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Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
Open accessAbstract
Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Self-citationThe amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Self-citationThe Amyloid-β Pathway in Alzheimer’s Disease
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
Self-citationCofactors are essential constituents of stable and seeding-active tau fibrils
Fichou, Y., Lin, Y., Rauch, J. N., Vigers, M., Zeng, Z., Srivastava, M., Keller, T. J., Freed, J. H., Kosik, K. S., & Han, S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810058115 · Cited by 128
Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters
Xue, W.-F., Hellewell, A. L., Hewitt, E. W., & Radford, S. E. (2010) · Prion · doi:10.4161/pri.4.1.11378 · Cited by 117
Production of lysozyme nanofibers using deep eutectic solvent aqueous solutions
Silva, N. H. C. S., Pinto, R. J. B., Freire, C. S. R., & Marrucho, I. M. (2016) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2016.07.005 · Cited by 47
Gutiérrez-Medina, B., Fehr, A. N., & Block, S. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907133106 · Cited by 37
Beal, D. M., Tournus, M., Marchante, R., Purton, T. J., Smith, D. P., Tuite, M. F., Doumic, M., & Xue, W.-F. (2020) · iScience · doi:10.1016/j.isci.2020.101512 · Cited by 29
Metadata
- Authors
- Knowles, T. P., Fitzpatrick, A. W., Meehan, S., Mott, H. R., Vendruscolo, M., Dobson, C. M., & Welland, M. E.
- Venue
- Science
- Published
- 2007-12-21
- Volume
- 318
- Issue
- 5858
- Pages
- 1900-1903
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1985121447
- Cited by
- 782
- References
- 0
- FWCI
- 20.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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