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Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Open accessAbstract
We describe a full structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ 1–40 ), based on numerous constraints from solid state NMR and electron microscopy. This model applies specifically to fibrils with a periodically twisted morphology, with twist period equal to 120 ± 20 nm (defined as the distance between apparent minima in fibril width in negatively stained transmission electron microscope images). The structure has threefold symmetry about the fibril growth axis, implied by mass-per-length data and the observation of a single set of 13 C NMR signals. Comparison with a previously reported model for Aβ 1–40 fibrils with a qualitatively different, striated ribbon morphology reveals the molecular basis for polymorphism. At the molecular level, the 2 Aβ 1–40 fibril morphologies differ in overall symmetry (twofold vs. threefold), the conformation of non-β-strand segments, and certain quaternary contacts. Both morphologies contain in-register parallel β-sheets, constructed from nearly the same β-strand segments. Because twisted and striated ribbon morphologies are also observed for amyloid fibrils formed by other polypeptides, such as the amylin peptide associated with type 2 diabetes, these structural variations may have general implications.
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Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · cited 1×
“Selfpropagating variations in the molecular structures of amyloid fibrils or amyloid-like aggregates formed by a single protein are believed to be responsible for the existence of multiple strains of mammalian prion diseases (6, 7) and yeast prion phenotypes (8–11), and may produce variations in the toxicity (4) or pa…”
BackgroundPrions of fungi: inherited structures and biological roles
Wickner, R. B., Edskes, H. K., Shewmaker, F., & Nakayashiki, T. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1708 · Cited by 231
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Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
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Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
Swanson, C. J., Zhang, Y., Dhadda, S., Wang, J., Kaplow, J., Lai, R. Y. K., Lannfelt, L., Bradley, H., Rabe, M., Koyama, A., et al. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00813-8 · Cited by 847
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
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Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361
Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin
Ultsch, M., Li, B., Maurer, T., Mathieu, M., Adolfsson, O., Muhs, A., Pfeifer, A., Pihlgren, M., Bainbridge, T. W., Reichelt, M., et al. (2016) · Scientific Reports · doi:10.1038/srep39374 · Cited by 124
Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119
Green Tea Extracts EGCG and EGC Display Distinct Mechanisms in Disrupting Aβ42 Protofibril
Zhan, C., Chen, Y., Tang, Y., & Wei, G. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00277 · Cited by 115
Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment
Morgado, I., Wieligmann, K., Bereza, M., Rönicke, R., Meinhardt, K., Annamalai, K., Baumann, M., Wacker, J., Hortschansky, P., Malešević, M., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206433109 · Cited by 80
Bamberger, C., Pankow, S., Martínez-Bartolomé, S., Ma, M., Diedrich, J., Rissman, R. A., & Yates, J. R. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00912 · Cited by 70
Belsare, K. D., Wu, H., Mondal, D., Bond, A., Castillo, E., Jin, J., Jo, H., Roush, A. E., Pilla, K. B., Sali, A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114486119 · Cited by 68
Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection
Brown, M. R., Radford, S. E., & Hewitt, E. W. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.609073 · Cited by 67
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53
Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease
Kim, C., Haldiman, T., Kang, S.-G., Hromadkova, L., Han, Z. Z., Chen, W., Lissemore, F., Lerner, A., de Silva, R., Cohen, M. L., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg0253 · Cited by 55
Abelein, A., Ciofi-Baffoni, S., Mörman, C., Kumar, R., Giachetti, A., Piccioli, M., & Biverstål, H. (2022) · JACS Au · doi:10.1021/jacsau.2c00438 · Cited by 52
Selectivity in ROS-Induced Peptide Backbone Bond Cleavage
Stringfellow, H. M., Jones, M. R., Green, M. C., Wilson, A. K., & Francisco, J. S. (2014) · The Journal of Physical Chemistry A · doi:10.1021/jp508877m · Cited by 28
Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils
Scherpelz, K. P., Wang, S., Pytel, P., Madhurapantula, R. S., Srivastava, A. K., Sachleben, J. R., Orgel, J., Ishii, Y., & Meredith, S. C. (2021) · Scientific Reports · doi:10.1038/s41598-020-80042-5 · Cited by 12
Saha, D., Sun, X., Yang, W., Luo, J., & Zheng, W. (2026) · JACS Au · doi:10.1021/jacsau.6c00126 · Cited by 2
Metadata
- Authors
- Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-11-25
- Volume
- 105
- Issue
- 47
- Pages
- 18349-18354
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2162741488
- Cited by
- 1,160
- References
- 3
- FWCI
- 39.21
- Type
- journal article
- Language
- en
- Open access
- green
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