Simulation of the fibril formation typical for Alzheimer's disease
December 2012
University of California Irvine, Irvine, USA
Amyloid-beta aggregation and fibril formation are some of the hallmarks of Alzheimer's disease, but the mechanism that connects these phenomena with the onset of the disease is not yet clear. Before, it has been proposed that the formation of these fibrils follows a dock/lock mechanism. Therefore, in this study, the researchers use a simulation of two-dimensional ultraviolet spectroscopy to confirm this hypothesis. The signals generated can be used to monitor local dynamics and conformational changes in the secondary structure of amyloid-beta peptides, showing that these are in agreement with a dock/lock pathway. The results confirm that this method can be used to further explore the dynamics of protein aggregation.
Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopy
Alfonso R Lam
Added on: 08-06-2021
[1] https://pubs.acs.org/doi/10.1021/jp3101267[2] https://data.jrc.ec.europa.eu/dataset/a8fd26ef-b113-47ab-92ba-fd2be449c7eb
