The Japanese mutant Aβ (ΔE22-Aβ 1-39) forms fibrils instantaneously, with low-thioflavin T fluorescence: Seeding of wild-type Aβ 1-40 into atypical fibrils by Δe22- Aβ 1-39

Biochemistry

Volumn 50, Issue 12, 2011, Pages 2026-2039

  Cloe, Adam L ^a   Orgel, Joseph P R O ^b   Sachleben, Joseph R ^a   Tycko, Robert ^c   Meredith, Stephen C ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b Illinois Institute of Technology   (United States)

^c NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID PRECURSOR PROTEINS; CRITICAL CONCENTRATION; D SPACING; EQUIMOLAR MIXTURES; FLUORESCENCE DEPOLARIZATION; LAG PHASE; LOW CONCENTRATIONS; LOW LEVEL; MOLAR MIXTURES; ORDER OF MAGNITUDE; RAPID NUCLEATION; SOLID-STATE NUCLEAR MAGNETIC RESONANCE; THIOFLAVIN T; WILD TYPES;

BINDING SITES; BIOCHEMISTRY; DIFFRACTION; FLUORESCENCE; GLYCOPROTEINS; NUCLEAR MAGNETIC RESONANCE; OLIGOMERS; ORGANIC SOLVENTS; RESONANCE; SIZE EXCLUSION CHROMATOGRAPHY; X RAY DIFFRACTION;

PEPTIDES;

AMYLOID BETA PROTEIN[1-40]; AMYLOID PRECURSOR PROTEIN; DIMETHYL SULFOXIDE; MONOMER; OLIGOMER; ORGANIC SOLVENT; THIOFLAVINE;

ARTICLE; BETA SHEET; BINDING AFFINITY; BINDING SITE; CONCENTRATION (PARAMETERS); DEPOLARIZATION; ELECTRON MICROSCOPY; FIBER; FLUORESCENCE MICROSCOPY; GEL PERMEATION CHROMATOGRAPHY; MUTANT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN STRUCTURE; SOLID STATE; WILD TYPE; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; BINDING SITES; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CONGO RED; DIMETHYL SULFOXIDE; KINETICS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; THIAZOLES; X-RAY DIFFRACTION;

EID: 79952938717     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1016217     Document Type: Article

References (49)

1. Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., and Frangione, B. (1990) Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type Science 248, 1124-1126
2. Van Broeckhoven, C., Haan, J., Bakker, E., Hardy, J. A., Van Hul, W., Wehnert, A, Vegter-Van der Vlis, M., and Roos, R. A. C. (1990) Amyloid β protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch) Science 248, 1120-1122 (Pubitemid 20189867)
3. Cras, P., van Harskamp, F., Hendriks, L., Ceuterick, C., van Duijn, C. M., Stefanko, S. Z., Hofman, A., Kros, J. M., Van Broeckhoven, C., and Martin, J. J. (1998) Presenile Alzheimer dementia characterized by amyloid angiopathy and large amyloid core type senile plaques in the APP 692Ala → Gly mutation Acta Neuropathol. 96, 253-260 (Pubitemid 28419843)
4. Tagliavini, F., Rossi, G., Padovani, A., Magoni, M., Andora, G., Sgarzi, M., Bizzi, A., Savioardo, M., Carella, F., Morbin, M., Giaccone, G., and Bugiani, O. (1999) A new bPP mutation related to hereditary cerebral haemorrhage Alzheimer's Rep. 2 (Suppl.) S28
5. Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., Näslund, J., and Lannfelt, L. (2001) The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation Nat. Neurosci. 4, 887-893 (Pubitemid 32801591)
6. Grabowski, T. J., Cho, H. S., Vonsattel, J. P., Rebeck, G. W., and Greenberg, S. M. (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy Ann. Neurol. 49, 697-705 (Pubitemid 32530235)
7. 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 (Pubitemid 36034043)
8. Balbach, J. J., Petkova, A. T., Oyler, N. A., Antzutkin, O. N., Gordon, D. J., Meredith, S. C., and Tycko, R. (2002) Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: Evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance Biophys. J. 83, 1205-1216 (Pubitemid 34803651)
9. Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 105, 18349-18354
10. Tycko, R. (2006) Molecular structure of amyloid fibrils: Insights from solid-state NMR Q. Rev. Biophys. 39, 1-55 (Pubitemid 44566373)
11. Tomiyama, T., Nagata, T., Shimada, H., Teraoka, R., Fukushima, A., Kanemitsu, H., Takuma, H., Kuwano, R., Imagawa, M., Ataka, S., Wada, Y., Yoshioka, E., Nishizaki, T., Watanabe, Y., and Mori, H. (2008) A new amyloid β variant favoring oligomerization in Alzheimer's-type dementia Ann. Neurol. 63, 377-387 (Pubitemid 351499867)
12. Hardy, J. A. and Higgins, G. A. (1992) Alzheimer's disease: The amyloid cascade hypothesis Science 256, 184-185
13. Tanzi, R. E. and Bertram, L. (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective Cell 120, 545-555 (Pubitemid 40269768)
14. Klein, W. L., Stine, W. B., Jr., and Teplow, D. B. (2004) Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease Neurobiol. Aging 25, 569-580 (Pubitemid 38686476)
15. Bitan, G., Fradinger, E. A., Spring, S. M., and Teplow, D. B. (2005) Neurotoxic protein oligomers: What you see is not always what you get Amyloid 12, 88-95 (Pubitemid 40978716)
16. Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., and Ashe, K. H. (2006) A specific amyloid-β protein assembly in the brain impairs memory Nature 440, 352-357
17. Nishitsuji, K., Tomiyama, T., Ishibashi, K., Ito, K., Teraoka, R., Lambert, M. P., Klein, W. L., and Mori, H. (2009) The E693Δ mutation in amyloid precursor protein increases intracellular accumulation of amyloid β oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells Am. J. Pathol. 174, 957-969
18. Klunk, W. E., Pettegrew, J. W., and Abraham, D. J. (1989) Quantitative evaluation of congo red binding to amyloid-like proteins with a β-pleated sheet conformation J. Histochem. Cytochem. 37, 1273-1282
19. 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 (Pubitemid 19088253)
20. Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., and Meredith, S. C. (2005) Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid Biochemistry 44, 6003-6014 (Pubitemid 40570694)
21. Tycko, R., Sciarretta, K. L., Orgel, P. R. O., and Meredith, S. C. (2009) Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils Biochemistry 48, 6072-6084
22. LeVine, H., III (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 309, 274-284
23. LeVine, H., III (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution Protein Sci. 2, 404-410
