Researchers at the University of Washington have created a molecule that aims to stop the formation of protein clusters thought to be a prime contributor to Alzheimer’s disease.
In a healthy brain, these amyloid beta proteins don’t cause problems. But in patients with Alzheimer’s, they stick together and become toxic. The team of researchers set out to create a compound that would block the protein clusters, called amyloid beta oligomers, from forming.
Historically, much of the focus on these proteins has been on the plaque they form over time. But more recent research suggests their negative effects start much earlier.
The researchers tested their synthetic peptide in mice and worms, as well as human brain cells that were grown in culture. In tests on live mice, the treatment reduced the levels of the toxic protein clusters by 40 percent in a day. In human brain cells, the synthetic peptide blocked the amyloid beta oligomers from forming even larger clusters.
The findings were published this week in the journal Proceedings of the National Academy of Sciences. The paper’s lead author was Dylan Shea, a UW doctoral student in molecular engineering.
The research team is continuing to hunt for even better compounds that can clear away the problematic clusters. Their test to detect amyloid beta oligomer levels could be also used to help spot Alzheimer’s disease before the onset of symptoms.
“What we’re really after are potential therapeutics against amyloid beta and diagnostic measures to detect toxic oligomers in people,” Valerie Daggett, a corresponding author of the research and a professor of bioengineering at UW, said in a news release.
The researchers also showed that the early stages of these protein clusters are the most toxic to brain cells, which supports other recent Alzheimer’s research.
“Amyloid beta definitely plays a lead role in Alzheimer’s disease, but while historically attention has been on the plaques, more and more research instead indicates that amyloid beta oligomers are the toxic agents that disrupt neurons,” Daggett said in the release.
