Visualization and classification of amyloid β supramolecular assemblies

Biochemistry

Volumn 46, Issue 51, 2007, Pages 15009-15017

  Yagi, Hisashi ^a,b   Ban, Tadato ^c   Morigaki, Kenichi ^c   Naiki, Hironobu ^b,d   Goto, Yuji ^a,b  

^a OSAKA UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^d UNIVERSITY OF FUKUI   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; DISEASES; FLUORESCENCE MICROSCOPY; SUPRAMOLECULAR CHEMISTRY; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID ASSEMBLIES; FIBRILLATION; RADIAL FIBRIL GROWTH; SPHERULITIC STRUCTURES;

PROTEINS;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; DODECYL SULFATE SODIUM; THIOFLAVINE;

ALZHEIMER DISEASE; AMYLOIDOSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; CONCENTRATION (PARAMETERS); ENVIRONMENTAL FACTOR; FLUORESCENCE SPECTROSCOPY; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID BETA-PROTEIN; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; QUARTZ;

EID: 37349062389     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701842n     Document Type: Article

References (53)

1. Shastry, B. S. (2003) Neurodegenerative disorders of protein aggregation, Neurochem. Int. 43, 1-7.
2. Dobson, C. M. (2003) Protein folding and misfolding, Nature 426, 884-890.
3. Cohen, F. E., and Kelly, J. W. (2003) Therapeutic approaches to protein-misfolding diseases, Nature 426, 905-909.
4. Naiki, H., and Nakakuki, K. (1996) First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro, Lab. Invest. 74, 374-383.
5. Dobson, C. M. (2001) The structural basis of protein folding and its links with human disease, Philos. Trans. R. Soc. London, Ser. B 356, 133-145.
6. Zerovnik, E. (2002) Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease, Eur. J. Biochem. 269, 3362-3371.
7. McLaurin, J., Yang, D., Yip, C. M., and Fraser, P. E. (2000) Review: Modulating factors in amyloid-β fibril formation, J. Struct. Biol. 130, 259-270.
8. Fandrich, M., and Dobson, C. M. (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation, EMBO J. 21, 5682-5690.
9. 2-microglobulin monomers in the presence of amyloid seeds, Biochemistry 45, 8760-8769.
10. Wei, G., and Shea, J. E. (2006) Effects of solvent on the structure of the Alzheimer amyloid-β(25-35) peptide, Biophys. J. 91, 1638-1647.
11. Westermark, P., Benson, M. D., Buxbaum, J. N., Cohen, A. S., Frangione, B., Ikeda, S., Masters, C. L., Merlini, G., Saraiva, M. J., and Sipe, J. D. (2002) Amyloid fibril protein nomenclature - 2002, Amyloid 9, 197-200.
12. Jin, L. W., Claborn, K. A., Kurimoto, M., Geday, M. A., Maezawa, I., Sohraby, F., Estrada, M., Kaminksy, W., and Kahr, B. (2003) Imaging linear birefringence and dichroism in cerebral amyloid pathologies, Proc. Natl. Acad. Sci. U.S.A. 100, 15294-15298.
13. Wetzel, R., Shivaprasad, S., and Williams, A. D. (2007) Plasticity of amyloid fibrils, Biochemistry 46, 1-10.
14. Kodali, R., and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly, Curr. Opin. Struct. Biol. 17, 48-57.
15. Tycko, R. (2004) Progress towards a molecular-level structural understanding of amyloid fibrils, Curr. Opin. Struct. Biol. 14, 96-103.
16. Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J. S. (2004) Conformational variations in an infectious protein determine prion strain differences, Nature 428, 323-328.
17. Jones, E. M., and Surewicz, W. K. (2005) Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids, Cell 121, 63-72.
18. Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W. M., Mattson, M. P., and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils, Science 307, 262-265.
19. Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., and Riek, R. (2005) 3D structure of Alzheimer's amyloid-β(1-42) fibrils, Proc. Natl. Acad. Sci. U.S.A. 102, 17342-17347.
20. Sunde, M., and Blake, C. (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction, Adv. Protein Chem. 50, 123-159.
21. Jimenez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., and Saibil, H. R. (2002) The protofilament structure of insulin amyloid fibrils, Proc. Natl. Acad. Sci. U.S.A. 99, 9196-9201.
22. Goldsbury, C. S., Wirtz, S., Muller, S. A., Sunderji, S., Wicki, P., Aebi, U., and Frey, P. (2000) Studies on the in vitro assembly of Aβ 1-40: Implications for the search for Aβ fibril formation inhibitors, J. Struct. Biol. 130, 217-231.
23. 2- microglobulin, J. Biol. Chem. 280, 32843-32848.
24. Ban, T., Yamaguchi, K., and Goto, Y. (2006) Direct observation of amyloid fibril growth, propagation, and adaptation, Acc. Chem. Res. 39, 663-670.
