Research: Amyloid recycling

28 July 2005

The components of amyloid fibrils, tangles of proteins seen in Alzheimer's disease and other conditions, are constantly being recycled.

Although initially thought to be exclusively disease-related structures, thread-like amyloid fibrils are now known to be adopted by a wide range of otherwise perfectly normal proteins. This suggests that the ability to form such structures is a common property of polypeptide chains. Indeed, it appears that some such structures even have normal biological functions.

In Cambridge, Chris Dobson and colleagues have looked at the behaviour of protein molecules within Amyloid fibrils. Unexpectedly, they discovered that the structures are constantly exchanging their individual components, with molecules recycling in and out of individual fibrils in an assembly. If generally true, this would have major implications for the design of therapeutics for amyloid fibril-based diseases – as sequestering of fibril components should lead to the gradual disappearance of the amyloid fibril.

External links

• Carulla N et al. Molecular recycling within amyloid fibrils. Nature 2005;436(7050):554–8.