London: Scientists have designed a new protein to understand the reason that leads to death of nerve cells in people suffering from Alzheimer's, an advance that can help cure the disease.
In those with Alzheimer's, Amyloid-beta (Abeta) proteins stick together to make amyloid fibrils which form clumps between neurons in the brain, researchers said.
It is believed the build-up of these clumps causes brain cells to die, leading to the cognitive decline in patients suffering from the disease, they said.
It is not known why this particular protein's "stickiness" causes cells to die and scientists have been unable to properly test whether the sticky clumps of Abeta proteins have different effects, compared with individual proteins that are not stuck together.
Now, scientists from University of Sussex in the UK have created a new protein which closely resembles the Abeta protein in size and shape, but contains two different amino acids (the building blocks that proteins are made up of).
These changes mean that the new protein does not form amyloid fibres or sticky clumps, and, unlike Abeta, is not toxic to nerve cells, researchers said.
The new protein will be an essential laboratory tool for those working to understand the causes and role of Abeta plays in Alzheimer's disease, they said.
"Understanding how the brain protein Abeta causes nerve cell death in Alzheimer's patients is key if we are to find a cure for this disease," said Karen Marshall from University of Sussex.
"Our study clearly shows that the aggregation of Abeta into bigger species is critical in its ability to kill cells. Stopping the protein aggregating in people with Alzheimer's could slow down the progression symptoms of the disease. We hope to work towards finding a strategy to do this in the lab and reverse the damaging effects of toxic Abeta," she said.
"This is a really exciting new tool that will contribute to research to uncover the causes for Alzheimer's disease and enable tangible progress to be made towards finding targets for therapy," added Louise Serpell from University of Sussex.