| Autor: |
Mikkel, Herzberg, Daniel, Szunyogh, Peter W, Thulstrup, Tue, Hassenkam, Lars, Hemmingsen |
| Rok vydání: |
2020 |
| Předmět: |
|
| Zdroj: |
Chembiochem : a European journal of chemical biology. 21(24) |
| ISSN: |
1439-7633 |
| Popis: |
Structural characterization of aggregates and fibrils of the Aβ protein is pivotal to the molecular-level elucidation of Alzheimer's disease (AD). AFM-IR spectroscopy provides nanoscale resolution, and thus allows the interrogation of individual aggregates and fibrils. During aggregation of Aβ, we observed mainly disordered Aβ at t=15 min, but substantial structural diversity including the co-existence of parallel and antiparallel β-sheets within a large amorphous aggregate at t=2 hours, while fibrils exhibited the expected signature of parallel β-sheets at t=1 week. The resonance observed for parallel β-sheets at t=2 hours coincides with that observed for fibrils (at 1634 cm |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
Plný text