Journal
METHODS AND APPLICATIONS IN FLUORESCENCE
Volume 1, Issue 1, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/2050-6120/1/1/015006
Keywords
-
Categories
Funding
- EPSRC
- SFC
- EPSRC [EP/K000195/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/K000195/1] Funding Source: researchfish
Ask authors/readers for more resources
The development of Alzheimer's disease is associated with the aggregation of the beta-amyloid peptides A beta(1-40) and A beta(1-42). It is believed that the small oligomers formed during the early stages of the aggregation are neurotoxic and involved in the process of neurodegeneration. In this paper we use fluorescence decay measurements of beta-amyloid intrinsic fluorophore tyrosine (Tyr) and molecular dynamics (MD) simulations to study the early stages of oligomer formation for the A beta(1-40) and A beta(1-42) peptides in vitro. We demonstrate that the lifetime distributions of the amyloid fluorescence decay efficiently describe changes in the complex Tyr photophysics during the peptide aggregation and highlight the differences in aggregation performance of the two amyloids. Tyr fluorescence decay is found to be a more sensitive sensor of A beta(1-40) and A beta(1-42) aggregation. The MD simulation of the peptide aggregation is compared with the experimental data and supports a four-rotamer model of Tyr.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available