Scientists at Oregon State University recently found a way to watch one of the main drivers of Alzheimer’s disease happen in real time. For years, researchers have known that protein clumping in the brain blocks neural pathways, but they usually only saw the end result. Now, they can watch the process second by second.

Marilyn Rampersad Mackiewicz and a team of undergraduate students used a technique called fluorescence anisotropy to monitor how metals like copper interact with amyloid-beta proteins. While the brain needs some metals to function, too much copper can cause proteins to bunch up. By watching this happen live, the team could see exactly how different molecules, called chelators, stepped in to stop the damage.

Cleaning Up the Brain

The word chelator comes from the Greek word for “claw,” which perfectly describes how they work. These molecules act like tiny hands that reach out and grab metal ions. The OSU team tested two different types of these “claws” to see if they could undo the protein clumping.

One chelator grabbed every metal ion it saw without picking the right ones. However, the second one was much more specific and targeted the exact copper ions that cause the most trouble. This distinction is a big deal for future drug design because it shows we can be surgical about which metals we remove from the brain.

“Too many of some metal ions, like copper, can interact with amyloid-beta proteins in ways that lead to protein aggregation, but most experiments have only shown the end result, not the interactions and aggregation process itself,” Mackiewicz said. “We developed a method that lets us observe those interactions live, second by second, and directly measure how different molecules interrupt or reverse them.

“It shifts the question from ‘does something work?’ to ‘how does it work, and when?’” Mackiewicz added.

A New Roadmap for Alzheimer’s Treatment

While actual medical treatments are still years away, this discovery gives researchers a clearer path forward. Many Alzheimer’s drugs fail because we don’t fully understand why these protein clumps form in the first place. By seeing the process as it happens, scientists can build better tools to stop it.

“That kind of real-time insight into how the protein aggregations form and unform is important for designing better treatments and for understanding why some widely used chemical approaches may not behave the way we assume they do,” Mackiewicz said. “Alzheimer’s affects millions of families and while clinical treatments based on this work remain years away, discoveries like this can offer genuine hope – with the correct targeting, some of the brain damage might be reversible.”

The next step for the team is to test these findings in more complex biological systems, like cellular models, to see if these “claws” hold up under pressure.

“Many potential Alzheimer’s treatments fail due to an incomplete understanding of how amyloid-beta protein aggregation occurs,” she said. “By directly observing and quantifying these interactions, our work provides a roadmap for creating more effective therapies.”