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Volumn 10, Issue 1, 2014, Pages 31-39

Scanning electron microscope imaging of amyloid fibrils

Author keywords

Amyloid fibrils; Lysozyme; Scanning electron microscopy

Indexed keywords

ATOMIC FORCE MICROSCOPY; ENZYMES; SCANNING ELECTRON MICROSCOPY; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84896462242     PISSN: 15533468     EISSN: None     Source Type: Journal    
DOI: 10.3844/ajbbsp.2014.31.39     Document Type: Article
Times cited : (22)

References (34)
  • 1
    • 77955230701 scopus 로고    scopus 로고
    • Understanding am-yloid aggregation by statistical analysis of atomic force microscopy images
    • DOI: 10.1038/nnano.2010.59
    • Adamcik, J., J.M. Jung, J. Flakowski, P.D.L. Rios and G. Dietler et al., 2010. Understanding am-yloid aggregation by statistical analysis of atomic force microscopy images. Nature Nanotechnol., 5: 423-428. DOI: 10.1038/nnano.2010.59
    • (2010) Nature Nanotechnol. , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.M.2    Flakowski, J.3    Rios, P.D.L.4    Dietler, G.5
  • 2
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • DOI: 10.1016/j.jmb.2006.02.007
    • Anderson, M., O.V. Bocharova, N. Makarava, L. Breydo and V.V. Salnikov et al., 2006. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy. J. Mol. Biol., 358: 580-596. DOI: 10.1016/j.jmb.2006.02.007
    • (2006) J. Mol. Biol. , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5
  • 3
    • 23444450012 scopus 로고    scopus 로고
    • Fine structure study of Abeta1-42 fibrillogenesis with atomic force microscopy
    • DOI: 10.1096/fj.04-3137fje
    • Arimon, M., I. Diez-Perez, M.J. Kogan, N. Durany and E. Giralt et al., 2005. Fine structure study of Abeta1-42 fibrillogenesis with atomic force microscopy. FASEB J., 19: 1344-1346. DOI: 10.1096/fj.04-3137fje
    • (2005) FASEB J. , vol.19 , pp. 1344-1346
    • Arimon, M.1    Diez-Perez, I.2    Kogan, M.J.3    Durany, N.4    Giralt, E.5
  • 4
    • 33749836310 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth, propagation and adaptation
    • DOI: 10.1021/ar050074l
    • Ban, T., K. Yamaguchi and Y. Goto, 2006. Direct observation of amyloid fibril growth, propagation and adaptation. Acc. Chem. Res., 39: 663-670. DOI: 10.1021/ar050074l
    • (2006) Acc. Chem. Res. , vol.39 , pp. 663-670
    • Ban, T.1    Yamaguchi, K.2    Goto, Y.3
  • 5
    • 72049130847 scopus 로고    scopus 로고
    • Reduction and degradation of amyloid aggregates by a pulsed radio-frequency cold atmospheric plasma jet
    • DOI:10.1088/1367-2630/11/11/115024
    • Bayliss, D.L., J.L. Walsh, G. Shama, F. Iza and M.G. Kong, 2009 Reduction and degradation of amyloid aggregates by a pulsed radio-frequency cold atmospheric plasma jet. New J. Phys., 11: 115024. DOI:10.1088/1367-2630/11/11/115024
    • (2009) New J. Phys. , vol.11 , pp. 115024
    • Bayliss, D.L.1    Walsh, J.L.2    Shama, G.3    Iza, F.4    Kong, M.G.5
  • 6
    • 0033637078 scopus 로고    scopus 로고
    • Ultrastructural organization of amyloid fibrils by atomic force microscopy
    • DOI: 10.1016/S0006-3495(00)76560-X
    • Chamberlain, A.K., C.E. MacPhee, J. Zurdo, L.A. Morozova-Roche and H.A. Hill et al., 2000. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys. J., 79: 3282-3293. DOI: 10.1016/S0006-3495(00)76560-X
    • (2000) Biophys. J. , vol.79 , pp. 3282-3293
    • Chamberlain, A.K.1    McPhee, C.E.2    Zurdo, J.3    Morozova-Roche, L.A.4    Hill, H.A.5
  • 7
    • 0036783381 scopus 로고    scopus 로고
    • Variability in the pKa of histidine side-chains correlates with burial within proteins
    • DOI: 10.1002/prot.10177
    • Edgcomb, S.P. and K.P. Murphy, 2002. Variability in the pKa of histidine side-chains correlates with burial within proteins. Proteins-Structure Funct. Genet., 49: 1-6. DOI: 10.1002/prot.10177
    • (2002) Proteins-Structure Funct. Genet. , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 8
    • 47349117210 scopus 로고    scopus 로고
    • Effect of an amyloidogenic sequence attached to yellow fluorescent protein
