The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation
Open accessAbstract
The fibrillation kinetics of the amyloid β peptide is analyzed in presence of cationic polystyrene nanoparticles of different size. The results highlight the importance of the ratio between the peptide and particle concentration. Depending on the specific ratio, the kinetic effects vary from acceleration of the fibrillation process by reducing the lag phase at low particle surface area in solution to inhibition of the fibrillation process at high particle surface area. The kinetic behavior can be explained if we assume a balance between two different pathways: first fibrillation of free monomer in solution and second nucleation and fibrillation promoted at the particle surface. The overall rate of fibrillation will depend on the interplay between these two pathways, and the predominance of one mechanism over the other will be determined by the relative equilibrium and rate constants.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Protein Misfolding, Functional Amyloid, and Human Disease
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Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
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Nucleation of protein fibrillation by nanoparticles
Linse, S., Cabaleiro-Lago, C., Xue, W.-F., Lynch, I., Lindman, S., Thulin, E., Radford, S. E., & Dawson, K. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701250104 · Cited by 886
Self-citationNecula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles
Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Lindman, S., Minogue, A. M., Thulin, E., Walsh, D. M., Dawson, K. A., & Linse, S. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8041806 · Cited by 546
Self-citation[17] Analysis of protein aggregation kinetics
Ferrone, F. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09019-9 · Cited by 539
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Cited by
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661
Biosafety and Bioapplication of Nanomaterials by Designing Protein–Nanoparticle Interactions
Yang, S., Liu, Y., Wang, Y., & Cao, A. (2013) · Small · doi:10.1002/smll.201201492 · Cited by 296
The viral protein corona directs viral pathogenesis and amyloid aggregation
Ezzat, K., Pernemalm, M., Pålsson, S., Roberts, T. C., Järver, P., Dondalska, A., Bestas, B., Sobkowiak, M. J., Levänen, B., Sköld, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10192-2 · Cited by 209
Recent Advancements of Nanomedicine in Neurodegenerative Disorders Theranostics
Mukherjee, S., Madamsetty, V. S., Bhattacharya, D., Roy Chowdhury, S., Paul, M. K., & Mukherjee, A. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202003054 · Cited by 152
Wei, Z., Dong, X., & Sun, Y. (2024) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2024.113907 · Cited by 36
Metadata
- Authors
- Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Dawson, K. A., & Linse, S.
- Venue
- ACS Chemical Neuroscience
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-01-27
- Volume
- 1
- Issue
- 4
- Pages
- 279-287
- ISSN
- 1948-7193 (ISSN-L)
- OpenAlex
- W1969699861
- Cited by
- 275
- References
- 24
- FWCI
- 7.04
- Type
- journal article
- Language
- en
- Open access
- green
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- Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Dawson, K. A., & Linse, S. (2010). Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation. ACS Chemical Neuroscience. https://doi.org/10.1021/cn900027u
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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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