Primary open angle glaucoma (POAG) affects over 60 million people worldwide and is the second leading cause of blindness in the United States. Mutations primarily in the myocilin olfactomedin domain (myoc-OLF) account for 10% of juvenile-onset and 4% of adult-onset cases of POAG, causing a toxic gain of function that accelerates disease progression. In vitro and in cells, aggregates of mutant myocilin exhibit many signatures of amyloid, a particular templated aggregate structure associated with numerous toxic gain of function neurodegenerative diseases like Alzheimer disease and type-1 diabetes. Prior data using atomic force microscopy has shown at nanometer resolution that myoc-OLF fibrils adopt a distinct straight conformation. I will present our molecular characterization of these straight myoc-OLF amyloid fibrils, including toxicity toward neuronal cells, solution dynamics and fibril structure.

Molecular characterization of glaucoma-causing myocilin variants and corresonding aggregates

Macromolecular Chemistry: The Second Century

[Author Benefits](https://scimeetings.acs.org/?utm_source=pubs_content_marketing&utm_medium=website&utm_campaign=0320_MCF_NPI_Launch_Spring_Homepage&ref=pubs_content_marketing)

[How to use SciMeetings](https://storage.googleapis.com/dl.morressier.com/acs/SciMeetings-ACSSpring2020-HowToGuide_M3020-Final.pdf)

[Frequently Asked Questions](https://storage.googleapis.com/dl.morressier.com/acs/SciMtng_ACSNMSp2020_FAQ_M3120_Final.pdf)

ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.