Abstract
The insoluble and fibrillar aggregates of some proteins are thought to be the pathological cause of neurodegenerative diseases. The aggregation-propensities of different types of proteins were investigated by Thioflavine T fluorescence assay and atomic force microscopy imaging. Then, the structural transformations of the proteins from aqueous state to solid state were studied by circular dichroism spectroscopy. The results indicate that proteins of dif-ferent secondary structure show variations in their aggregation-propensities, together with their various structural transformations from aqueous state to solid state. Our studies imply that the structural transformation of proteins from solution to solid state is closely associated with their aggregation-propensities, which will provide insight into the molecular mechanism of protein aggregation in neurodegenerative diseases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6-11 |
| Number of pages | 6 |
| Journal | Nuclear Science and Techniques/Hewuli |
| Volume | 16 |
| Issue number | 1 |
| State | Published - Feb 2005 |
Keywords
- Aggregation-propensity
- Atomic force micros-copy imaging
- Circular dichroism spectroscopy
- Secondary structural transformation
- ThT fluorescence