Computational model of amyloid-beta aggregation
October 2017
Rice University, Houston, USA(1)
University of Miami, Coral Gables, USA(2)
University of Miami, Coral Gables, USA(2)
Currently, the onset of Alzheimer's disease is thought to be linked to the transition of amyloid-beta from soluble peptides to aggregated fibrils. Therefore, inhibiting amyloid-beta aggregation has been a long-pursued objective. But how amyloid-beta aggregates and how different molecules bind to it is still not known. Here, a rhenium complex that binds to amyloid-beta is used to identify its binding sites through light irradiation. Afterwards, the researchers used molecular dynamics to simulate the binding sites of amyloid-beta with the rhenium complex. The identified locations were further confirmed by the identification of oxidised sites via tandem mass spectrometry. This method elucidates binding sites and mechanisms that could be potentially used to design therapeutic strategies to interrupt amyloid-beta aggregation and/or accumulation.
Photochemical identification of molecular binding sites on the surface of amyloid-β fibrillar aggregates
Angel A Martí(1), Rajeev Prabhakar(2)
Added on: 08-09-2021
[1] https://www.sciencedirect.com/science/article/pii/S2451929417304011[2] https://data.jrc.ec.europa.eu/dataset/a8fd26ef-b113-47ab-92ba-fd2be449c7eb
