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Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
Open accessAbstract
Assembly of normally soluble proteins into amyloid fibrils is a cause or associated symptom of numerous human disorders, including Alzheimer's and the prion diseases. We report molecular-level simulation of spontaneous fibril formation. Systems containing 12-96 model polyalanine peptides form fibrils at temperatures greater than a critical temperature that decreases with peptide concentration and exceeds the peptide's folding temperature, consistent with experimental findings. Formation of small amorphous aggregates precedes ordered nucleus formation and subsequent rapid fibril growth through addition of β-sheets laterally and monomeric peptides at fibril ends. The fibril's structure is similar to that observed experimentally.
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Cites
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
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Espinosa, H. D., Rim, J. E., Barthelat, F., & Buehler, M. J. (2009) · Progress in Materials Science · doi:10.1016/j.pmatsci.2009.05.001 · Cited by 817
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Self-citationDeshpande, A., Mina, E., Glabe, C., & Busciglio, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1189-06.2006 · Cited by 494
Metadata
- Authors
- Nguyen, H. D., & Hall, C. K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-11-08
- Volume
- 101
- Issue
- 46
- Pages
- 16180-16185
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2074255526
- Cited by
- 368
- References
- 2
- FWCI
- 13.11
- Type
- journal article
- Language
- en
- Open access
- green
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