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SUMMARY:The Evolution of Amyloid Fibrils from Pathological to Functional M
 aterials - Raffaele Mezzenga\, ETH Zurich\, Switzerland
DTSTART:20170208T103000Z
DTEND:20170208T113000Z
UID:TALK70992@talks.cam.ac.uk
CONTACT:Francesco Simone Ruggeri
DESCRIPTION:Amyloid protein fibrils were originally known for their implic
 ation in several aberrant neurodegenerative pathologies. Today we know tha
 t amyloid fibrils can be produced in-vitro from a much broader range of pr
 oteins\, including non-toxic\, food-grade proteins. The resulting protein 
 fibrils possess unique chemical\, structural and colloidal properties whic
 h make them of possible use in an extraordinary vast context of applicatio
 ns. Their stiffness combined with their chiral\, polar and charged nature\
 , provides these systems with some unique physical behavior. In this talk 
 I will discuss our current understanding on the mesoscopic properties of a
 myloid fibrils at the single molecule level\, the implication of their sem
 iflexible nature on their liquid crystalline properties\, and I will illus
 trate how this information prove useful in understanding their collective 
 behavior in bulk and when adsorbed at liquid interfaces. By the careful ex
 ploitation of the physical properties of amyloid fibrils\, the design of a
 dvanced materials with unprecedented physical properties become possible\,
  and I will give a few examples on how these systems can ideally suit the 
 design not only of complex food systems\, but also of biosensors\, biomate
 rials\, cellular scaffolds\, catalytic and water purification membranes\, 
 making them promising candidates for building blocks in advanced materials
  and emerging nanotechnologies.
LOCATION:Unilever Lecture Theatre\,  Department of Chemistry
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