Scientists could be one step closer to a cure for Alzheimer’s after discovering how a key process that triggers the disease takes place.
The signature hallmark of the disease – the most common form of dementia – is the build-up of protein plaques in the brain.
Now, a team of researchers at Cambridge University, believe they have identified the mechanism by which these plaques accumulate.
But the real breakthrough is that they believe they can show it is possible to control this process – raising hopes of ultimately stopping it altogether.
Scientists at Cambridge University have discovered how to control the process by which key protein plaques build up in the brains of Alzheimer’s patients
The ability of biological molecules, such as our DNA, to replicate themselves is the foundation of life.
It is a process that usually involves complex cellular machinery.
However, certain protein structures manage to replicate without any additional assistance, such as the small, disease-causing protein fibers – fibrils – that are involved in neurodegenerative disorders, including Alzheimer’s and Parkinson’s.
The fibrils, known as amyloids, become intertwined and entangled with each other, causing the so-called ‘plaques’ that are found in the brains of Alzheimer’s patients.
Spontaneous formation of the first amyloid fibrils is very slow, and typically takes several decades.
Boys as well as girls WILL get the HPV vaccine, according to…
Miracle diets ‘NEVER work’: Fad weight loss plans only…
Are YOU a slave to OCD? Scientists identify receptor in the…
Could a NOSE SPRAY prevent chlamydia? World’s first vaccine…
This helps to explain why Alzheimer’s is usually a disease that affects people in their old age.
However, once the first fibrils are formed, they begin to replicate and spread much more rapidly by themselves, making the disease extremely challenging to control.
Despite its importance, the fundamental mechanism of how protein fibrils can self-replicate without any additional machinery, is not well understood.
The new findings, uncovered by the Cambridge team, were generated using a powerful combination of computer simulations and laboratory experiments to identify the necessary requirements for the self-replication of protein fibrils.
The researchers found that the seemingly complicated process of fibril self-replication is actually governed by a simple physical mechanism – the build-up of healthy proteins on the surface of existing fibrils.
The researchers used a molecule known as amyloid-beta, which forms the main component of the amyloid plaques found in the brains of Alzheimer’s patients.
The researchers believe they can show it is possible to control the process, which results in the formation of amyloid-beta plaques – raising hopes of ultimately stopping the disease in its tracks
They found a relationship between the amount of healthy proteins that are deposited on to the existing fibrils, and the rate of the fibril self-replication.
In other words, the greater the build-up of proteins on the fibril, the faster it self-replicates.
They were also able to show, as a proof of principle, that by changing how the healthy proteins interact with the surface of fibrils, it is possible to control the fibril self-replication.
Dr Andela Saric, the study’s first author, said: ‘One of the mysteries of amyloid plaque formation is how, after their long, slow formation, the speed of their progression becomes much faster.
‘We’ve identified the factors that in fact cause the system to catalyse its own activity, becoming a runaway process.
‘But this discovery suggests that if we’re able to control the build-up of healthy proteins on the fibrils, we might be able to limit the aggregation and spread of plaques.’
Dr Saric also argued that the findings could be of great interest in the field of nanotechnology.
‘One of the unfilled goals in nanotechnology is achieving efficient self-replication in manufacturing of nanomaterials.
‘This is exactly what we’ve observed happening with these fibrils – if we’re able to learn the design rules from this process, we may be able to achieve this goal.’
The findings are published in the journal Nature Physics.