The length of amyloid fibrils found in diseases such as
Alzheimer and Parkinson appears to play a role in the degree of
their toxicity, according to researchers at the University of
Leeds. Their findings are published in The Journal of Biological
Chemistry in a paper titled “Fibril Fragmentation Enhances
Amyloid Cytotoxicity.” Sheena Radford, Ph.D., and colleagues
systematically analyzed the effects of fragmentation on three of
the 30 or so proteins that form amyloid in human diseases. Their
results showed that in addition to the expected relationship
between fragmentation and the ability to seed, the length of
fibrils also correlated with their ability to disrupt membranes
and reduce cell viability. This was evident even when there were
no other changes in molecular architecture. Co-author, Eric
Hewitt, Ph.D., says that while the findings provide scientists
with unexpected new insights for the development of therapeutics
against amyloid deposit-related diseases, the next stage of
research will involve lookin