Your body runs on the food you eat and the protein it gets. However, what really break these proteins down are the amino acids your body synthesises. Known as the building blocks of proteins, these amino acids are also needed for vital processes like the synthesis of hormones and neurotransmitters.
One of these essential amino acids is Asparagine, known for its key role in the biosynthesis of glycoproteins. The human nervous system also needs this amino acid to be able to maintain equilibrium. However, with time, this amino acid will eventually degrade, says chemistry and chemical biology associate professor Sunny Zhou at Northeastern University. “The phenomenon has come to be accepted as yet another part of aging: our hair turns gray, our joints begin to ache, and our asparagine turns into isoaspartic acid,” says Zhou.
Zhou is working on research that studies the etiologic role of isoaspartic acid or isoAsp, in aging and disease. It’s research that could dramatically change how doctors treat diseases such as Alzheimer’s, which significantly elevates patients’ isoAsp levels. “The rate at which isoAsp form depends on the sequence of amino acids contained in the protein. If asparagine sits next to the amino acid proline, it will take a long time to degrade. If it’s next to glycine, on the other hand, it may take just half a day. Luckily, there’s an antidote. The enzyme ‘protein isoaspartate methyl transferase’ or PIMT, can rectify the damage,” he explains.
“Degradation cannot be prevented,” he said, “because it happens spontaneously. However, if researchers found a way to repair the damage, their work could have a significant effect on the ability to treat age-related diseases such as Alzheimer’s.”
“If we can find the machinery that gets rid of isoaspartic faster, then we can somehow use a driver to boost that machinery,” Zhou said, noting that the damaged cells in an Alzheimer’s brain contain up 70 percent isoaspartic acid. “That’s the hope.”
Anisha Naidu