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

We monitor early stages of beta-amyloid (Aβ1–40) aggregation, one of the key processes leading to Alzheimer's disease (AD), in the presence of high glucose concentrations by measuring Aβ1– 40 intrinsic fluorescence. The multiple peaks and their shifts observed in the time-resolved emission spec...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2021-06, Vol.704, p.108886-108886, Article 108886
Hauptverfasser:	Alghamdi, Abeer, Forbes, Shareen, Birch, David J.S., Vyshemirsky, Vladislav, Rolinski, Olaf J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Alzheimer's disease Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Beta-amyloid aggregation Diabetes Mellitus - metabolism Glycation Humans Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Multimerization Time-resolved emission spectra Tyrosine fluorescence decay
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Beschreibung
Zusammenfassung:	We monitor early stages of beta-amyloid (Aβ1–40) aggregation, one of the key processes leading to Alzheimer's disease (AD), in the presence of high glucose concentrations by measuring Aβ1– 40 intrinsic fluorescence. The multiple peaks and their shifts observed in the time-resolved emission spectra (TRES) reveal the impact of glycation on Aβ1– 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. [Display omitted]
ISSN:	0003-9861 1096-0384
DOI:	10.1016/j.abb.2021.108886