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New discovery 'could halt Alzheimer's in early stages'

New discovery 'could halt Alzheimer's in early stages'
17th February 2015

Researchers have made a breakthrough in the fight against Alzheimer's that could stop the disease in its early stages.

Scientists at the University of Cambridge have identified a type of molecule that occurs naturally in humans and has the ability to break the cycle of events that scientists believe leads to the disease. 

Known as Brichos, the molecule sticks to threads made up of malfunctioning proteins, called amyloid fibrils, that characterise the disease.

This prevents the threads from coming into contact with one another, helping to avoid the formation of highly toxic clusters that enable the condition to proliferate in the brain. 

As this is one of the critical stages in the development of Alzheimer's, the researchers' discovery opens up the prospect of finding a substance that could eventually be used to treat the disease.

The condition develops in a number of stages, beginning with the misfolding of naturally occurring proteins. These then stick together - or nucleate - with other proteins to create thin filamentous structures called amyloid fibrils.

Following their initial formation from misfolded proteins, amyloid fibrils help other proteins that come into contact with them to misfold and form small clusters, called oligomers. Oligomers are thought to be responsible for the devastating effects of Alzheimer's, as they are highly toxic to nerve cells.

Known as secondary nucleation, the next stage of the condition kickstarts a chain reaction which creates many more toxic oligomers and ultimately amyloid fibrils.

If this did not occur, single molecules would have to misfold and form toxic clusters unaided - a much slower and far less devastating process. 

The researchers discovered that the Brichos molecule effectively inhibits secondary nucleation by acting as a 'molecular chaperone' by binding to catalytic sites on the surface of amyloid fibrils.

Tests conducted on mice revealed that, in the presence of the molecular chaperone, amyloid fibrils formed but the did not develop in the brain tissue, meaning it had suppressed the secondary nucleation process.

"A good tactic now is to search for other molecules that have this same highly targeted effect and to see if these can be used as the starting point for developing a future therapy," said Dr Samuel Cohen, a Research Fellow at St John's College, Cambridge, and a lead author of the report.

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