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Polymers and Self Assembly: From Biology to Nanomaterials
Tuesday Speaker Abstracts
Exploiting Amyloid Fibrils as Functional Biomaterials
Louise Serpell
University of Sussex, Brighton, United Kingdom
Amyloid fibrils are known to be composed of a cross-ß structural core that is hydrogen bonded
along the length of the fibre to form a highly ordered and repetitive structure. It is clear however,
that side chains play an important role in driving self-assembly and strengthening the overall
structure via internal interactions between the ß-sheets as well as stacking within sheets. Our
work utilizes electron microscopy, X- ray fibre diffraction and biophysical and spectroscopic
techniques to examine the structure of amyloid fibrils.
Research into the self-assembly of short amyloidogenic peptides has provided a novel
architecture in the form of a cross-ß nanotube formed by an amphipathic peptide. Our work has
highlighted the important central role for the aromatic side chains phenylalanine and tyrosine in
the internal interactions within the amyloid protofilament. Most recently, we have shown
oxidation leads to covalent linking of the tyrosine side chains may play a very significant role in
the structure and stability of amyloid fibrils in diseases including Alzheimer’s disease. We have
also shown that charge interactions play an important role and recently investigated the
functionalization of amyloid fibrils using the lysine residues to promote sillconisation. This
presentation will focus on recent insights into the contribution of primary sequence to the
architecture of the amyloid fibrils and how these extremely stable structures may be further
exploited as templates for further functionalization.