Abstract
It is demonstrated using three independent methods that salmon calcitonin can form amyloid fibrils in vitro. Large aggregates are shown to exhibit a blue-green birefringence in cross polarised light after staining with congo red. Individual fibrils were observed using electron microscopy. These fibrils are approx. 50-60 Å in diameter and up to 20 000 Å in length and are similar in appearance to those observed in Alzheimer's disease. Finally, X-ray diffraction studies of the large aggregates reveal the cross-β conformation characteristic of the monomers in the fibre.
| Original language | English |
|---|---|
| Pages (from-to) | 111-114 |
| Number of pages | 4 |
| Journal | BBA - Molecular Basis of Disease |
| Volume | 1182 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 4 Aug 1993 |
Keywords
- Alzheimer's disease
- Amyloid formation
- Amyloid plaque
- Calcitonin
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology