The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein
Open accessAbstract
The flavonoid baicalein inhibits fibrillation of α-synuclein, which is a major component of the Lewy bodies in Parkinson’s disease. It has been known that baicalein induces the formation of the α-synuclein oligomers and consequently prevents its fibrillation. In order to evaluate structural properties of the baicalein-stabilized oligomers, we purified the oligomer species by HPLC and examined their stability and structure by CD, FTIR, SEC-HPLC, SAXS, and AFM. Baicalein-stabilized oligomers are β-sheet-enriched according to CD and FTIR analysis. They did not form fibrils even after very prolonged incubation. From the SAXS data and AFM images, the oligomers were characterized as quite compact globular species. Oligomers were extremely stable, with a GdmCl Cm=3.3 M. This high stability explains the previously observed inhibition properties of baicalein toward α-synuclein fibrillation. These baicalein-stabilized oligomers, being added to the solution of the aggregating α-synuclein, were able to noticeably inhibit its fibrillation. After the prolonged co-incubation, short fibrils were formed, suggesting effective interaction of oligomers with the monomeric α-synuclein. Membrane permeability tests suggested that the baicalein-stabilized oligomers had a mild effect on the integrity of the membrane surface. This effect was rather similar to that of the monomeric protein, suggesting that the targeted stabilization of certain α-synuclein oligomers might offer a potential strategy for the development of novel Parkinson’s disease therapies.
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
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Metadata
- Authors
- Hong, D.-P., Fink, A. L., & Uversky, V. N.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 383
- Issue
- 1
- Pages
- 214-223
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1969859162
- Cited by
- 177
- References
- 5
- FWCI
- 7.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Hong, D.-P., Fink, A. L., & Uversky, V. N. (2008). Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2008.08.039
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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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