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SUMMARY:The properties of nano-scale amyloid fibril fragments in vitro and
  in vivo - Dr  Wei-Feng Xue\, School of Biosciences\, University of Kent
DTSTART:20160525T093000Z
DTEND:20160525T103000Z
UID:TALK66317@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:What are the molecular mechanisms that govern the amyloid fibr
 ils’ potential to seed the formation of new amyloid to facilitate their 
 spreading\, and to damage cells in amyloid-associated diseases such as Alz
 heimer’s disease\, Parkinson’s disease\, type 2 diabetes\, and systemi
 c amyloidoses? These disease-associated properties of amyloid have been li
 nked to small nano-sized particles created through the fragmentation of am
 yloid fibrils\, which is a process governed by the stability of amyloid fi
 brils toward breakage. We have previously described an approach that is ca
 pable of resolving fibril fragmentation rates\, fibril particle concentrat
 ions\, and fibril length distributions\, through direct observations by at
 omic force microscopy image analysis. Applying our approach to several dif
 ferent amyloid model systems\, such as alpha-synuclein\, lysozyme\, and th
 e yeast prion protein Sup35NM\, we present an unique comparison of the sta
 bility of these different amyloid fibrils toward breakage. Using the yeast
  prion protein Sup35NM that forms amyloid particles capable of conferring 
 district yeast phenotypes in vivo\, we have also quantified the biological
  impact of fibril fragments in terms of their transmissive potential. Our 
 results allow new quantitative insights into key properties of amyloid agg
 regated in terms of their their destructive association to disease as well
  as the constructive potential they have for future functional amyloid mat
 erials development.\n\n\n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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