    • DOI: 10.1002/prot.21971
    • Hamada, D., K. Tsumoto, M. Sawara, N. Tanaka and K. Nakahira et al., 2008. Effect of an amyloidogenic sequence attached to yellow fluorescent protein. Proteins-Structure Funct. Bioinformat., 72: 811-821. DOI: 10.1002/prot.21971
    • (2008) Proteins-Structure Funct. Bioinformat. , vol.72 , pp. 811-821
    • Hamada, D.1    Tsumoto, K.2    Sawara, M.3    Tanaka, N.4    Nakahira, K.5
  • 9
    • 78650380856 scopus 로고    scopus 로고
    • One-dimensional protein-based nanopar-ticles induce lipid bilayer disruption: Carbon nanotube conjugates and amyloid fibrils
    • DOI: 10.1021/la103615b
    • Hirano, A., K. Uda, Y. Maeda, T. Akasaka and K. Shiraki, 2010. One-dimensional protein-based nanopar-ticles induce lipid bilayer disruption: Carbon nanotube conjugates and amyloid fibrils. Langmuir, 26: 17256-17259. DOI: 10.1021/la103615b
    • (2010) Langmuir , vol.26 , pp. 17256-17259
    • Hirano, A.1    Uda, K.2    Maeda, Y.3    Akasaka, T.4    Shiraki, K.5
  • 10
    • 0036196674 scopus 로고    scopus 로고
    • Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy
    • DOI: 10.1021/bm0156429
    • Ikeda, S. and V.J. Morris, 2002. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules, 3: 382-389. DOI: 10.1021/bm0156429
    • (2002) Biomacromolecules , vol.3 , pp. 382-389
    • Ikeda, S.1    Morris, V.J.2
  • 11
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • DOI: 10.1093/emboj/18.4.815
    • Jimenez, J.L., J.L. Guijarro, E. Orlova, J. Zurdo and C.M. Dobson et al., 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J., 18: 815-821. DOI: 10.1093/emboj/18.4.815
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.L.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5
  • 12
    • 0035839046 scopus 로고    scopus 로고
    • Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy
    • DOI: 10.1006/jmbi.2001.4863
    • Jimenez, J.L., G. Tennent, M. Pepys and H.R. Saibil, 2001. Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J. Mol. Biol., 311: 241-247. DOI: 10.1006/jmbi.2001.4863
    • (2001) J. Mol. Biol. , vol.311 , pp. 241-247
    • Jimenez, J.L.1    Tennent, G.2    Pepys, M.3    Saibil, H.R.4
  • 13
    • 17144399857 scopus 로고    scopus 로고
    • High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry
    • DOI: 10.1002/elps.200410187
    • Jin, Y. and T. Manabe, 2005. High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis, 26: 1019-1028. DOI: 10.1002/elps.200410187
    • (2005) Electrophoresis , vol.26 , pp. 1019-1028
    • Jin, Y.1    Manabe, T.2
  • 14
    • 77958066419 scopus 로고    scopus 로고
    • Destruction of α-synuclein based amyloid fibrils by a low temperature plasma jet
    • DOI:10.1063/1.3499277
    • Karakas, E., A. Munyanyi, L. Greene and M. Laroussi, 2010 Destruction of α-synuclein based amyloid fibrils by a low temperature plasma jet. Appl. Phys. Lett., 97:143702. DOI:10.1063/1.3499277
    • (2010) Appl. Phys. Lett. , vol.97 , pp. 143702
    • Karakas, E.1    Munyanyi, A.2    Greene, L.3    Laroussi, M.4
  • 15
    • 11244309572 scopus 로고    scopus 로고
    • Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry
    • DOI: 10.1074/jbc.M409677200
    • Kardos, J., K. Yamamoto, K. Hasegawa, H. Naiki and Y. Goto, 2004. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J. Biol. Chem., 279: 55308-55314. DOI: 10.1074/jbc.M409677200
    • (2004) J. Biol. Chem. , vol.279 , pp. 55308-55314
    • Kardos, J.1    Yamamoto, K.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 16
    • 0041343061 scopus 로고    scopus 로고
    • A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy
    • DOI: 10.1016/S0006-3495(03)74550-0
    • Khurana, R., C. Ionescu-Zanetti, M. Pope, J. Li and L. Nielson et al., 2003. A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophys. J., 85: 1135-1144. DOI: 10.1016/S0006-3495(03)74550-0
    • (2003) Biophys. J. , vol.85 , pp. 1135-1144
    • Khurana, R.1    Ionescu-Zanetti, C.2    Pope, M.3    Li, J.4    Nielson, L.5
  • 17
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • DOI: 10.1038/nnano.2011.102
