A Natural Chemical Found in Yeast Could be the Key to Eliminating Alzheimer’s Disease.
Watching your friends or loved ones suffer from Alzheimer’s disease is painful to watch. Alzheimer’s disease goes beyond forgetfulness and is difficult to comprehend. But scientists have been studying Alzheimer’s disease for years and found a natural compound in yeast that could possibly be used in a drug to cure it.
Culprit Behind Alzheimer’s
The culprit behind Alzheimer’s disease is a tangle of proteins found in the brain. These proteins fold and clump themselves into plaques and tangles (Amyloid and Tau) in the brain, which trigger memory loss, confusion, and damage to neurons in the brain.
Scientists have been trying to understand what can untangle the plaques and knotted masses in Alzheimer’s-infected brains. One possible solution is a chemical compound naturally found in yeast.
James Shorter, Pd.D and biochemist professor from the Perleman School of Medicine, was working with the yeast molecule Hsp104 (heat shock protein 104) to see if it could kill the proteins that folded into the wrong shapes.
Hsp104 is the Answer
Shorter wanted to know if Hsp104 could be used as a drug to dismantle proteins clumps. In the past, Shorter’s lab observed the natural version of Hsp104 go after neurodegenerative proteins such as alpha-synuclein.
The lab observed how the yeast chemical pulls out the tangles of brain strands, one protein at a time. Shorter and his colleagues have high-resolution images of Hsp104 at work as it kills mangled clumps of protein.
"This superb collaboration has yielded the highest resolution picture of Hsp104 caught in the act of processing a protein,” Shorter said.
"We can now see the moving parts of the Hsp104 complex and how we might tune it to optimally attack neurodegenerative disease proteins."
How Hsp104 Fights Alzheimer’s
Hsp104 “processes” proteins by pulling it in through a central channel.
Because Shorter and his team were able to catch high resolution photos of Hsp104, there is a possibility that this compound in yeast can be introduced as a drug to dismantle clumps of protein that cause Alzheimer’s and other similar diseases.
Hsp104 is made up of six subunits that break down toxic proteins with water. As Hsp104 climbs up the strand, it pulls out the mangled proteins from the aggregate. After its released, the protein will either refold or degrade.
Shorter and his lab want to reprogram Hsp104 to enhance its ability to better pull the toxic proteins from the brain.
"The study helps us to understand how cells can break apart toxic protein aggregates to restore protein function, Shorter said.”
"Finally having a clear picture of this remarkable nanomachine will empower our designs for therapeutic versions that work in humans."