The Crystal Maze
Uncovering the complex biochemistry behind cataract formation
Eugene Serebryany, Phoebe Harkin | | Longer Read
Crystallins are the collection of structural proteins found in the lens of the eye that help to focus light onto the retina. We know that over our lifetimes they can accumulate damage, losing their native structure and sticking together to form aggregates – one of several mechanisms that causes cataracts. But how exactly does this happen – and can it be stopped? Eugene Serebryany, a Post-Doctoral Fellow at the Department of Chemistry and Chemical Biology at Harvard University, USA, wants to find out.
In 2015, Serebryany and his Harvard-MIT team made the crucial discovery that wild-type (undamaged) crystallin promoted aggregation of mutant (damaged) versions – without itself aggregating (1). Chemical bonds between sulfur atoms within the protein (disulfide bonds) were found to play a role in aggregation (2). Most recently, the team found that crystallin protein molecules engaged in oxidation–reduction reactions with one another – disproving the long-held assumption that crystallins are inert (3).
We spoke to Serebryany to find out more about the role of crystallins in cataract formation.
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