    • Knowles, T.P.J. and M.J. Buehler, 2011. Nanomechanics of functional and pathological amyloid materials. Nature Nanotechnol., 6: 469-479. DOI: 10.1038/nnano.2011.102
    • (2011) Nature Nanotechnol. , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 18
    • 79955863547 scopus 로고    scopus 로고
    • General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons
    • DOI: 10.1021/bm200216u
    • Lara, C., J. Adamcik, S. Jordens and R. Mezzenga, 2011. General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons. Biomacromolecules, 12: 1868-1875. DOI: 10.1021/bm200216u
    • (2011) Biomacromolecules , vol.12 , pp. 1868-1875
    • Lara, C.1    Adamcik, J.2    Jordens, S.3    Mezzenga, R.4
  • 19
    • 22844440807 scopus 로고    scopus 로고
    • Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis
    • DOI: 10.1385/1-59259-874-9:081
    • Lashuel, H.A. and J.S. Wall, 2005. Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis. Methods Mol Biol., 299: 81-101. DOI: 10.1385/1-59259-874-9:081
    • Methods Mol Biol. , vol.299 , pp. 81-101
    • Lashuel, H.A.1    Wall, J.S.2
  • 20
    • 82555175362 scopus 로고    scopus 로고
    • Co-assembly of human islet Amyloid Poly-Peptide (hIAPP)/insulin
    • DOI: 10.1039/c1cc14285b
    • Liu, P., S. Zhang, M.S. Chen, Q. Liu and C.X. Wang et al., 2012. Co-assembly of human islet Amyloid Poly-Peptide (hIAPP)/insulin. Chem. Commun., 48: 191-193. DOI: 10.1039/c1cc14285b
    • (2012) Chem. Commun. , vol.48 , pp. 191-193
    • Liu, P.1    Zhang, S.2    Chen, M.S.3    Liu, Q.4    Wang, C.X.5
  • 21
    • 68149165906 scopus 로고    scopus 로고
    • Plasmon resonance-based photoelectrochemical tailoring of spectrum, morphology and orientation of Ag nanoparticles on TiO2 single crystals
    • DOI: 10.1039/B906795G
    • Matsubara, K., K.L. Kelly, N. Sakai and T. Tatsuma, 2009. Plasmon resonance-based photoelectrochemical tailoring of spectrum, morphology and orientation of Ag nanoparticles on TiO2 single crystals. J. Mater. Chem., 19: 5526-5532. DOI: 10.1039/B906795G
    • (2009) J. Mater. Chem. , vol.19 , pp. 5526-5532
    • Matsubara, K.1    Kelly, K.L.2    Sakai, N.3    Tatsuma, T.4
  • 22
    • 77949781943 scopus 로고    scopus 로고
    • The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry
    • DOI: 10.1021/jp9102993
    • Morel, B., L. Varela and F. Conejero-Lara, 2010. The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry. J. Phys. Chem. B, 114: 4010-4019. DOI: 10.1021/jp9102993
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4010-4019
    • Morel, B.1    Varela, L.2    Conejero-Lara, F.3
  • 23
    • 36749011905 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action
    • DOI: 10.1111/j.1742-4658.2007.06158.x
    • Morshedi, D., N. Rezaei-Ghaleh, A. Ebrahim-Habibi, S. Ahmadian and M. Nemat-Gorgani, 2007. Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action. FEBS J., 274: 6415-6425. DOI: 10.1111/j.1742-4658.2007.06158.x
    • (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
  • 24
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • DOI: 10.1016/j.ymeth.2004.03.012
    • Nilsson, M.R., 2004. Techniques to study amyloid fibril formation in vitro. Methods, 34: 151-160. DOI: 10.1016/j.ymeth.2004.03.012
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 25
    • 79953210716 scopus 로고    scopus 로고
    • Destruction of amyloid fibrils of keratoepithelin peptides by laser irradiation coupled with amyloid-specific thioflavin T
    • DOI: 10.1074/jbc.M111.222901
    • Ozawa, D., Y. Kaji, H. Yagi, K. Sakurai and T. Kawakami et al., 2011. Destruction of amyloid fibrils of keratoepithelin peptides by laser irradiation coupled with amyloid-specific thioflavin T. J. Biol. Chem., 286: 10856-10863. DOI: 10.1074/jbc.M111.222901
    • (2011) J. Biol. Chem. , vol.286 , pp. 10856-10863
    • Ozawa, D.1    Kaji, Y.2    Yagi, H.3    Sakurai, K.4    Kawakami, T.5
  • 26
    • 59449106971 scopus 로고    scopus 로고
    • Destruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation
    • DOI: 10.1074/jbc.M805118200
