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SUMMARY:Novel insights into the molecular mechanism of α-synuclein amyloi
 d formation - The effects of intrinsic and extrinsic factors - Dr Celine G
 alvagnion\, University of Cambridge
DTSTART:20160316T103000Z
DTEND:20160316T113000Z
UID:TALK65103@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:The conversion of soluble monomeric α-synuclein into amyloid 
 fibrils is the hallmark of a range of neurological disorders\, including P
 arkinson’s disease. Unlike other amyloidogenic proteins\, such as Abeta 
 peptide\, involved in Alzheimer’s disease\, α-synuclein is surprisingly
  stable in solution under quiescent conditions and its aggregation is main
 ly triggered via interaction with surfaces including air/water interface\,
  surfactants\, lipid membranes. In fact\, we have recently shown that nega
 tively charged lipid vesicles can trigger the aggregation of α-synuclein 
 by enhancing the rate of primary nucleation by up to 3 orders of magnitude
 . In addition\, our results indicate that both the protein:lipid ratio and
  the chemical properties of the lipids play a role in modulating the kinet
 ics of α-synuclein lipid-induced aggregation.\nMoreover\, the rate of an 
 other surface-induced fibril production process\, the auto-catalytic fibri
 l amplification\, was shown to be highly sensitive to the solution conditi
 ons and to increase by at least 4 orders of magnitude at acidic pHs.\nIn l
 ight of these findings\, we have developed and applied a series of quiesce
 nt experimental protocols to study the effects of intrinsic (disease assoc
 iated mutations) and extrinsic (homologous proteins and small molecules) f
 actors on the individual microscopic steps of α-synuclein aggregation inc
 luding\, the de novo formation of fibrils\, their elongation and their amp
 lification. We find that surface-induced fibril production processes are s
 trongly influenced by these factors.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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