Scientists are investigation a new method of counteracting the death of nerve cells in Alzheimer’s disease.
A team led by Professor Bernd Reif of the Technical University of Munich, Germany, has been taking a close look at beta amyloids.
To prevent these proteins from clumping together, the scientists used small heat shock proteins – a family of proteins that cells make when exposed to stressful conditions. These heat shock proteins were shown in tests to attach to the deformed proteins and help them to restore their proper form.
They used a procedure called solid-state nuclear magnetic resonance spectroscopy to identify sites in heat shock proteins called alpha-B-crystallin that attach to the beta-amyloid. Alpha-B-crystallin exists in various different forms that are permanently being swapped, they say.
"In addition, it has a large molecular weight," says Professor Reif. "These factors make structure analysis very difficult."
Despite a lack of clarity in role these proteins play in neurodegenerative diseases, they are already being considered as agents in new medications.
This represents a "new field of application for this versatile helper", the team say. Small heat shock proteins are a promising new approach that can be deployed in the treatment of neurodegenerative diseases, they believe.
The team plan to carry out further research on a region of alpha-B-crystallin that binds protein types that, unlike the beta-amyloid, clump together in an unordered manner. Their work was published on Monday (12 October) in the journal Nature Structural Molecular Biology.
Mainz, A. et al. The Chaperone alpha B-Crystallin Deploys Different Interfaces to Capture an Amorphous and an Amyloid Client. Nature Structural Molecular Biology 12 October 2015 doi: 10.1038/nsmb.3108
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