Georgia Institute of Technology Georgia Institute of Technology

Research Horizons

Georgia Tech's Research Horizons Magazine

extreme closeup of a human eye


Using a novel high-throughput screening process, scientists have, for the first time, identified molecules with the potential to block the accumulation of a toxic eye protein that can lead to the early onset of glaucoma.

Glaucoma is a group of diseases that can damage the eye’s optic nerve to cause vision loss and blindness. Elevated eye pressure is the main risk factor for optic nerve damage.
Previous research in the field identified a mutant form of a protein called myocilin as a root cause of this increased eye pressure in some patients. Mutant myocilin is toxic to the cells in the part of the eye that regulates pressure. These genetically inherited mutants of myocilin clump together in the front of the eye, preventing proper fluid discharge from the eye, which then raises eye pressure. This cascade of events can lead to early onset glaucoma, which affects several million people before age 35.

To find molecules that bind to mutant myocilin and block its aggregation, researchers designed a simple, high-throughput assay and then screened a library of compounds. They identified two molecules with potential to treat early onset glaucoma.

“These are really the first specific drug targets to treat glaucoma,” said Raquel Lieberman, an associate professor in the Georgia Tech School of Chemistry and Biochemistry. Lieberman presented her findings at the Society for Laboratory Automation and Screening Conference in San Diego, California, and published them in the journal ACS Chemical Biology earlier this year.

The National Institutes of Health and the Pew Scholars Program in the Biomedical Sciences provided support for the research. The work was a collaboration involving Georgia Tech, Emory University, and the University of South Florida.

At the heart of the study was an assay created to take advantage of the fundamental principles of ligand binding.

Raquel Lieberman

Raquel Lieberman is an associate professor in the School of Chemistry and Biochemistry, where she studies the structure and dysfunction of proteins implicated in misfolding disorders.

Related Stories

Read More
Read More
Read More

Media Contacts

John Toon

John Toon

Director of Research News
Phone: 404.894.6986

Anne Wainscott-Sargent

Research News
Phone: 404-435-5784

Subscribe & Connect

Follow Us on Twitter:


RSS Feeds

Subscribe to our RSS Feeds with your favorite reader.

Email Newsletter

Sign up to receive our monthly email newsletter.

Research Horizons Magazine

Sign up for a free subscription to Research Horizons magazine.