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There have been impressive new findings in the field of research in cataracts from the UC Irvine's chemistry team. Researchers have endeavored to learn more about the molecular structure of the eye when something goes wrong leading to formation of cataracts. As cataracts affect more than twenty million people worldwide the findings bring a hope that effective treatments and highly sophisticated new drugs can be developed to combat the disease.
Our eyes focus thanks to three different crystallin proteins in each lens.The proteins maintain transparency via both repelling and attracting light. Two of the forms of crystallin are structural, the third however is named a chaperone as it's role is to prevent the others from clumping into cataracts if they become mutated by chemical or ultraviolet light damage.
The researchers investigations discovered that these chaperone proteins form a far stronger bond to any mutated proteins in an attempt to keep the lens clear. The difficulty is this; the human eye does not have an infinite number of helpful proteins, so once they are all used up, those that have become weakened begin to bind and thereby form a cataract.
Now that this mechanism has been mapped at a molecular level, the team is hopeful that organic chemists can create sight-saving treatments to prevent such aggregation.