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SUMMARY:Some Optical Properties of Fluorescently Modified Amyloid Fibrils 
 - Kevin Channon
DTSTART:20060510T120000Z
DTEND:20060510T130000Z
UID:TALK4895@talks.cam.ac.uk
CONTACT:vh233
DESCRIPTION:Amyloid plaques\, as found in the organs of individuals suffer
 ing from a number of degenerative diseases\, are found mainly to constitut
 e fibrous protein aggregates.  These aggregates may be made in vitro from 
 almost any protein\, or poly-peptide  not limited to the disease-causing o
 nes.  The structure formed is very stable and resistant to relatively hars
 h conditions.\n\nIn this study we aim to investigate the following key poi
 nts: -\n\nWhat is the plasticity of the amyloid structure to chemical modi
 fication with small molecules?\n\nWhat are the effects of incorporating sm
 all molecules into the fibrils? Both on the fibril structure and the label
  molecule.\n\nIs any ordering induced in the arrangement of the label mole
 cules upon fibrilisation?\n\nIs there any delocalisation of excitons over 
 a number of dye molecules?\n\nCan we make macromolecular equivalents of di
 -block co-polymers that display features such as exciton migration and tra
 pping or semi-conducting effects?\n\nNumerous spectroscopic techniques are
  employed\, including steady-state and time-resolve fluorescence methods a
 nd circular dichroism\, FTIR and raman spectroscopy.  A number of microsco
 pic techniques are also used\, such as AFM\, SNOM and confocal microscopy.
 \n\nThis work shows that additional groups\, with interesting properties\,
  can be successfully incorporated into the amyloid structure.  Using appro
 priate groups could lead to some useful and novel nano-materials.\n
LOCATION:Edwards Room\, Bragg Building\, Cavendish Laboratory\, Department
  of Physics
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