Detecting beta-amyloid glycation by intrinsic fluorescence-Understanding the link between diabetes and Alzheimer's disease

We monitor early stages of beta-amyloid (A beta 1-40) aggregation, one of the key processes leading to Alzheimer's disease (AD), in the presence of high glucose concentrations by measuring A beta 1- 40 intrinsic fluorescence. The multiple peaks and their shifts observed in the time-resolved emission spectra (TRES) reveal the impact of glycation on A beta 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.

Automated summary

Monitoring the aggregation of Aβ1-40 in the presence of high glucose concentrations reveals the impact of glycation on oligomerization, altering the aggregation pathway and providing insights into the pathophysiology of Alzheimer's disease. The formation of advanced glycation end products plays a significant role in these pathways, highlighting the connection between AGEs, diabetes, and AD progression.