Researchers have published a list of proteins most linked to aging and age-related disease. They have found that short and highly charged proteins are most vulnerable to vast damage. It just takes one oxidation within these proteins to weaken its natural, balled-up form.
A team of researchers has explained how oxidative damage, which is part of aging cell's natural process, affects proteins. By the age of 80, oxidation has already damaged almost half of the body's proteins.
The team was led by senior study author Ken A. Dill, Ph.D., who is also the Center's Physical and Quantitative Biology director and a Chemistry and Physics Distinguished professor. The researchers have utilized computer analysis and physics principles to study protein charges.
"Our paper explains the molecular mechanism by which natural chemical processes of aging affect our proteins," says Dill whose method can predict which proteins are most vulnerable to unfolding when they are damaged.
The list of 20 proteins most at risk for oxidative unfolding includes DNA-binding histones proteins, which play a role in cancer development and memory loss; and telomerase proteins, which are involved in the cell's aging process and cancer advancement due to telomeres extending.
According to Dill, the process can provide scientists with a better foundation in analyzing how oxidation weakens the proteins of aging cells. Moreover, the team will also look for more proteins that could be playing vital roles in the development of age-related diseases and aging using the new method.
The researchers believe that the method can lead to the discovery of more proteins that are currently not suspected to be vulnerable to high oxidation and instability or linked to age-related disease.
The findings can also help the medical and scientific communities get a deeper understanding of age-related diseases and lead the way towards the development of better, targeted treatments.
The study was published online in the journal Structure and titled "Highly charged proteins: the Achilles' heel of aging proteoms."