The windows through which we view the world are made of amazing stuff. Human eyes are about 50 percent water and 50 percent protein, including remarkable proteins called crystallins.
Unlike most other proteins that make up our bodies, which break down and must be regenerated within hours or weeks, the crystallins in the lenses of our eyes last a lifetime. And when something goes wrong, the lenses can cloud over, forming cataracts that steal away our vision.
By employing sophisticated chemistry to manipulate biological material, UC Irvine researchers have pried out some of the secrets of cataract formation. One recent study revealed the precise structural effects of mutations in crystallin proteins, exposing them in stark molecular detail, that give rise to cataracts in children as young as six. It’s a discovery that could allow other scientists to develop treatments for the condition, targeting the mutation to halt the clumping of crystallin proteins that leads to cataract formation.
The tools of modern-day chemical biology include nuclear magnetic resonance spectroscopy and a kind of laboratory sleight-of-hand that allows the recruitment of bacteria to manufacture virtually any proteins the researchers require; they are now using them to investigate similar mutations that mimic the damage caused by age-related cataracts.