The research has uncovered that the protein plaques associated with Alzheimer’s are stickier than previously believed. Scientists from Rice University are shedding new light on a peptide associated with Alzheimer's disease through the use of fluorescence lifetime. According to the Centers for Disea
A researcher in the lab of Rice’s Angel Martí holds a vial of fluorescent dye molecules in solution. Using time-resolved spectroscopy, which tracks the fluorescence lifetime of dye molecules, Martí and collaborators describe a second binding site on amyloid-beta deposits associated with Alzheimer’s disease, opening the door to the development of new therapies.
Amyloid plaque deposits in the brain are a main feature of Alzheimer’s. “Amyloid-beta is a peptide that aggregates in the brains of people that suffer from Alzheimer’s disease, forming these supramolecularfibers, or fibrils,” said Martí, a professor of chemistry, bioengineering, and materials science and nanoengineering and faculty director of the Rice Emerging Scholars Program. “Once they grow sufficiently, these fibrils precipitate and form what we call amyloid plaques.
The Martí group had previously identified a first binding site for amyloid-beta deposits by figuring out how metallic dye molecules were able to bind to pockets formed by the fibrils. The molecules’ ability to fluoresce, or emit light when excited under a spectroscope, indicated the presence of the binding site.
“These findings are allowing us to create a map of binding sites in amyloid-beta and a record of the aminocompositions required for the formation of binding pockets in amyloid-beta fibrils,” Martí said. “The molecule was not binding to a unique site in the amyloid-beta but to two different sites. And that was extremely interesting because our previous studies only indicated one binding site. That happened because we were not able to see all the components with the technologies we were using previously,” he added.
Martí said the findings will also impact the study of “many diseases associated with other kinds of amyloids: Parkinson’s, amyotrophic lateral sclerosis , Type 2 diabetes, systemic amyloidosis.”
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