Abstract
We monitor early stages of beta-amyloid (Aβ 1–40) aggregation, one of the key processes leading to Alzheimer's disease (AD), in the presence of high glucose concentrations by measuring Aβ 1– 40 intrinsic fluorescence. The multiple peaks and their shifts observed in the time-resolved emission spectra (TRES) reveal the impact of glycation on Aβ 1– 40 oligomerisation. The results show that formation of the advanced glycation end products (AGEs) alters the aggregation pathway. These changes are highly relevant to our understanding of the pathophysiology of AD and the implication of AGE and diabetes in these pathways.
Original language | English |
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Article number | 108886 |
Number of pages | 8 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 704 |
Early online date | 19 Apr 2021 |
DOIs | |
Publication status | Published - 15 Jun 2021 |
Keywords
- beta-amyloid aggregation
- time-resolved emission spectra
- glycation
- tyrosine fluorescence decay
- Alzheimer’s disease