- Researchers at the National Institutes of Health have identified how the neurological conditions develop differently between patients
- The finding could revolutionise medical treatment and even lead to new drugs
- About 850,000 people are living with Alzheimer’s in the UK, a figure expected to to rise to a million by 2025
The treatment of Alzheimer’s Disease could be revolutionised after a breakthrough discovery by US scientists.
Researchers at Maryland’s National Institutes of Health have identified how the neurological condition develops differently between patients – a move which offers fresh scope for better, more-targeted drugs.
The findings, published in medical journal Nature on Wednesday, shed fresh light on the toxic chemicals behind dementia and offers renewed hope of a remedy.
One of the main causes of dementia is the clumping together of a protein known as amyloid beta.
It has been suggested different formations of these fine fibres, or fibrils, may be linked with different forms of Alzheimer’s.
So the researchers, lead by Dr Robert Tycko, analysed 37 brain tissue samples from 18 individuals who had died from either typical Alzheimer’s or two unusual subtypes of the disease.
National concern: About 850,000 people are living with Alzheimer’s in the UK, a figure expected to to rise to a million by 2025
The study supports the theory different clinical subtypes of Alzheimer’s may be defined by different amyloid-beta fibril structures.
‘Aggregation of amyloid beta peptides into fibrils or other self assembled states is central to the patho genesis of Alzheimer’s disease,’ Tyco said.
‘We compared two atypical Alzheimer’s disease clinical subtypes – the rapidly progressive form (r-AD) and the posterior cortical atrophy variant (PCA-AD) – with a typical prolonged duration form (t-AD).
‘We find a single fibril structure is most abundant in samples from patients with t-AD and PCA-AD, whereas fibrils from r-AD samples exhibit a significantly greater proportion of additional structures.
‘These results demonstrate the existence of a specific predominant fibril structure in t-AD and PCA-AD, suggest that r-AD may relate to additional fibril structures and indicate that there is a qualitative difference between aggregates in the brain tissue of patients with Alzheimer’s disease.’