633 scopus 로고    scopus 로고
    • Flow linear dichroism of some prototypical proteins
    • Bulheller B.M., Rodger A., Hicks M.R., et al. Flow linear dichroism of some prototypical proteins. J. Am. Chem. Soc. 2009, 131:13305-13314.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13305-13314
    • Bulheller, B.M.1    Rodger, A.2    Hicks, M.R.3
  • 19
    • 0037191109 scopus 로고    scopus 로고
    • Conformational transitions of a free amino-acid-functionalized polythiophene induced by different buffer systems
    • Nilsson K.P.R., Andersson M.R., Inganas O. Conformational transitions of a free amino-acid-functionalized polythiophene induced by different buffer systems. J. Phys. Condens. Matter. 2002, 14:10011-10020.
    • (2002) J. Phys. Condens. Matter. , vol.14 , pp. 10011-10020
    • Nilsson, K.P.R.1    Andersson, M.R.2    Inganas, O.3
  • 20
    • 0033873993 scopus 로고    scopus 로고
    • Photovoltaic cells with a conjugated polyelectrolyte
    • Ding L., Jonforsen M., Roman L.S., et al. Photovoltaic cells with a conjugated polyelectrolyte. Synth. Met. 2000, 110:133-140.
    • (2000) Synth. Met. , vol.110 , pp. 133-140
    • Ding, L.1    Jonforsen, M.2    Roman, L.S.3
  • 21
    • 78650655986 scopus 로고    scopus 로고
    • Linear Dichroism and Circular Dichroism
    • A Textbook on Polarized-Light Spectroscopy, Royal Society of Chemistry
    • B. Nordén, A. Rodger, T.R. Dafforn, Linear Dichroism and Circular Dichroism: A Textbook on Polarized-Light Spectroscopy, Royal Society of Chemistry, 2010.
    • (2010)
    • Nordén, B.1    Rodger, A.2    Dafforn, T.R.3
  • 22
    • 33847027742 scopus 로고    scopus 로고
    • Alignment of a conjugated polymer onto amyloid-like protein fibrils
    • Herland A., Björk P., Hania P.R., et al. Alignment of a conjugated polymer onto amyloid-like protein fibrils. Small 2007, 3:318-325.
    • (2007) Small , vol.3 , pp. 318-325
    • Herland, A.1    Björk, P.2    Hania, P.R.3
  • 24
    • 0015134051 scopus 로고
    • Isoelectric focusing in acrylamide gels - use of amphoteric dyes as internal markers for determination of isoelectric points
    • Conway-Jacobs A., Lewin L.M. Isoelectric focusing in acrylamide gels - use of amphoteric dyes as internal markers for determination of isoelectric points. Anal. Biochem. 1971, 43:394-400.
    • (1971) Anal. Biochem. , vol.43 , pp. 394-400
    • Conway-Jacobs, A.1    Lewin, L.M.2
  • 26
    • 0031592945 scopus 로고    scopus 로고
    • Core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde M., Serpell L.C., Bartlam Common M., et al. Core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol. 1997, 273:729-739.
    • (1997) J Mol Biol. , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam Common, M.3
  • 27
    • 0020991935 scopus 로고
    • Structural properties of Protein β-Sheets
    • Salemme F. Structural properties of Protein β-Sheets. Prog Biophys Mol Biol. 1983, 42:95-133.
    • (1983) Prog Biophys Mol Biol. , vol.42 , pp. 95-133
    • Salemme, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.