GETTY - STOCK IMAGE Drug that rids the brain of the rogue protein that causes Alzheimer's could be on the horizon

The key is a chemical found naturally in yeast that breaks up tangles of proteins behind the illness, as well as other devastating neurological conditions. Scientists believe it can help them develop treatments that "optimally attack neurodegenerative disease proteins." They have filmed it dissolving the misfolded proteins that clump together and trigger memory loss, confusion and a host of other symptoms. The researchers are hopeful of turning their findings into an effective therapy for dementia, Parkinson's disease and motor neurone disease.

This superb collaboration has yielded the highest resolution picture of Hsp104 caught in the act of processing a protein James Shorter - Biochemist Professor

Biochemist Professor James Shorter and colleagues have been working with the yeast molecule Hsp104 (heat shock protein 104), which they call a 'nanomachine' for a decade. Now, for the first time, they have high-resolution images of its mechanism as it kills proteins that have folded into the wrong shape, leading to Alzheimer's and Parkinson's. Professor Shorter, of the Universty of Pennsylvania, said: "This superb collaboration has yielded the highest resolution picture of Hsp104 caught in the act of processing a protein. "We can now see the moving parts of the Hsp104 complex and how we might tune it to optimally attack neurodegenerative disease proteins."

GETTY - STOCK IMAGE Scientists believe it can help them develop treatments

Misfolded proteins are the culprits behind a form of motor neurone disease called ALS (amyotrophic lateral sclerosis), Alzheimer's, Parkinson's and other brain disorders. When these proteins become distorted they are unable to perform their normal functions, causing devastating problems for neurons. Currently, there is no way to untangle the knotted mass of these proteins to treat disease. Now the video of Hsp104 provides Professor Shorter with fresh insight into how they may be able to dismantle the harmful protein clumps.

His lab team used cutting edge freezing technology called cryo-EM (electron microscopy) to produce the clearest images to date of the yeast chemical's structure as it eliminated mutated proteins. Hsp104 pulls in proteins it "processes" through a central channel, but scientists had not seen this at high resolution before the pioneering study, published in Science. Co author Dr JiaBei Lin, a postdoctoral fellow in Professor Shorter's lab, said: "With this more-in-focus view, we can see parts of its structure we want to engineer to make better on target therapeutics for neurodegenerative diseases." Normally, Hsp104 is a "disaggregase" enyzme, which dissolves previously aggregated proteins and helps them acquire the correct shape.

GETTY - STOCK IMAGE The researchers are hopeful of turning their findings into an effective therapy

Although Hsp104 is found in most organisms on the planet, there is nothing similar in humans or animals. So Professor Shorter wondered whether it could be introduced as a drug to dismantle the protein clumps that characterise Alzheimer's and other diseases. In previous studies, his lab established the natural version of Hsp104 is active against neurodegenerative proteins such as alpha-synuclein. The yeast chemical pulls out one protein at a time from the tangles of minute brain strands, called fibrils.

Signs and symptoms of Alzheimer's Tue, August 23, 2016 There are more than 520,000 people in the UK with Alzheimer's disease. Here are 10 early signs and symptoms including memory loss and problem-solving to look out for. Play slideshow Getty Images 1 of 10 Changes in mood and personality - If you notice a loved one become easily upset, confused, depressed or anxious they could be suffering from Alzheimer's so talk to them and book an appointment with the doctor

The six tiny subunits of Hsp104 break down the toxic proteins with water as they climb up the strand, ultimately pulling them out of the aggregate. Once released, the protein can refold, or be degraded. The team has already made some tweaks to Hsp104 by mutating specific residues to enhance its activity. Working to break up disease clumps, the reprogrammed Hsp104 pulls these proteins apart better. Professor Daniel Southworth, of the University of Michigan, said: "It appears to pull substrates through stepwise, like a ratchet.

GETTY - STOCK IMAGE In the UK there are 850,000 people living with dementia