25. 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, 16462-16465.
26. Ban, T., Hoshino, M., Takahashi, S., Hamada, D., Hasegawa, K., Naiki, H., and Goto, Y. (2004) Direct observation of Aβ amyloid fibril growth and inhibition, J. Mol. Biol. 344, 757-767.
27. Ban, T., Morigaki, K., Yagi, H., Kawasaki, T., Kobayashi, A., Yuba, S., Naiki, H., and Goto, Y. (2006) Real-time and single fibril observation of the formation of amyloid β spherulitic structures, J. Biol. Chem. 281, 33677-33683.
28. Selkoe, D. J. (1994) Alzheimer's disease: A central role for amyloid, J. Neuropathol. Exp. Neurol. 53, 438-447.
29. Serpell, L. C. (2000) Alzheimer's amyloid fibrils: Structure and assembly, Biochim. Biophys. Acta 1502, 16-30.
30. Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics, Science 297, 353-356.
31. Gellermann, G. P., Appel, T. R., Tannert, A., Radestock, A., Hortschansky, P., Schroeckh, V., Leisner, C., Lutkepohl, T., Shtrasburg, S., Rocken, C., Pras, M., Linke, R. P., Diekmann, S., and Fandrich, M. (2005) Raft lipids as common components of human extracellular amyloid fibrils, Proc. Natl. Acad. Sci. U.S.A. 102, 6297-6302.
32. Gorbenko, G. P., and Kinnunen, P. K. (2006) The role of lipid-protein interactions in amyloid-type protein fibril formation, Chem. Phys. Lipids 141, 72-82.
33. Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., and Cole, G. (1996) Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice, Science 274, 99-102.
34. Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., and Rydel, R. E. (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death, J. Neurosci. 25, 1071-1080.
35. Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1, Anal. Biochem. 177, 244-249.
36. Wazawa, T., and Ueda, M. (2005) Total internal reflection fluorescence microscopy in single molecule nanobioscience, Adv. Biochem. Eng. Biotechnol. 95, 77-106.
37. Fraser, P. E., Nguyen, J. T., Chin, D. T., and Kirschner, D. A. (1992) Effects of sulfate ions on Alzheimer βA4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions, J. Neurochem. 59, 1531-1540.
38. 2-microglobulin-related amyloid fibrils at a neutral pH, Biochemistry 43, 11075-11082.
39. Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., and Matsuzaki, K. (2002) Interactions of amyloid β-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid, Biochemistry 41, 7385-7390.
40. Cruz, L., Urbanc, B., Borreguero, J. M., Lazo, N. D., Teplow, D. B., and Stanley, H. E. (2005) Solvent and mutation effects on the nucleation of amyloid β-protein folding, Proc. Natl. Acad. Sci. U.S.A. 102, 18258-18263.
41. Krebs, M. R., Macphee, C. E., Miller, A. F., Dunlop, I. E., Dobson, C. M., and Donald, A. M. (2004) The formation of spherulites by amyloid fibrils of bovine insulin, Proc. Natl. Acad. Sci. U.S.A. 101, 14420-14424.
42. 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond, J. Biol. Chem. 277, 21554-21560.
43. 2-microglobulin and amyloid formation in vitro, Biochemistry 39, 8735-8746.
44. Chen, Y. R., and Glabe, C. G. (2006) 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, 24414-24422.
45. Deshpande, A., Mina, E., Glabe, C., and Busciglio, J. (2006) Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons, J. Neurosci. 26, 6011-6018.
46. Yan, Y., and Wang, C. (2006) Aβ42 is more rigid than Aβ40 at the C terminus: Implications for Aβ aggregation and toxicity, J. Mol. Biol. 364, 853-862.
47. Lim, K. H., Collver, H. H., Le, Y. T., Nagchowdhuri, P., and Kenney, J. M. (2007) Characterizations of distinct amyloidogenic conformations of the Aβ (1-40) and (1-42) peptides, Biochem. Biophys. Res. Commun. 353, 443-449.
48. Fezoui, Y., Hartley, D. M., Walsh, D. M., Selkoe, D. J., Osterhout, J. J., and Teplow, D. B. (2000) A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils, Nat. Struct. Biol. 7, 1095-1099.
49. Fandrich, M., Zandomeneghi, G., Krebs, M. R., Kittler, M., Buder, K., Rossner, A., Heinemann, S. H., Dobson, C. M., and Diekmann, S. (2006) Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation, Acta Histochem. 108, 215-219.
50. Librizzi, F., and Rischel, C. (2005) The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways, Protein Sci. 14, 3129-3134.
51. Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., and Tycko, R. (2002) A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR, Proc. Natl. Acad. Sci. U.S.A. 99, 16742-16747.
52. Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils, Biochemistry 45, 498-512.
53. 2-microglobulin fragment are induced by fluorine-substituted alcohols, J. Mol. Biol. 363, 279-288.