Researchers Reverse Alzheimer's-Linked Chemical Process

Oregon State University team observes how metals promote protein clumping, and how chelators can disrupt it

Published on Feb. 24, 2026

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Researchers at Oregon State University have uncovered real-time insights into a chemical process linked with Alzheimer's disease, using a molecule measuring technique to observe how certain metals can promote the protein clumping that leads to blocked neural pathways. The team also watched molecules known as chelators disrupt or reverse the clumping, providing valuable insights for designing better treatments.

Why it matters

Alzheimer's is the sixth-leading cause of death for people age 65 and older, affecting millions of families. This research offers hope that some of the brain damage caused by Alzheimer's may be reversible, by targeting the underlying chemical processes that lead to the disease.

The details

Led by Marilyn Rampersad Mackiewicz, associate professor of chemistry at OSU, the research team used fluorescence anisotropy to observe how different chelator molecules can selectively bind to metal ions believed to be a factor in Alzheimer's, disrupting the protein aggregations that block neural pathways. One chelator was shown to effectively 'snatch up' metal ions in a non-selective way, while another demonstrated a strong ability to selectively grasp the copper ions linked to Alzheimer's.

  • The research findings were published in February 2026 in the journal ACS Omega.

The players

Marilyn Rampersad Mackiewicz

An associate professor of chemistry in the OSU College of Science who led the research team.

Alyssa Schroeder

An undergraduate student at OSU who contributed to the research.

Eleanor Adams, Dane Frost, Erica Lopez, and Jennie Giacomini

Undergraduate students at Portland State University who contributed to the research.

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What they’re saying

“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. 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?'”

— Marilyn Rampersad Mackiewicz, Associate Professor of Chemistry, Oregon State University

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

— Marilyn Rampersad Mackiewicz, Associate Professor of Chemistry, Oregon State University

What’s next

The researchers say testing in more complex biological systems, including cellular and preclinical models, is the next step in their work.

The takeaway

This research offers valuable insights into the chemical processes underlying Alzheimer's disease, providing a potential path toward more effective treatments by targeting the root causes of the condition and potentially reversing some of the brain damage it causes.