Irvine, Calif., March 4, 2026 — Cataracts, a leading cause of blindness globally, have long puzzled scientists and healthcare professionals. Researchers at the University of California, Irvine have made a significant breakthrough by identifying how a subtle chemical change in an eye lens protein can lead to cataract formation. This discovery, detailed in the latest issue of Biophysical Reports, sheds light on the early stages of the disease, potentially paving the way for new preventative treatments.
The study focuses on crystallins, proteins crucial for maintaining the clarity of the eye lens. Unlike most cells in the body, the lens cannot regenerate damaged proteins, making it susceptible to chemical changes that accumulate over time. “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,” explained Yeonseong (Catherine) Seo, a UC Irvine Ph.D. candidate and lead author of the study. “Over time, those small interactions can add up and cloud the lens.”
Understanding Age-Related Cataracts
Age-related cataracts, the most common form of the disease, typically develop due to environmental factors rather than genetics. Ultraviolet light from the sun, for instance, creates chemical stress in the eye, damaging crystallin proteins. To explore how this damage impacts the lens, the researchers employed a technique known as genetic code expansion (GCE), which allows for the precise modification of proteins.
Seo and her team utilized GCE to replicate a specific chemical change that occurs naturally in aging eyes. “GCE lets us make very precise changes to a protein,” Seo noted. “We used it to copy one kind of damage that shows up in age-related cataracts and see exactly what it does.”
The Role of Oxidation in Protein Clumping
By introducing a minor oxidative change to γS-crystallin, a lens protein, the researchers observed that while the protein remained stable, it was more prone to clumping under stress. “The protein doesn’t fall apart right away,” Seo explained. “It just becomes a little more likely to interact with its neighbors, and over time that can lead to clumping.”
Seo’s team is now investigating how oxidation affects the natural movement of these proteins. “We’re essentially watching how the protein breathes,” said Seo. “If certain parts start moving more than they should, it can briefly open up areas that are normally protected.” This insight could be crucial in understanding how the eye’s defenses against protein clumping weaken with age.
Implications for Future Treatments
The implications of this research are profound. “Almost everyone who lives long enough will get age-related cataracts,” stated Rachel Martin, UC Irvine professor of chemistry and corresponding author of the study. “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,” Martin added.
Key collaborators on this project include UC Irvine alumni Zane Long, Tsoler Demerdjian, Acts Avenido, and UC Irvine Professor Carter T. Butts. The experimental work was conducted in the lab of Rachel W. Martin, with funding from the National Institutes of Health.
About UC Irvine
Founded in 1965, UC Irvine is a member of the prestigious Association of American Universities and is consistently ranked among the nation’s top public universities. The institution is renowned for its academic excellence, innovative research, and vibrant campus life. Located in one of the world’s safest and most economically dynamic communities, UC Irvine contributes significantly to the local and state economy.
For more information about UC Irvine and its groundbreaking research, visit www.uci.edu. Media can access additional resources and interview opportunities through the university’s media relations department.