24. Finder, W. H., Vodopivec, I., Nitsch, R. M., and Rudi Glockshuber, R. (2010) The recombinant amyloid-β peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ1-42 J. Mol. Biol. 396, 9-18
25. Biancalana, M., Makabe, K., Koide, A., and Koide, S. (2009) Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies J. Mol. Biol. 385, 1052-1063
26. Wu, C., Biancalana, M., Koide, S., and Shea, J. E. (2009) Binding modes of thioflavin-T to the single-layer β-sheet of the peptide self-assembly mimics J. Mol. Biol. 394, 627-633
27. Biancalana, M. and Koide, S. (2010) Molecular mechanism of Thioflavin-T binding to amyloid fibrils Biochim. Biophys. Acta 1804, 1405-1412
28. O'Nuallain, B., Shivaprasad, S., Kheterpal, I., and Wetzel, R. (2005) Thermodynamics of Aβ(1-40) Amyloid Fibril Elongation Biochemistry 44, 12709-12718 (Pubitemid 41377310)
29. Lanning, J. D., Hawk, A. J., Derryberry, J., and Meredith, S. C. (2010) Chaperone-like N -methyl Peptide Inhibitors of Polyglutamine Aggregation Biochemistry 49, 7108-7118
30. Stubbs, G. (1999) Developments in fiber diffraction Curr. Opin. Struct. Biol. 9, 615-619 (Pubitemid 29460589)
31. Torbet, J. (1987) Using magnetic orientation to study structure and assembly Trends Biochem. Sci. 12, 327-330
32. Lakowicz, J. R. (1983) Principles of Fluorescence Spectroscopy, Chapter 5, Plenum Press, New York.
33. Tycko, R. (2007) Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR J. Chem. Phys. 126, 064506
34. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques J. Biomol. NMR 4, 845-858
35. Jarrett, J. T. and Lansbury, P. T., Jr. (1993) Seeding "One-Dimensional Crystallization" of Amyloid: A Pathogenic Mechanism in Alzheimer's Disease and Scrapie? Cell 73, 1055-1059
36. Thirumalai, D., Klimov, D. K., and Dima, R. I. (2003) Emerging ideas on the molecular basis of protein and peptide aggregation Curr. Opin. Struct. Biol. 13, 146-159 (Pubitemid 36515142)
37. Kodaka, M. (2004) Requirements for generating sigmoidal time-course aggregation in nucleation-dependent polymerization model Biophys. Chem. 107, 243-253 (Pubitemid 38221272)
38. 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 (Pubitemid 43100415)
39. Takuma, H., Teraoka, R., Mori, H., and Tomiyama, T. (2008) Amyloid β E22Δ variant induces synapse alteration in mouse hippocampal slices NeuroReport 19, 615-619 (Pubitemid 351489355)
40. DePace, A. H. and Weissman, J. S. (2002) Origins and kinetic consequences of diversity in Sup35 yeast prion fibers Nat. Struct. Biol. 9, 389-396 (Pubitemid 34462559)
41. Vitrenko, Y. A., Gracheva, E. O., Richmond, J. E., and Liebman, S. W. (2007) Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM J. Biol. Chem. 282, 1779-1787 (Pubitemid 47076692)
42. Toyama, B. H., Kelly, M. J., Gross, J. D., and Weissman, J. S. (2007) The structural basis of yeast prion strain variants Nature 449, 233-237 (Pubitemid 47402368)
43. Makarava, N., Ostapchenko, V. G., Savtchenko, R., and Baskakov, I. V. (2009) Conformational switching within individual amyloid fibrils J. Biol. Chem. 284, 14386-14395
44. Kodali, R. and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly Curr. Opin. Struct. Biol. 17, 48-57 (Pubitemid 46242190)
45. Cobb, N. J. and Surewicz, W. K. (2009) Prion diseases and their biochemical mechanisms Biochemistry 48, 2574-2585
46. Yamaguchi, K., Takahashi, S., Kawai, T., Naiki, H., and Goto, Y. (2005) Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352, 952-960 (Pubitemid 41267080)
47. Kihara, M., Chatani, E., Sakai, M., Hasegawa, K., Naiki, H., and Goto, Y. (2005) Seeding-dependent maturation of β2-microglobulin amyloid fibrils at neutral pH J. Biol. Chem. 280, 12012-12018 (Pubitemid 40418519)
48. Miravalle, L., Tokuda, T., Chiarle, R., Giaccone, G., Bugiani, O., Tagliavini, F., Frangione, B., and Ghiso, J. (2000) Substitutions at codon 22 of Alzheimer's Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells J. Biol. Chem. 275, 27110-27116
49. Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., Nishitsuji, K., Ito, K., Shimada, H., Lambert, M. P., Klein, W. L., and Mori, H. (2010) A Mouse Model of Amyloid β Oligomers: Their Contribution to Synaptic Alteration, Abnormal Tau Phosphorylation, Glial Activation, and Neuronal Loss In Vivo J. Neurosci. 30, 4845-4856