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SUMMARY:The self-assembly\, functionalization and cellular interactions of
  short amyloid fibril forming peptides - Sally Gras\, The University of Me
 lbourne
DTSTART:20160419T093000Z
DTEND:20160419T110000Z
UID:TALK65656@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:We are interested in the self-assembly of de novo designed or 
 naturally occurring peptide sequences into amyloid fibrils\; this includes
  variants of the TTR105-115 peptide and the chaplins from the bacteria Str
 eptomycetes coelicolor.  \n\nIn this talk I will describe how we have used
  synthetic DNA molecules\, known as DNA origami\, to nucleate and organize
  the growth of amyloid fibrils.  A 20-helix DNA nanotube was used to sheat
 he amyloid fibrils and to organize the fibrils onto predefined two-dimensi
 onal platforms via DNA–DNA hybridization interactions.  \n\nOther materi
 als have been created from a family of peptide variants based on the TTR10
 5-115 sequence and we are seeking to better understand how mammalian cells
  interact with these designed fibrils.  We have tracked the interactions o
 f these fibrils with cells and separated the effects of the topographic ph
 ysical and chemical structural features on cell behavior.  \n\nThe five ch
 aplin peptides produced by Streptomycetes coelicolor provide an interestin
 g contrast\, as these peptides are surface active and assemble both in sol
 ution and at the air-water interface.  We have found surprising difference
 s in the properties and assembly of the individual chaplin peptides that p
 otentially allow control of the self-assembly process.  Molecular dynamics
  simulations have also provided new insights into intermediate structures 
 that may determine the rates of assembly in these pathways. 
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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