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New therapy targets for amyloid disease
Date:12/4/2009

f sixty or so."

The study was funded by the Wellcome Trust and the Biotechnology and Biological Sciences Research Council (BBSRC), supporting a team that included both cell biologists and biophysicists.

The next stage of this work is to look at a greater number of proteins that form amyloid fibres in order to consolidate these findings, says co-author and cell biologist Dr Eric Hewitt. "What we've discovered is fundamental and offers a whole new area for those working on therapeutics in this area. We anticipate that when we look at amyloid fibres formed from other proteins, they may well follow the same rules."

The team also hopes to discover why the shorter amyloid fibres are more toxic that their longer counterparts.

"It may be that because they're smaller it's easier for them to infiltrate cells," says Dr Hewitt. "We've observed them killing cells, but we're not sure yet exactly how they do it. Nor do we know whether these short fibres form naturally when amyloid fibres assemble or whether some molecular process makes them disassemble or fragment into shorter fibres.These are our next big challenges."


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Contact: Clare Elsley
clare@campuspr.co.uk
44-113-258-9880
University of Leeds
Source:Eurekalert  

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