For the best experience on the Abcam website please upgrade to a modern browser such as Google Chrome
Lewy bodies are intraneuronal aggregates of alpha-synuclein protein characteristic of Parkinson’s disease, Lewy body dementia, and other disorders. They are found in the regions of the brain responsible for motor control and result in a progressive decline in mental ability.
Figure 1. Alpha-synuclein fibril aggregate formation from the monomeric form.
The advantages of alpha-synuclein proteins
Assay alpha-synuclein proteins using thioflavin T (ThT)
Active alpha-synuclein aggregate seeds the formation of new alpha-synuclein aggregates from a pool of active alpha-synuclein monomers. ThT is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha-synuclein aggregates. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity.
Recombinant human alpha-synuclein protein monomer (active)
Recombinant human alpha-synuclein protein aggregate (active)
Recombinant human alpha-synuclein protein monomer (control)
Recombinant human alpha-synuclein protein aggregate (control)
Thioflavin T (ThT)
1. Luk, K. C. & Lee, V. M.-Y. Modeling Lewy pathology propagation in Parkinson’s disease. Parkinsonism Relat. Disord. 20, S85–S87 (2014). Read more
2. Vieira, B. D. M., Radford, R. A., Chung, R. S., Guillemin, G. J. & Pountney, D. L. Neuroinflammation in Multiple System Atrophy: Response to and Cause of α-Synuclein Aggregation. Front. Cell. Neurosci. 9, 437 (2015). Read more
3. Roberts, H. & Brown, D. Seeking a Mechanism for the Toxicity of Oligomeric α-Synuclein. Biomolecules 5, 282–305 (2015). Read more
4. Fernagut, P.-O. & Chesselet, M.-F. Alpha-synuclein and transgenic mouse models. Neurobiol. Dis. 17, 123–130 (2004). Read more
5. Ariesandi, W., Chang, C.-F., Chen, T.-E. & Chen, Y.-R. Temperature-Dependent Structural Changes of Parkinson’s Alpha-Synuclein Reveal the Role of Pre-Existing Oligomers in Alpha-Synuclein Fibrillization. PLoS One 8, e53487 (2013). Read more