UC Irvine Chemists Uncover Cataract Causes in Aging

Research reveals how a subtle chemical change in an eye lens protein can lead to cataract formation over time.

Published on Mar. 5, 2026

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Researchers at the University of California, Irvine have uncovered how a small chemical change in an eye lens protein can make the protein more likely to clump together over time, suggesting an early step in cataract formation. The team used a tool called genetic code expansion to recreate a specific type of oxidative damage that naturally occurs in the aging eye, and found that even with this minor modification, the protein became much more prone to aggregation when stressed.

Why it matters

Cataracts are a leading cause of blindness worldwide, and understanding the molecular mechanisms behind age-related cataracts is crucial for developing new treatments or preventative measures. This research provides insights into how gradual, subtle changes in eye lens proteins can contribute to cataract development, which could lead to non-surgical interventions or improved artificial lenses in the future.

The details

The study, published in Biophysical Reports, focused on proteins called crystallins that help keep the eye lens clear. Unlike most cells in the body, the lens cannot replace damaged proteins, so chemical changes can accumulate over decades. The researchers used a tool called genetic code expansion to recreate a specific type of oxidative damage that naturally occurs in aging eyes. They found that even with this small modification, the protein remained folded and stable, but became much more likely to clump together when stressed by heat.

  • The research was published on March 4, 2026.
  • The study was conducted by researchers at the University of California, Irvine.

The players

Yeonseong (Catherine) Seo

A UC Irvine Ph.D. candidate in chemistry and the lead author of the study.

Rachel Martin

A UC Irvine professor of chemistry and the corresponding author on the study.

University of California, Irvine

A member of the prestigious Association of American Universities and ranked among the nation's top 10 public universities.

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What they’re saying

“What surprised us is that the protein can still look mostly normal, but even a small chemical change makes it much more likely to stick to other proteins. Over time, those small interactions can add up and cloud the lens.”

— Yeonseong (Catherine) Seo, UC Irvine Ph.D. candidate in chemistry (Mirage News)

“The protein doesn't fall apart right away. It just becomes a little more likely to interact with its neighbors, and over time that can lead to clumping.”

— Yeonseong (Catherine) Seo, UC Irvine Ph.D. candidate in chemistry (Mirage News)

“Almost everyone who lives long enough will get age-related cataracts. GCE enables us to study specific changes that happen with proteins in the aging lens, furthering our understanding of what causes cataracts at the molecular level. Understanding the loss of function that comes with aging could lead to non-surgical treatments or improved artificial lenses in the future.”

— Rachel Martin, UC Irvine professor of chemistry (Mirage News)

What’s next

The researchers are now investigating why the oxidative change makes the protein more prone to clumping by studying how it affects the natural movement and dynamics of the lens proteins.

The takeaway

This research provides important insights into the molecular mechanisms behind age-related cataracts, a leading cause of blindness worldwide. By understanding how subtle chemical changes in eye lens proteins can contribute to cataract formation, scientists are one step closer to developing non-surgical treatments or improved artificial lenses to address this common vision problem.