    • Ozawa, D., H. Yagi, T. Ban, A. Kameda and T. Kawakami et al., 2009. Destruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation. J. Biol. Chem., 284: 1009-1017. DOI: 10.1074/jbc.M805118200
    • (2009) J. Biol. Chem. , vol.284 , pp. 1009-1017
    • Ozawa, D.1    Yagi, H.2    Ban, T.3    Kameda, A.4    Kawakami, T.5
  • 27
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • DOI: 10.1126/science.1082387
    • Reches, M. and E. Gazit, 2003. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science, 300: 625-627. DOI: 10.1126/science.1082387
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 28
    • 4344678675 scopus 로고    scopus 로고
    • Ultra-structural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study
    • DOI: 10.1016/j.bbadis.2004.04.007
    • Relini, A., R. Rolandi, M. Bolognesi, M. Aboudan and G. Merlini et al., 2004. Ultra-structural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study. Biochim. Biophys. Acta, 1690: 33-41. DOI: 10.1016/j.bbadis.2004.04.007
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 33-41
    • Relini, A.1    Rolandi, R.2    Bolognesi, M.3    Aboudan, M.4    Merlini, G.5
  • 29
    • 79551690202 scopus 로고    scopus 로고
    • Application of two morphologically different fibrillar and filamentous insulin amyloids as a biomaterial for cell culture surfaces
    • DOI: 10.1016/j.reactfunctpolym.2010.10.012
    • Sakono, M., S. Akiyama, T. Zako, S. Sakaki and T. Waku et al., 2011. Application of two morphologically different fibrillar and filamentous insulin amyloids as a biomaterial for cell culture surfaces. React. Funct. Polym., 71: 324-328. DOI: 10.1016/j.reactfunctpolym.2010.10.012
    • (2011) React. Funct. Polym. , vol.71 , pp. 324-328
    • Sakono, M.1    Akiyama, S.2    Zako, T.3    Sakaki, S.4    Waku, T.5
  • 30
    • 34548389339 scopus 로고    scopus 로고
    • Heat-induced conversion of beta(2)-Microglobulin and hen egg-white lysozyme into amyloid fibrils
    • DOI: 10.1016/j.jmb.2007.06.088
    • Sasahara, K., H. Yagi, H. Naiki and Y. Goto, 2007. Heat-induced conversion of beta(2)-Microglobulin and hen egg-white lysozyme into amyloid fibrils. J. Mol. Biol., 372: 981-991. DOI: 10.1016/j.jmb.2007.06.088
    • (2007) J. Mol. Biol. , vol.372 , pp. 981-991
    • Sasahara, K.1    Yagi, H.2    Naiki, H.3    Goto, Y.4
  • 31
    • 84893124456 scopus 로고    scopus 로고
    • De-generation of amyloid-ß fibrils caused by exposure to low-temperature atmospheric-pressure plasma in aqueous solution, Appl
    • DOI: 10.1063/1.4861842
    • Takai, E., G. Ohashi, T. Yoshida, K.M. Sorgjerd and T. Zako et al., 2014a. De-generation of amyloid-ß fibrils caused by exposure to low-temperature atmospheric-pressure plasma in aqueous solution, Appl. Phys. Lett., 104: 023701. DOI: 10.1063/1.4861842
    • (2014) Phys. Lett. , vol.104 , pp. 023701
    • Takai, E.1    Ohashi, G.2    Yoshida, T.3    Sorgjerd, K.M.4    Zako, T.5
  • 33
    • 84893437764 scopus 로고    scopus 로고
    • Cysteine inhibits the fibrillisation and cytotoxicity of amyloid-β 40 and 42: Implications for the contribution of the thiophilic interaction, Phys
    • DOI: 10.1039/C3CP54245A
    • Takai E., K. Uda, T. Yoshida, T. Zako and M. Maeda et al., 2014c. Cysteine inhibits the fibrillisation and cytotoxicity of amyloid-β 40 and 42: Implications for the contribution of the thiophilic interaction, Phys. Chem. Chem. Phys., 16: 3566-3572. DOI: 10.1039/C3CP54245A
    • (2014) Chem. Chem. Phys. , vol.16 , pp. 3566-3572
    • Takai, E.1    Uda, K.2    Yoshida, T.3    Zako, T.4    Maeda, M.5
  • 34
    • 77953495098 scopus 로고    scopus 로고
    • Laser-induced propagation and destruction of amyloid beta fibrils
    • DOI: 10.1074/jbc.M109.076505
    • Yagi, H., D. Ozawa, K. Sakurai, T. Kawakami and H. Kuyama et al., 2010. Laser-induced propagation and destruction of amyloid beta fibrils. J. Biol. Chem., 285: 19660-19667. DOI: 10.1074/jbc.M109.076505
    • (2010) J. Biol. Chem. , vol.285 , pp. 19660-19667
    • Yagi, H.1    Ozawa, D.2    Sakurai, K.3    Kawakami, T.4    Kuyama, H.5


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