The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Concentration Dependent Cu2+Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-β Peptide
Open accessAbstract
The Amyloid beta peptide (Abeta) of Alzheimer's diseases (AD) is closely linked to the progressive cognitive decline associated with the disease. Cu2+ ions can induce the de novo aggregation of the Abeta peptide into non-amyloidogenic aggregates and the production of a toxic species. The mechanism by which Cu2+ mediates the change from amyloid material toward Cu2+ induced aggregates is poorly defined. Here we demonstrate that the aggregation state of Abeta1-42 at neutral pH is governed by the Cu2+:peptide molar ratio. By probing amyloid content and total aggregation, we observed a distinct Cu2+ switching effect centered at equimolar Cu2+:peptide ratios. At sub-equimolar Cu2+:peptide molar ratios, Abeta1-42 forms thioflavin-T reactive amyloid; conversely, at supra-equimolar Cu2+:peptide molar ratios, Abeta1-42 forms both small spherical oligomers approximately 10-20 nm in size and large amorphous aggregates. We demonstrate that these insoluble aggregates form spontaneously via a soluble species without the presence of an observable lag phase. In seeding experiments, the Cu2+ induced aggregates were unable to influence fibril formation or convert into fibrillar material. Aged Cu2+ induced aggregates are toxic when compared to Abeta1-42 aged in the absence of Cu2+. Importantly, the formation of dityrosine crosslinked Abeta, by the oxidative modification of the peptide, only occurs at equimolar molar ratios and above. The formation of dityrosine adducts occurs following the initiation of aggregation and hence does not drive the formation of the Cu2+ induced aggregates. These results define the role Cu2+ plays in modulating the aggregation state and toxicity of Abeta1-42.
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Cites
Neurodegenerative diseases and oxidative stress
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Self-citationCopper, iron and zinc in Alzheimer's disease senile plaques
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Self-citationAtwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
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Self-citationAqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal Depletion
Cherny, R. A., Legg, J. T., McLean, C. A., Fairlie, D. P., Huang, X., Atwood, C. S., Beyreuther, K., Tanzi, R. E., Masters, C. L., & Bush, A. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23223 · Cited by 482
Self-citationCopper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42
Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327
Amyloid-β Binds Cu 2+ in a Mononuclear Metal Ion Binding Site
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Cited by
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870
Biological metals and metal-targeting compounds in major neurodegenerative diseases
Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497
Self-citationMolecular targets of oxidative stress
Avery, S. V. (2011) · Biochemical Journal · doi:10.1042/bj20101695 · Cited by 474
Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332
Hureau, C., & Faller, P. (2009) · Biochimie · doi:10.1016/j.biochi.2009.03.013 · Cited by 259
Metadata
- Authors
- Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero-Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-02-13
- Volume
- 46
- Issue
- 10
- Pages
- 2881-2891
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1980357013
- Cited by
- 194
- References
- 9
- FWCI
- 7.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero-Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R. (2007). Concentration Dependent Cu2+Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-β Peptide. Biochemistry. https://doi.org/10.1021/bi0620961
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